|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
1-1137 |
0e+00 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 2290.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1 MADGRSSASVVAVDPEKAARERDEAARALLRDS----PLQTHLQYMTNGLELTVPFTLKV-VAEAVAFSRAKEVADEVLR 75
Cdd:PTZ00306 14 MADGRTSASVVVVDPEKAAKERDRAARALLQDNfpelHVNQRAQLLYKGLEHTVPYTLKVvVAGPVARQDADAVAKEVLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 76 SAWHLADTVLNNFNPNSEISMIGRLPVGQKHTMSATLKSVITCCQHVFNSSRGVFDPATGPIIEALRAKVAEKASVSDEQ 155
Cdd:PTZ00306 94 SAFQMVDTHLNSFNPNSEVSRVNRMPVGEKHQMSAHLKRVMACCQRVYNSSGGCFDPAAGPLVHELREAARRQKSVEAEF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 156 M-EKLFRVCNFSSSFIVDLEMGTIARKHEDARFDLGGVSKGYIVDYVVERLNAAGIVDVYFEWGGDCRASGTNARRTPWM 234
Cdd:PTZ00306 174 ViEELAGRFTLTNSFAIDLEEGTIARKHEDAMLDLGGVNKGYTVDYVVDRLNAAGFDDVLFEWGGDCRASGVNVQRQPWA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 235 VGIIRPPSLEQLR--------NPPKDPSYIRVLPLNDEALCTSGDYENLTEGSNKKLYTSIFDWKKRSLLEPVESELAQV 306
Cdd:PTZ00306 254 VGIVRPPSVDEVRaaaksgksAPPDHKSLLRVMSLNNEALCTSGDYENVLEGPASKVYSSTFDWKRRSLLEPTESELAQV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 307 SIRCYSAMYADALATASLIKRDIKKVRQMLEDWRHVRNRVTNYVTYTRQGERVARMFEIATDNAEIRKKRIAGSLPARVI 386
Cdd:PTZ00306 334 SVKCYSCMYADALATASLVKRDPVKVRYMLENWRYVRNRVTDYTTYTREGERVAHMFEIATEDAEMRKKRIAGSLPARVI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 387 VVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGINGWGTRAQAEQDVYDSGKYFERDTHKSGLGGSTDPGLV 466
Cdd:PTZ00306 414 VVGGGLAGCSAAIEAASCGAQVILLEKEAKLGGNSAKATSGINGWGTRAQAKQDVLDGGKFFERDTHLSGKGGHCDPGLV 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 467 RTLSVKSGDAISWLSSLGVPLTVLSQLGGHSRKRTHRAPDKADGTPVPIGFTIMQTLEQHVRTKLADRVTIMENTTVTSL 546
Cdd:PTZ00306 494 KTLSVKSADAISWLSSLGVPLTVLSQLGGASRKRCHRAPDKKDGTPVPIGFTIMRTLEDHIRTKLSGRVTIMTETTVTSL 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 547 LSKSRVRHDGAKQVRVYGVEVLQD---EGVVSRILADAVILATGGFSNDKTPNSLLQEFAPQLSGFPTTNGPWATGDGVK 623
Cdd:PTZ00306 574 LSESSARPDGVREIRVTGVRYKQAsdaSGQVMDLLADAVILATGGFSNDHTPNSLLREYAPQLSGFPTTNGPWATGDGVK 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 624 LARELGVKLVDMDKVQLHPTGLIDPKDPANPTKYLGPEALRGSGGVLLNKKGERFVNELDLRSVVSNAIIEQGDEYPDAG 703
Cdd:PTZ00306 654 LARKLGATLVDMDKVQLHPTGLIDPKDPSNRTKYLGPEALRGSGGVLLNKNGERFVNELDLRSVVSQAIIAQGNEYPGSG 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 704 GSKFAFCVLNDAAVKLFGVNSHGFYWKRLGLFVKADTVEKLAALIGCPVENVRNTLGDYEQLSKENRQCPKTRKVVYPCV 783
Cdd:PTZ00306 734 GSKFAYCVLNEAAAKLFGKNSLGFYWKRLGLFQRVDDVKGLAKLIGCPVENLHRTLETYERLSTKKVACPLTGKVVFPCV 813
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 784 VGPQGPFYVAFVTPSIHYTMGGCLISPSAEMQLEENTTSPFGHRRPIFGLFGAGEVTGGVHGGNRLGGNSLLECVVFGRI 863
Cdd:PTZ00306 814 VGTQGPYYVAFVTPSIHYTMGGCLISPSAEMQMEDNSVNIFEDRRPILGLFGAGEVTGGVHGGNRLGGNSLLECVVFGKI 893
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 864 AGDRAATILQKKPVPLSFKTWTTVILREVREGGMYGTGSRVLRFNLPGALQRSGLQLGQFIAIRGEWDGQQLIGYYSPIT 943
Cdd:PTZ00306 894 AGDRAATILQKKKYGLSKDKWTTVVVREVREGGQFGTGSRVLRFNLPGALQRSGLTLGQFIAIRGDWDGQQLIGYYSPIT 973
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 944 LPDDLGVIGILARSDKGTLKEWISALEPGDAVEMKGCGGLVIERRFSERYLYFSGHALKKLCLIAGGTGVAPMLQIIRAA 1023
Cdd:PTZ00306 974 LPDDLGVISILARGDKGTLKEWISALRPGDSVEMKACGGLRIERRPADKQFVFRGHVIRKLALIAGGTGVAPMLQIIRAA 1053
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1024 LKKPFLENIESIRLIYAAEDVSELTYRELLEHHQRDSKGKFRSIFVLNRPPPIWTDGVGFIDKKLLSSSVQPPAKDLLVA 1103
Cdd:PTZ00306 1054 LKKPYVDSIESIRLIYAAEDVSELTYRELLESYRKENPGKFKCHFVLNNPPEGWTDGVGFVDRALLQSALQPPSKDLLVA 1133
|
1130 1140 1150
....*....|....*....|....*....|....
gi 71400421 1104 ICGPPIMQRVVKTCLKSLGYDMQLVRTVDEVETQ 1137
Cdd:PTZ00306 1134 ICGPPVMQRAVKADLLALGYNMELVRTVDEDEPL 1167
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
385-874 |
2.54e-121 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 381.10 E-value: 2.54e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGINGWGTRAQAEQDVyDSGKYFERDTHKSGlGGSTDPG 464
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHTAAAQGGINAAGTNVQKAAGE-DSPEEHFYDTVKGG-DGLADQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 465 LVRTLSVKSGDAISWLSSLGVPLTV-----LSQLGGHSRKRTHRAPDKAdgtpvpiGFTIMQTLEQHVrtkLADRVTIME 539
Cdd:COG1053 84 LVEALAEEAPEAIDWLEAQGVPFSRtpdgrLPQFGGHSVGRTCYAGDGT-------GHALLATLYQAA---LRLGVEIFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 540 NTTVTSLlsksrVRHDGakqvRVYGVEVLQDEGVVSRILADAVILATGGFSNDKtpnSLLQEFAPQLSGFPTTNGPWATG 619
Cdd:COG1053 154 ETEVLDL-----IVDDG----RVVGVVARDRTGEIVRIRAKAVVLATGGFGRNY---EMRAEYLPEAEGALSTNAPGNTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 620 DGVKLARELGVKLVDMDKVQLHPTGLidPKDPANPTkylgpEALRGS-GGVLLNKKGERFVNELDLRSVVSNAIIEQGDE 698
Cdd:COG1053 222 DGIAMALRAGAALADMEFVQFHPTGL--PGDGGLIS-----EGARGKpGGILVNKEGERFMNEYAPRDVVSRAILEEIDE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 699 YpdaggskfAFCVLNDAAVKLFGvnshgfYWKRLGLFVKADTVEKLAALIGCPVENVRNTLGDYEQLSK----ENRQCPK 774
Cdd:COG1053 295 P--------AYLVLDLRHRRRLE------EYLEAGYLVKADTIEELAAKLGIDAAELAATVARYNAAAKagvdPRGTCLG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 775 TRKvvypcvvgpQGPFYVAFVTPSIHYTMGGCLISPSAEMQLEENTTSPfghrrpifGLFGAGEVTGGVHGGNRLGGNSL 854
Cdd:COG1053 361 PIK---------EGPFYAIPVRPGVHYTMGGLRVDADARVLDADGTPIP--------GLYAAGEAAGSVHGANRLGGNSL 423
|
490 500
....*....|....*....|
gi 71400421 855 LECVVFGRIAGDRAATILQK 874
Cdd:COG1053 424 GDALVFGRIAGRHAAEYAKA 443
|
|
| flavo_cyto_c |
TIGR01813 |
flavocytochrome c; This model describes a family of redox proteins related to the succinate ... |
385-866 |
2.83e-114 |
|
flavocytochrome c; This model describes a family of redox proteins related to the succinate dehydrogenases and fumarate reductases of E. coli, mitochondria, and other well-characterized systems. A member of this family from Shewanella frigidimarina NCIMB400 is characterized as a water-soluble periplasmic protein with four heme groups, a non-covalently bound FAD, and essentially unidirectional fumarate reductase activity. At least seven distinct members of this family are found in Shewanella oneidensis, a species able to use a wide variety of pathways for respiraton. [Energy metabolism, Electron transport]
Pssm-ID: 273816 [Multi-domain] Cd Length: 439 Bit Score: 362.04 E-value: 2.83e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACG-AQVILLEKEPKVGGNSAKATSGINGWGTRAQAEQDVYDSGKYFERDTHKSGlGGSTDP 463
Cdd:TIGR01813 2 VVVVGSGFAGLSAALSAKKAGaANVVLLEKMPVIGGNSAIAAGGMNAAGTDQQKALGIEDSPELFIKDTLKGG-RGINDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 464 GLVRTLSVKSGDAISWLS-SLGVPLTVLSQLGGHSRKRTHRAPDKAdgtpvPIGFTIMQTLEQHVRTKladRVTIMENTT 542
Cdd:TIGR01813 81 ELVRILAEESKDAVDWLQdGVGARLDDLIQLGGHSVPRAHRPTGGA-----ASGAEIVQTLYKKAKKE---GIDTRLNSK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 543 VTSLLSksrvrhdgAKQVRVYGVEVLQDEGVVSRILADAVILATGGFSNDktpNSLLQEFAPQLSGFPTTNGPWATGDGV 622
Cdd:TIGR01813 153 VEDLIQ--------DDQGSVVGVVVKGKGKGIYIKAAKAVVLATGGFGSN---KEMIAKYDPTLKHLGSTNQPGATGDGL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 623 KLARELGVKLVDMDKVQLHPTGLIDPKdpanptKYLGPEALRGSGGVLLNKKGERFVNELDLRSVVSNAIIEQGDeypda 702
Cdd:TIGR01813 222 LMAEKIGAALVDMDYIQAHPTASPDEG------GFLISEAVRGYGAILVNKTGERFMNELATRDKVSDAILAQPG----- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 703 ggsKFAFCVLNDA-AVKLFGVNSHgfywKRLGLFVKADTVEKLAALIGCPVENVRNTLGDYEQLSKENRQCPKTRKVVYP 781
Cdd:TIGR01813 291 ---KDAYLIFDDDvYKKAKMVDNY----YRLGVAYKGDSLEELAKQFGIPAAALKQTIKDYNGYVASGKDTPFGRPMDMP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 782 cVVGPQGPFYVAFVTPSIHYTMGGCLISPSAEMqLEENTTspfghrrPIFGLFGAGEVTGGVHGGNRLGGNSLLECVVFG 861
Cdd:TIGR01813 364 -TDLSKAPYYAIKVTPGVHHTMGGVKINTKAEV-LDANGK-------PIPGLFAAGEVTGGVHGANRLGGNAIADCIVFG 434
|
....*
gi 71400421 862 RIAGD 866
Cdd:TIGR01813 435 RIAGE 439
|
|
| PRK06481 |
PRK06481 |
flavocytochrome c; |
385-869 |
2.83e-102 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 332.57 E-value: 2.83e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGINGWGTRAQAEQDVYDSGKYFERDTHKSGlGGSTDPG 464
Cdd:PRK06481 64 IVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAGGNTMKASSGMNASETKFQKAQGIADSNDKFYEETLKGG-GGTNDKA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 465 LVRTLSVKSGDAISWLSSLGVPLTVLSQLGGHSRKRTHRApdkADGTPVpiGFTIMQTLEQHVRTKladRVTIMENTTVT 544
Cdd:PRK06481 143 LLRYFVDNSASAIDWLDSMGIKLDNLTITGGMSEKRTHRP---HDGSAV--GGYLVDGLLKNVQER---KIPLFVNADVT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 545 SLLSKsrvrhDGAkqvrVYGVEVLQDEGVVSRILADAVILATGGFSNDKtpnSLLQEFAPQLSGFPTTNGPWATGDGVKL 624
Cdd:PRK06481 215 KITEK-----DGK----VTGVKVKINGKETKTISSKAVVVTTGGFGANK---DMIAKYRPDLKGYVTTNQEGSTGDGIKM 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 625 ARELGVKLVDMDKVQLHPTglidpkdPANPTKYLGPEALRGSGGVLLNKKGERFVNELDLRSVVSNAIIEQGDeypdagg 704
Cdd:PRK06481 283 IEKLGGTTVDMDQIQIHPT-------VQQSKSYLIGEAVRGEGAILVNQKGKRFGNELDTRDKVSAAINKLPE------- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 705 sKFAFCVLnDAAVKLfGVNSHGFYWKRlGLFVKADTVEKLAALIGCPVENVRNTLGDYEQL--SKENRQCPKTRKVVYPC 782
Cdd:PRK06481 349 -KYAYVVF-DSGVKD-RVKAIAQYEEK-GFVEEGKTIDELAKKINVPAETLTKTLDTWNKAvkNKKDEAFGRTTGMDNDL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 783 vvgPQGPFYVAFVTPSIHYTMGGCLISPSAEMQLEENTtspfghrrPIFGLFGAGEVTGGVHGGNRLGGNSLLECVVFGR 862
Cdd:PRK06481 425 ---STGPYYAIKIAPGIHYTMGGVKINTNTEVLKKDGS--------PITGLYAAGEVTGGLHGENRIGGNSVADIIIFGR 493
|
....*..
gi 71400421 863 IAGDRAA 869
Cdd:PRK06481 494 QAGTQSA 500
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
385-854 |
5.34e-75 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 253.75 E-value: 5.34e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGINGWGTRAQAEQdvyDSGKYFERDThKSGLGGSTDPG 464
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWSSGGIDALGNPPQGGI---DSPELHPTDT-LKGLDELADHP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 465 LVRTLSVKSGDAISWLSSLGVPLT-------VLSQLGGHSRKRTHrAPDKADGTPVPI-GFTIMQTLEQHVRTKLadrVT 536
Cdd:pfam00890 78 YVEAFVEAAPEAVDWLEALGVPFSrtedghlDLRPLGGLSATWRT-PHDAADRRRGLGtGHALLARLLEGLRKAG---VD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 537 IMENTTVTSLlsksrVRHDGakqvRVYGVEV-LQDEGVVSRILAD-AVILATGGFSNDKtpnsllQEFAPQLSGFPTTNG 614
Cdd:pfam00890 154 FQPRTAADDL-----IVEDG----RVTGAVVeNRRNGREVRIRAIaAVLLATGGFGRLA------ELLLPAAGYADTTNP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 615 PWATGDGVKLARELGVKLVD--MDKVQLHPTGLIDPKDPANptkyLGPEALRGSGGVLLNKKGERFVNELDLRSVVSNAI 692
Cdd:pfam00890 219 PANTGDGLALALRAGAALTDdlMEFVQFHPTSLVGIRLGSG----LLIEALRGEGGILVNKDGRRFMNELASRDVVSRAI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 693 IEQGdeyPDAGGSkfAFCVLNDaavklfgvnSHGFywkrlglfvkadtveklaaligcPVENVRNTLGDYEQLSKENRQC 772
Cdd:pfam00890 295 TRNE---IDEGRG--ANVYLDA---------SGSL-----------------------DAEGLEATLPAINEEAIFGLDV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 773 PKTRKVVYpcvvgpqgpfyvafVTPSIHYTMGGCLISPSAEMQLEENTtspfghrrPIFGLFGAGEVT-GGVHGGNRLGG 851
Cdd:pfam00890 338 DPYDRPIP--------------VFPAQHYTMGGVRTDENGRVLDADGQ--------PIPGLYAAGEVAcGGVHGANRLGG 395
|
...
gi 71400421 852 NSL 854
Cdd:pfam00890 396 NSL 398
|
|
| NadB |
COG0029 |
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ... |
383-884 |
1.98e-71 |
|
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439800 [Multi-domain] Cd Length: 521 Bit Score: 247.71 E-value: 1.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 383 ARVIVVGGGLAGLSAAIEATACGaQVILLEKEPKVGGNSAKATSGINGwgtrAQAEQDVYDSgkyFERDTHKSGlGGSTD 462
Cdd:COG0029 5 TDVLVIGSGIAGLSAALKLAERG-RVTLLTKGELGESNTRWAQGGIAA----VLDPGDSPEL---HIADTLAAG-AGLCD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 463 PGLVRTLSVKSGDAISWLSSLGVPLT-------VLSQLGGHSRKRTHRApdkADGTpvpiGFTIMQTLEQHVRTklADRV 535
Cdd:COG0029 76 PEAVRVLVEEGPERIRELIELGVPFDrdedgelALTREGGHSRRRILHA---GDAT----GREIERALLEAVRA--HPNI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 536 TIMENTTVTSLLsksrVRHDGakqvRVYGVEVL-QDEGVVSRILADAVILATGGfsndktpnsllqefAPQLsgFP-TTN 613
Cdd:COG0029 147 TVLENHFAVDLI----TDADG----RCVGAYVLdEKTGEVETIRAKAVVLATGG--------------AGQL--YAyTTN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 614 GPWATGDGVKLARELGVKLVDMDKVQLHPTGLIDPKDPAnptkYLGPEALRGSGGVLLNKKGERFV------NELDLRSV 687
Cdd:COG0029 203 PDVATGDGIAMAYRAGARLADMEFVQFHPTALYHPGAPS----FLISEAVRGEGAVLRNADGERFMpdyhprAELAPRDV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 688 VSNAIieqgDEYPDAGGSKfafCVLNDAavklfgvnSHgfywkRLGLFVKA---DTVEKLAALiGC-----PVEnvrntl 759
Cdd:COG0029 279 VARAI----DAEMKKTGGD---CVYLDI--------SH-----LDAEFIRErfpTIYARCLEL-GIditkePIP------ 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 760 gdyeqlskenrqcpktrkvvypcvvgpqgpfyvafVTPSIHYTMGGCLISPSAEmqleentTSpfghrrpIFGLFGAGEV 839
Cdd:COG0029 332 -----------------------------------VAPAAHYTMGGVATDLDGR-------TS-------IPGLYAVGEV 362
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 71400421 840 T-GGVHGGNRLGGNSLLECVVFGRIAGDRAATILQKKPVPLSFKTW 884
Cdd:COG0029 363 AcTGVHGANRLASNSLLEGLVFGRRAAEDIAARLAESPLPPEIPEW 408
|
|
| cyt_b5_reduct_like |
cd06183 |
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ... |
902-1124 |
5.84e-56 |
|
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.
Pssm-ID: 99780 [Multi-domain] Cd Length: 234 Bit Score: 193.94 E-value: 5.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 902 SRVLRFNLPGALQRSGLQLGQFIAIRGEWDGQQLIGYYSPITLPDDLGVIGILARS-DKGTLKEWISALEPGDAVEMKGC 980
Cdd:cd06183 13 TRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDDKGYFDLLIKIyPGGKMSQYLHSLKPGDTVEIRGP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 981 GGlvierrfseRYLYFSGHALKKLCLIAGGTGVAPMLQIIRAALKKPflENIESIRLIYAAEDVSELTYRELLEHHQRDS 1060
Cdd:cd06183 93 FG---------KFEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKDP--EDKTKISLLYANRTEEDILLREELDELAKKH 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71400421 1061 KGKFRSIFVLNRPPPIWTDGVGFIDKKLLSSSVQP-PAKDLLVAICGPPIMQRV-VKTCLKSLGYD 1124
Cdd:cd06183 162 PDRFKVHYVLSRPPEGWKGGVGFITKEMIKEHLPPpPSEDTLVLVCGPPPMIEGaVKGLLKELGYK 227
|
|
| ApbE |
COG1477 |
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ... |
51-343 |
3.28e-51 |
|
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441086 [Multi-domain] Cd Length: 294 Bit Score: 182.65 E-value: 3.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 51 PFTLKVVAEAVAfsRAKEVADEVLRSAWHLaDTVLNNFNPNSEISMIGRLPVGQKHTMSATLKSVITCCQHVFNSSRGVF 130
Cdd:COG1477 4 TVSITLYGPDEA--QAEAALAAAFAELDRL-EALLSTYRPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 131 DPATGPIIEALRAKVAEKASVSDEQMEKLFRVCNFSSsFIVDLEMGTIARKHEDARFDLGGVSKGYIVDYVVERLNAAGI 210
Cdd:COG1477 81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRK-VELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 211 VDVYFEWGGDCRASGTNARRTPWMVGIirppsleqlRNPPKDPSYIRVLPLNDEALCTSGDYENLTEgSNKKLYTSIFD- 289
Cdd:COG1477 160 TNALVNLGGDIRALGTKPDGRPWRVGI---------EDPRDPGAVLAVLELSDGAVATSGDYERYFE-IDGKRYSHIIDp 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 71400421 290 ---WkkrsllePVESELAQVSIRCYSAMYADALATASLIKrDIKKVRQMLEDWRHVR 343
Cdd:COG1477 230 rtgY-------PVEHGLASVTVIAPDAMLADALATALFVL-GPEKGLALAERLPGLE 278
|
|
| sdhA_frdA_Gneg |
TIGR01812 |
succinate dehydrogenase or fumarate reductase, flavoprotein subunitGram-negative/mitochondrial ... |
385-878 |
1.02e-48 |
|
succinate dehydrogenase or fumarate reductase, flavoprotein subunitGram-negative/mitochondrial subgroup; This model represents the succinate dehydrogenase flavoprotein subunit as found in Gram-negative bacteria, mitochondria, and some Archaea. Mitochondrial forms interact with ubiquinone and are designated EC 1.3.5.1, but can be degraded to 1.3.99.1. Some isozymes in E. coli and other species run primarily in the opposite direction and are designated fumarate reductase. [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]
Pssm-ID: 273815 [Multi-domain] Cd Length: 566 Bit Score: 183.30 E-value: 1.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGINGwgtrAQAEQDVYDSGKYFERDTHKSG--LGgstD 462
Cdd:TIGR01812 2 VVIVGAGLAGLRAAVEAAKAGLNTAVISKVYPTRSHTVAAQGGMAA----ALGNVDPDDSWEWHAYDTVKGSdyLA---D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 463 PGLVRTLSVKSGDAISWLSSLGVPLTVLSQ-------LGGHSRKRTHRAPDKAdgtpvpiGFTIMQTLEQhvrTKLADRV 535
Cdd:TIGR01812 75 QDAVEYMCQEAPKAILELEHWGVPFSRTPDgriaqrpFGGHSKDRTCYAADKT-------GHALLHTLYE---QCLKLGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 536 TIMENTTVTSLLsksrvrHDGAkqvRVYGVEVLQ-DEGVVSRILADAVILATGGFsndktpnsllqefapqlsG---FPT 611
Cdd:TIGR01812 145 SFFNEYFALDLI------HDDG---RVRGVVAYDlKTGEIVFFRAKAVVLATGGY------------------GriyKTT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 612 TNGPWATGDGVKLARELGVKLVDMDKVQLHPTGLIdpkdpanPTKYLGPEALRGSGGVLLNKKGERFV-----NELDL-- 684
Cdd:TIGR01812 198 TNAHINTGDGMAMALRAGVPLKDMEFVQFHPTGLY-------PSGILITEGCRGEGGYLVNKNGERFMeryapEKMELap 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 685 RSVVSNAIIEqgdEYPDAGGskfafcvlndaavklFGVNSHGFYWKRLglfvkadtveklaaligcpvenvrNTLGdyEQ 764
Cdd:TIGR01812 271 RDVVSRAMWT---EIREGRG---------------VGSPPGDYVYLDL------------------------RHLG--EE 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 765 LSKEN----RQCPKTRKVVYPcVVGPqgpfyvAFVTPSIHYTMGGclispsaemqLEENTTSPFGHRRPIFGLFGAGEVT 840
Cdd:TIGR01812 307 KIEERlpqiRELAKYFAGVDP-VKEP------IPVRPTAHYSMGG----------IPTDYTGRVICETIVKGLFAAGECA 369
|
490 500 510
....*....|....*....|....*....|....*....
gi 71400421 841 G-GVHGGNRLGGNSLLECVVFGRIAGDRAATILQKKPVP 878
Cdd:TIGR01812 370 CvSVHGANRLGGNSLLELVVFGRIAGEAAAEYAAKTGNP 408
|
|
| nadB |
TIGR00551 |
L-aspartate oxidase; L-aspartate oxidase is the B protein, NadB, of the quinolinate synthetase ... |
383-876 |
5.73e-47 |
|
L-aspartate oxidase; L-aspartate oxidase is the B protein, NadB, of the quinolinate synthetase complex. Quinolinate synthetase makes a precursor of the pyridine nucleotide portion of NAD. This model identifies proteins that cluster as L-aspartate oxidase (a flavoprotein difficult to separate from the set of closely related flavoprotein subunits of succinate dehydrogenase and fumarate reductase) by both UPGMA and neighbor-joining trees. The most distant protein accepted as an L-aspartate oxidase (NadB), that from Pyrococcus horikoshii, not only clusters with other NadB but is just one gene away from NadA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
Pssm-ID: 273131 [Multi-domain] Cd Length: 489 Bit Score: 176.14 E-value: 5.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 383 ARVIVVGGGLAGLSAAIeATACGAQVILLEKEPKVGGNSAKATSGIngwgTRAQAEQDVYDSgkYFErDTHKSGlGGSTD 462
Cdd:TIGR00551 3 MDVVVIGSGAAGLSAAL-ALAEKGRVSVITKASVTDSNSYYAQGGI----AAALAETDSIDA--HVE-DTLAAG-AGICD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 463 PGLVRTLSVKSGDAISWLSSLGVPLT-------VLSQLGGHSRKRTHRApdkADGTpvpiGFTIMQTLEQHVRTKLadRV 535
Cdd:TIGR00551 74 EEAVWFVVSDGSEAVQFLVSHGVTFDrneqggvALTREGGHSYPRIFHA---GDAT----GREIIPTLEKHARSEP--NV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 536 TIMENTTVTSLLSKSRvrhdgakqvRVYGVEVlQDEGVVSRILADAVILATGGFSNdktpnsLLQEfapqlsgfpTTNGP 615
Cdd:TIGR00551 145 NIIEGEFALDLLIETG---------RCAGVFV-QGSGTLETLHADAVVLATGGFGG------LYRF---------TTNPK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 616 WATGDGVKLARELGVKLVDMDKVQLHPTGLIDPKDPanptKYLGPEALRGSGGVLLNKKGERFVN------ELDLRSVVS 689
Cdd:TIGR00551 200 NSTGDGIALAWRAGVPVRDLEFVQFHPTALIKPRVR----YFLITEAVRGEGAKLVDRDGERFMAdrhprgELAPRDIVA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 690 NAIieqgDEYPDAGGskfAFCVLNDAAvklfgvnshgfywkrlglfvkadtveklaaligcPVENVRntlgdyeqlsken 769
Cdd:TIGR00551 276 RAI----DMEMAEGG---GDCVFLDAS----------------------------------GIENFK------------- 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 770 RQCPKTRKVVYPCVVGP-QGPFYVAfvtPSIHYTMGGClispsaemqleenTTSPFGhRRPIFGLFGAGEVT-GGVHGGN 847
Cdd:TIGR00551 302 DRFPTIYAVCRGAGIDPeREPIPVA---PGAHYTMGGI-------------SVDAFG-RTTIPGLYAIGETAcTGLHGAN 364
|
490 500
....*....|....*....|....*....
gi 71400421 848 RLGGNSLLECVVFGriaGDRAATILQKKP 876
Cdd:TIGR00551 365 RLASNSLLECLVFG---LRAARTISREPP 390
|
|
| sdhA |
PRK06263 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
385-869 |
3.84e-46 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 235758 [Multi-domain] Cd Length: 543 Bit Score: 175.17 E-value: 3.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGINGwgtrAQAEQDVYDsgKYFErDTHKSGlGGSTDPG 464
Cdd:PRK06263 10 VLIIGSGGAGARAAIEAERGKNVVIVSKGLFGKSGCTVMAEGGYNA----VLNPEDSFE--KHFE-DTMKGG-AYLNDPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 465 LVRTLSVKSGDAISWLSSLGVPLTV-----LSQ--LGGHSRKRTHRAPDKAdgtpvpiGFTIMQTLEQHVRtklADRVTI 537
Cdd:PRK06263 82 LVEILVKEAPKRLKDLEKFGALFDRtedgeIAQrpFGGQSFNRTCYAGDRT-------GHEMMMGLMEYLI---KERIKI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 538 MENTTVTSLLSKSRVRHDGAkqvrvYGVEVLQDEGVVsrILADAVILATGGfsndktpnsllqefAPQLsgFP-TTNGPW 616
Cdd:PRK06263 152 LEEVMAIKLIVDENREVIGA-----IFLDLRNGEIFP--IYAKATILATGG--------------AGQL--YPiTSNPIQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 617 ATGDGVKLARELGVKLVDMDKVQLHPTGLIDPKDpanPTKYLGPEALRGSGGVLLNKKGERFVN-------ELDLRSVVS 689
Cdd:PRK06263 209 KTGDGFAIAYRAGAELIDMEMVQFHPTGMVYPYS---GRGILVTEAVRGEGGILYNKNGERFMKrydpermELSTRDVVA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 690 NAI---IEQGDeypdaggskfafcvlndaavklfGVNSHGFYwkrlgLFV---KADTVE-KLAALigcpvenvrntlgdY 762
Cdd:PRK06263 286 RAIyteIQEGR-----------------------GTNHGGVY-----LDVthlPDEVIEeKLETM--------------L 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 763 EQ-------LSKEnrqcpktrkvvypcvvgpqgPFYVAfvtPSIHYTMGGCLISPSAEmqleenTTspfghrrpIFGLFG 835
Cdd:PRK06263 324 EQfldvgvdIRKE--------------------PMEVA---PTAHHFMGGIRINEDCE------TN--------IPGLFA 366
|
490 500 510
....*....|....*....|....*....|....
gi 71400421 836 AGEVTGGVHGGNRLGGNSLLECVVFGRIAGDRAA 869
Cdd:PRK06263 367 CGEVAGGVHGANRLGGNALADTQVFGAIAGKSAA 400
|
|
| PRK07121 |
PRK07121 |
FAD-binding protein; |
385-869 |
4.88e-42 |
|
FAD-binding protein;
Pssm-ID: 180854 [Multi-domain] Cd Length: 492 Bit Score: 161.59 E-value: 4.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGIN-GWGTRAQAEQDVYDSG----KYFERDthksgLGG 459
Cdd:PRK07121 23 VVVVGFGAAGACAAIEAAAAGARVLVLERAAGAGGATALSGGVIYlGGGTAVQKAAGFEDSPenmyAYLRVA-----VGP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 460 STDPGLVRTLSVKSGDAISWLSSLGVPL--------TV-------LSQLGG--------HSR--KRTHR--APDKADGtp 512
Cdd:PRK07121 98 GVDEEKLRRYCEGSVEHFDWLEGLGVPFersffpekTSyppndegLYYSGNekawpfaeIAKpaPRGHRvqGPGDSGG-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 513 vpiGFTIMQTLeqhVRTKLADRVTIMENTTVTSLLsksrVRHDGakqvRVYGVEVLQDeGVVSRILAD-AVILATGGFSN 591
Cdd:PRK07121 176 ---GAMLMDPL---AKRAAALGVQIRYDTRATRLI----VDDDG----RVVGVEARRY-GETVAIRARkGVVLAAGGFAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 592 DKTpnsLLQEFAPQLSGFPTTNGPWATGDGVKLARELGVKLVDMDKVQLhpTGLIDPkdpanptkylgPEALrgSGGVLL 671
Cdd:PRK07121 241 NRE---MVARYAPAYAGGLPLGTTGDDGSGIRLGQSAGGATAHMDQVFA--WRFIYP-----------PSAL--LRGILV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 672 NKKGERFVNELDLRSVVSNAIIEQgdeyPDAGgskfAFCVLNDAAVKLFGVNSHGFYWKRLGLFVKADTVEKLAALIGCP 751
Cdd:PRK07121 303 NARGQRFVNEDTYGARIGQFILEQ----PGGT----AYLIVDEALFEEARAQLRPQIDGRTPGAWKAETVEELARKLGIP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 752 VENVRNTLGDYEQLSKENRQCP--KTRKVVYPCVvgpQGPFYV----AFVTPSIHYTMGGCLISPSAEMQLEEnttspfg 825
Cdd:PRK07121 375 PGGLQATVDAYNRAAAGGEDPPfhKQPEWLRPLD---TGPFAAidlsLGKAPTPGFTLGGLRVDEDTGEVLRA------- 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 71400421 826 HRRPIFGLFGAGEVTGGVHGGNRLGGNSLLECVVFGRIAGDRAA 869
Cdd:PRK07121 445 DGAPIPGLYAAGRCASGIASNGYVSGLSLADCSFFGRRAGRHAA 488
|
|
| sdhA |
PRK06069 |
succinate dehydrogenase/fumarate reductase flavoprotein subunit; |
385-878 |
3.35e-40 |
|
succinate dehydrogenase/fumarate reductase flavoprotein subunit;
Pssm-ID: 235689 [Multi-domain] Cd Length: 577 Bit Score: 157.91 E-value: 3.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACG---AQVILLEKEPKVGGNSAKATSGingwgTRAQAEQDVYDSGKYFERDTHKsglgGS- 460
Cdd:PRK06069 8 VVIVGSGLAGLRAAVAAAERSggkLSVAVVSKTQPMRSHSVSAEGG-----TAAVLYPEKGDSFDLHAYDTVK----GSd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 461 --TDPGLVRTLSVKSGDAISWLSSLGVPLT-----VLSQ--LGGHSRKRTHRAPDKAdgtpvpiGFTIMQTLeqHVRTKL 531
Cdd:PRK06069 79 flADQDAVEVFVREAPEEIRFLDHWGVPWSrrpdgRISQrpFGGMSFPRTTFAADKT-------GFYIMHTL--YSRALR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 532 ADRVTIMENTTVTSLLSKsrvrhDGakqvRVYGVEVLQ-DEGVVSRILADAVILATGGfsndktpnsllqefAPQLSGFp 610
Cdd:PRK06069 150 FDNIHFYDEHFVTSLIVE-----NG----VFKGVTAIDlKRGEFKVFQAKAGIIATGG--------------AGRLYGF- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 611 TTNGPWATGDGVKLARELGVKLVDMDKVQLHPTGLIdpkdpanPTKYLGPEALRGSGGVLLNKKGERFVN-------ELD 683
Cdd:PRK06069 206 TTYAHSVTGDGLAIAYRAGIPLKDMEFVQFHPTGLV-------PSGILITEAARGEGGYLINKEGERFMKryapqkmELA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 684 LRSVVSNAI---IEQGDEYPDAGGSKFafcVLNDaaVKLFG---VNshgfywKRLGL-------FVKADTVEKLaaligC 750
Cdd:PRK06069 279 PRDVVSRAImteIMEGRGFKHESGLCY---VGLD--LRHLGeekIN------ERLPLireiakkYAGIDPVTEP-----I 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 751 PVEnvrntlgdyeqlskenrqcpktrkvvypcvvgpqgpfyvafvtPSIHYTMGGclispsaeMQLEENTTSPFGHRRPI 830
Cdd:PRK06069 343 PVR-------------------------------------------PAAHYTMGG--------IHTDVYGRVLTADGEWV 371
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 71400421 831 FGLFGAGEVTG-GVHGGNRLGGNSLLECVVFGRIAGDRAATILQKKPVP 878
Cdd:PRK06069 372 RGLWAAGEAAAvSVHGANRLGSNSTAECLVWGRIAGEQAAEYALKRPAP 420
|
|
| PRK08071 |
PRK08071 |
L-aspartate oxidase; Provisional |
383-875 |
1.86e-39 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236147 [Multi-domain] Cd Length: 510 Bit Score: 154.38 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 383 ARVIVVGGGLAGLSAAIEATAcGAQVILLEKEPKVGGNSAKATSGIngwgTRAQAEQDvyDSGKYFErDTHKSGLGgSTD 462
Cdd:PRK08071 4 ADVIIIGSGIAALTVAKELCH-EYNVIIITKKTKRNSNSHLAQGGI----AAAVATYD--SPNDHFE-DTLVAGCH-HNN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 463 PGLVRTLsVKSG-DAISWLSSLGVPLTV-------LSQLGGHSRKRTHRAPDKADGtpvpigftimQTLEQHVRTKLADR 534
Cdd:PRK08071 75 ERAVRYL-VEEGpKEIQELIENGMPFDGdetgplhLGKEGAHRKRRILHAGGDATG----------KNLLEHLLQELVPH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 535 VTIMENTTVTSLLsksrvRHDGakqvRVYGVEVLQDEGVVSRILADAVILATGGFSNdktpnslLQEFapqlsgfpTTNG 614
Cdd:PRK08071 144 VTVVEQEMVIDLI-----IENG----RCIGVLTKDSEGKLKRYYADYVVLASGGCGG-------LYAF--------TSND 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 615 PWATGDGVKLARELGVKLVDMDKVQLHPTGLIdpkdpANPTKY-LGPEALRGSGGVLLNKKGERFVNE----LDL--RSV 687
Cdd:PRK08071 200 KTITGDGLAMAYRAGAELVDLEFIQFHPTMLY-----ANGRCVgLVSEAVRGEGAVLINEDGRRFMMGihplADLapRDV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 688 VSNAIIEQgdeyPDAGGSKFafcvLNDAAVKLFGvnshgfywKRLglfvkaDTVEKLAALIGCPVENVRntlgdyeqlsk 767
Cdd:PRK08071 275 VARAIHEE----LLSGEKVY----LNISSIQNFE--------ERF------PTISALCEKNGVDIETKR----------- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 768 enrqCPktrkvvypcvvgpqgpfyvafVTPSIHYTMGGCLISPSAEmqleenTTSPfghrrpifGLFGAGEVT-GGVHGG 846
Cdd:PRK08071 322 ----IP---------------------VVPGAHFLMGGVKTNLDGE------TSIP--------GLYAIGEVAcTGVHGA 362
|
490 500
....*....|....*....|....*....
gi 71400421 847 NRLGGNSLLECVVFGRIAGDRaatILQKK 875
Cdd:PRK08071 363 NRLASNSLLEGLVFGKRAAEH---ILTKA 388
|
|
| PRK08274 |
PRK08274 |
FAD-dependent tricarballylate dehydrogenase TcuA; |
385-869 |
3.67e-39 |
|
FAD-dependent tricarballylate dehydrogenase TcuA;
Pssm-ID: 236214 [Multi-domain] Cd Length: 466 Bit Score: 152.34 E-value: 3.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPK--VGGNSAKATsgingwGTR-AQAEQDVYDSGKYFERDTHKSGL---G 458
Cdd:PRK08274 7 VLVIGGGNAALCAALAAREAGASVLLLEAAPRewRGGNSRHTR------NLRcMHDAPQDVLVGAYPEEEFWQDLLrvtG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 459 GSTDPGLVRTLSVKSGDAISWLSSLGVpltvlsqlggHSRKRTHRAPDKADGTPVPI--GFTIMQTLEqhvRTklADR-- 534
Cdd:PRK08274 81 GRTDEALARLLIRESSDCRDWMRKHGV----------RFQPPLSGALHVARTNAFFWggGKALVNALY---RS--AERlg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 535 VTIMENTTVTSLLsksrvRHDGakqvRVYGVEVLQDEGVVSRILADAVILATGGF-SNdktPNSLLQEFAPQLSGFPTTN 613
Cdd:PRK08274 146 VEIRYDAPVTALE-----LDDG----RFVGARAGSAAGGAERIRAKAVVLAAGGFeSN---REWLREAWGQPADNFLVRG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 614 GPWATGDGVKLARELGVKLVDmDKVQLHPTGlIDpkdpANPTKYLGPEALRGSG---GVLLNKKGERFVNE-LDLR---- 685
Cdd:PRK08274 214 TPYNQGDLLKALLDAGADRIG-DPSQCHAVA-ID----ARAPLYDGGICTRIDCvplGIVVNRDGERFYDEgEDFWpkry 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 686 SVVSNAIIEQgdeyPDAggskFAFCVLNDAAVKLFgvNSHGFYwkrlglFVKADTVEKLAALIGCPVENVRNTLGDYEQL 765
Cdd:PRK08274 288 AIWGRLVAQQ----PGQ----IAYQIFDAKAIGRF--MPPVFP------PIQADTLEELAEKLGLDPAAFLRTVAAFNAA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 766 SK--------------ENRQCPKT---RKVVypcvvgpQGPFYVAFVTPSIHYTMGGCLISPSAEMQLEENttspfghrR 828
Cdd:PRK08274 352 VRpgpfdptvlddcgtEGLTPPKShwaRPID-------TPPFYAYPVRPGITFTYLGLKVDEDARVRFADG--------R 416
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 71400421 829 PIFGLFGAGEVTGG-VHGGNRLGGNSLLECVVFGRIAGDRAA 869
Cdd:PRK08274 417 PSPNLFAAGEMMAGnVLGKGYPAGVGLTIGAVFGRIAGEEAA 458
|
|
| ApbE |
pfam02424 |
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ... |
51-337 |
3.74e-39 |
|
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella typhimurium. ApbE is involved in thiamine synthesis. It acts as an FAD:protein FMN-transferase, catalysing the attachment of an FMN residue to a threonine residue of a protein via a phosphoester bond in such bacterial flavoproteins.
Pssm-ID: 460554 [Multi-domain] Cd Length: 227 Bit Score: 145.28 E-value: 3.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 51 PFTLKVVAEAvafSRAKEVADEVLRSAWHLADTVLNNFNPNSEISMIGRLPvGQKHTMSATLKSVITCCQHVFNSSRGVF 130
Cdd:pfam02424 3 TVSITVYGPD---EAAAEALEAAIDAELDRLEALLSTYRPDSELSRLNRAG-AGPVKVSPELFELLERALEISELSGGAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 131 DPATGPIIealrakvaekasvsdeqmeklfrvcnfsssfivdlemgtiarkhedarFDLGGVSKGYIVDYVVERLNAAGI 210
Cdd:pfam02424 79 DITVGPLV------------------------------------------------LDLGGIAKGYAVDRAAELLKAKGV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 211 VDVYFEWGGDCRASGTNARRTPWMVGIirppsleqlRNpPKDPSYIRVLPLNDEALCTSGDYEN-LTEGsnkKLYTSIFD 289
Cdd:pfam02424 111 TSALVNLGGDIRALGTKPDGSPWRVGI---------QD-PRDPDSLAVLELSDKAVATSGDYERyFEDG---KRYHHIID 177
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 71400421 290 wkKRSLLePVESELAQVSIRCySAMYADALATASLIKrDIKKVRQMLE 337
Cdd:pfam02424 178 --PRTGY-PVANGLASVTVIA-DAMLADALATALFVL-GPEKGLALLE 220
|
|
| PRK07512 |
PRK07512 |
L-aspartate oxidase; Provisional |
384-879 |
7.77e-39 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236036 [Multi-domain] Cd Length: 513 Bit Score: 152.37 E-value: 7.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 384 RVIVVGGGLAGLSAAIeaTACGAQVILLEKEP-KVGGNSAKATSGIngwgtraQAEQDVYDSGKYFERDTHKSGlGGSTD 462
Cdd:PRK07512 11 RPVIVGGGLAGLMAAL--KLAPRPVVVLSPAPlGEGASSAWAQGGI-------AAALGPDDSPALHAADTLAAG-AGLCD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 463 PGLVRTLSVKSGDAISWLSSLGVPLT-------VLSQLGGHSRKRTHRApdKADGTpvpiGFTIMQTLEQHVRTklADRV 535
Cdd:PRK07512 81 PAVAALITAEAPAAIEDLLRLGVPFDrdadgrlALGLEAAHSRRRIVHV--GGDGA----GAAIMRALIAAVRA--TPSI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 536 TIMENTTVTSLLsksrvRHDGakqvRVYGVEVLQDEGVVSrILADAVILATGGfsndktpnsllqefapqlSG---FPTT 612
Cdd:PRK07512 153 TVLEGAEARRLL-----VDDG----AVAGVLAATAGGPVV-LPARAVVLATGG------------------IGglyAVTT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 613 NGPWATGDGVKLARELGVKLVDMDKVQLHPTGLIDPKDPAnPtkyLGPEALRGSGGVLLNKKGERFV------NELDLRS 686
Cdd:PRK07512 205 NPAGAFGQGLALAARAGAVIADPEFVQFHPTAIDIGRDPA-P---LATEALRGEGAILINEDGERFMadihpgAELAPRD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 687 VVSNAIIEQ---------------GDEYPDAGGSKFAFCvlndaavklfgvnshgfywkrlglfvkadtvekLAALIgcp 751
Cdd:PRK07512 281 VVARAVFAEiaagrgafldaraalGAHFATRFPTVYAAC---------------------------------RSAGI--- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 752 venvrntlgDyeqlskenrqcPKTRKVvyPcvvgpqgpfyvafVTPSIHYTMGGCLispsaemqleentTSPFGhRRPIF 831
Cdd:PRK07512 325 ---------D-----------PARQPI--P-------------VAPAAHYHMGGIA-------------VDADG-RSSLP 355
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 71400421 832 GLFGAGEVTG-GVHGGNRLGGNSLLECVVFG-RIAGDRAATILQKKPVPL 879
Cdd:PRK07512 356 GLWAAGEVAStGLHGANRLASNSLLEAVVFAaRAAEDIAGTPAAAAAPLS 405
|
|
| PRK06175 |
PRK06175 |
L-aspartate oxidase; Provisional |
385-869 |
1.92e-38 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 180442 [Multi-domain] Cd Length: 433 Bit Score: 149.45 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATAcGAQVILLEKEPKVGGNSAKATSGIngwgTRAQAEQDVydsgKYFERDTHKSGlGGSTDPG 464
Cdd:PRK06175 7 VLIVGSGVAGLYSALNLRK-DLKILMVSKGKLNECNTYLAQGGI----SVARNKDDI----TSFVEDTLKAG-QYENNLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 465 LVRTLSVKSGDAISWLSSLGVPLT------VLSQLGGHSrkrTHRAPDKADGTpvpiGFTIMQTLEQHVRTKlaDRVTIM 538
Cdd:PRK06175 77 AVKILANESIENINKLIDMGLNFDkdekelSYTKEGAHS---VNRIVHFKDNT----GKKVEKILLKKVKKR--KNITII 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 539 ENTTVTSLLSKSRvrhdgakqvRVYGVEVLQDEGVVSrILADAVILATGG----FSNdktpnsllqefapqlsgfpTTNG 614
Cdd:PRK06175 148 ENCYLVDIIENDN---------TCIGAICLKDNKQIN-IYSKVTILATGGigglFKN-------------------STNQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 615 PWATGDGVKLARELGVKLVDMDKVQLHPTGLIDPKDpaNPTKYLGPEALRGSGGVLLNKKGERFVNELDLRSVVSNAIIE 694
Cdd:PRK06175 199 RIITGDGIAIAIRNNIKIKDLDYIQIHPTAFYEETI--EGKKFLISESVRGEGGKLLNSKGERFVDELLPRDVVTKAILE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 695 QGDEypdaGGSKfafCVLNDAAvklfgvnshgfywkrlglFVKADTVEKLAALIgcpvenvrntlgdYEQLSKENRQCPK 774
Cdd:PRK06175 277 EMKK----TGSN---YVYLDIT------------------FLDKDFLKNRFPTI-------------YEECLKRGIDITK 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 775 TrkvvypCVvgPqgpfyvafVTPSIHYTMGGclispsaeMQLEENTTSPFGHrrpifgLFGAGEVT-GGVHGGNRLGGNS 853
Cdd:PRK06175 319 D------AI--P--------VSPAQHYFMGG--------IKVDLNSKTSMKN------LYAFGEVScTGVHGANRLASNS 368
|
490
....*....|....*.
gi 71400421 854 LLECVVFGRiagdRAA 869
Cdd:PRK06175 369 LLEGLVFSK----RGA 380
|
|
| PLN02815 |
PLN02815 |
L-aspartate oxidase |
386-864 |
4.91e-37 |
|
L-aspartate oxidase
Pssm-ID: 215436 [Multi-domain] Cd Length: 594 Bit Score: 148.71 E-value: 4.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 386 IVVGGGLAGLSAAIEATACGAQVILLEKEPKVGgNSAKATSGINgwgtraqAEQDVYDSGKYFERDTHKSGlGGSTDPGL 465
Cdd:PLN02815 33 LVIGSGIAGLRYALEVAEYGTVAIITKDEPHES-NTNYAQGGVS-------AVLDPSDSVESHMRDTIVAG-AFLCDEET 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 466 VRTLSVKSGDAISWLSSLGVPLTV-------LSQLGGHSRkrtHRAPDKADGTPVPIGFTIMQTLEQHvrtklaDRVTIM 538
Cdd:PLN02815 104 VRVVCTEGPERVKELIAMGASFDHgedgnlhLAREGGHSH---HRIVHAADMTGREIERALLEAVKND------PNITFF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 539 ENTTVTSLLsksrVRHDGAkQVRVYGVEVL-QDEGVVSRILADAVILATGGfsndktpnsllqefAPQLsgFP-TTNGPW 616
Cdd:PLN02815 175 EHHFAIDLL----TSQDGG-SIVCHGADVLdTRTGEVVRFISKVTLLASGG--------------AGHI--YPsTTNPLV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 617 ATGDGVKLARELGVKLVDMDKVQLHPTGLIDPKDPANPTK-----YLGPEALRGSGGVLLNKKGERFVN------ELDLR 685
Cdd:PLN02815 234 ATGDGIAMAHRAQAVVSNMEFVQFHPTALADEGLPIKPAKarenaFLITEAVRGDGGILYNLAGERFMPlyderaELAPR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 686 SVVSNAIieqgDEYPDAGGSKfafCVLNDAAVKlfgvnshgfywkrlglfvkadtveklaaligcPVENVrntLGDYEQL 765
Cdd:PLN02815 314 DVVARSI----DDQLKKRNEK---YVLLDISHK--------------------------------PREEI---LSHFPNI 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 766 SKEnrqCPK-----TRKVVyPcvvgpqgpfyvafVTPSIHYTMGGClispSAEMQLEENttspfghrrpIFGLFGAGEVT 840
Cdd:PLN02815 352 AAE---CLKrgldiTKQPI-P-------------VVPAAHYMCGGV----RTGLQGETN----------VQGLYAAGEVA 400
|
490 500
....*....|....*....|....*
gi 71400421 841 -GGVHGGNRLGGNSLLECVVFGRIA 864
Cdd:PLN02815 401 cTGLHGANRLASNSLLEALVFARRA 425
|
|
| PRK07395 |
PRK07395 |
L-aspartate oxidase; Provisional |
385-862 |
2.99e-35 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236010 [Multi-domain] Cd Length: 553 Bit Score: 142.49 E-value: 2.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATAcGAQVILLEKEPKVGGNSAKATSGIngwgtraQAEQDVYDSGKYFERDTHKSGlGGSTDPG 464
Cdd:PRK07395 12 VLVVGSGAAGLYAALCLPS-HLRVGLITKDTLKTSASDWAQGGI-------AAAIAPDDSPKLHYEDTLKAG-AGLCDPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 465 LVRTLSVKSGDAISWLSSLGVPLT------VLSQLGGHSRKRTHRApdkADGTpvpiGFTIMQTLEQHVRtklaDR--VT 536
Cdd:PRK07395 83 AVRFLVEQAPEAIASLVEMGVAFDrhgqhlALTLEAAHSRPRVLHA---ADTT----GRAIVTTLTEQVL----QRpnIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 537 IMENTTVTSLLSKSRVRhdgakqvRVYGVEVLQdEGVVSRILADAVILATGGFSndktpnsllQEFAPqlsgfpTTNGPW 616
Cdd:PRK07395 152 IISQALALSLWLEPETG-------RCQGISLLY-QGQITWLRAGAVILATGGGG---------QVFAQ------TTNPAV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 617 ATGDGVKLARELGVKLVDMDKVQLHPTGLIDPKDPanptKYLGPEALRGSGGVLLNKKGERFV------NELDLRSVVSN 690
Cdd:PRK07395 209 STGDGVALAWRAGAQLRDLEFFQFHPTALTKPGAP----RFLISEAVRGEGAHLVDAQGRRFAfdyhpaGELAPRDVVSR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 691 AIieqgdeypdaggskfaFCVLNDAAVKLfgVNSHgfywkrlglfVKADtveklaaLIGCPVENVRntlgdyeqlskenR 770
Cdd:PRK07395 285 AI----------------FSHLQKTATDP--ATAH----------VWLD-------LRPIPAERIR-------------R 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 771 QCPKTRKV-------VYpcvvgpQGPFYVAfvtPSIHYTMGGCLISpsaemqLEENTTSPfghrrpifGLFGAGEVTG-G 842
Cdd:PRK07395 317 RFPNIIRVcqkwgidVF------QEPIPVA---PAAHYWMGGVVTD------LNNQTSIP--------GLYAVGETAStG 373
|
490 500
....*....|....*....|
gi 71400421 843 VHGGNRLGGNSLLECVVFGR 862
Cdd:PRK07395 374 VHGANRLASNSLLECLVFAA 393
|
|
| PRK09077 |
PRK09077 |
L-aspartate oxidase; Provisional |
385-884 |
8.54e-35 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236374 [Multi-domain] Cd Length: 536 Bit Score: 140.82 E-value: 8.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEaTACGAQVILLEKEPKVGGNSAKATSGINGwgtraqaeqdVYDSGKYFE---RDTHKSGlGGST 461
Cdd:PRK09077 11 VLIIGSGAAGLSLALR-LAEHRRVAVLSKGPLSEGSTFYAQGGIAA----------VLDETDSIEshvEDTLIAG-AGLC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 462 DPGLVRTLSVKSGDAISWLSSLGVPLTV-----------LSQLGGHSRKRTHRApdkADGTpvpiGFTIMQTLEQHVRTK 530
Cdd:PRK09077 79 DEDAVRFIAENAREAVQWLIDQGVPFTTdeqangeegyhLTREGGHSHRRILHA---ADAT----GKAVQTTLVERARNH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 531 laDRVTIMENTTVTSLLSKSRVRHDGAkqvRVYGVEVL-QDEGVVSRILADAVILATGGFSNdktpnsllqefAPQLsgf 609
Cdd:PRK09077 152 --PNITVLERHNAIDLITSDKLGLPGR---RVVGAYVLnRNKERVETIRAKFVVLATGGASK-----------VYLY--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 610 pTTNGPWATGDGVKLARELGVKLVDMDKVQLHPTGLIDPkdpaNPTKYLGPEALRGSGGVLLNKKGERFV------NELD 683
Cdd:PRK09077 213 -TTNPDIASGDGIAMAWRAGCRVANMEFNQFHPTCLYHP----QARSFLITEALRGEGAYLKLPDGTRFMpdfderAELA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 684 LRSVVSNAIieqgdeypdaggskfafcvlndaavklfgvnshGFYWKRLGL-FVKADTVEKLAALIGCPVENVrntlgdY 762
Cdd:PRK09077 288 PRDIVARAI---------------------------------DHEMKRLGAdCVYLDISHKPADFIRQHFPTI------Y 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 763 EQL-------SKEnrqcpktrkvvyPCvvgPqgpfyvafVTPSIHYTMGGCLISPSAEMQLEenttspfghrrpifGLFG 835
Cdd:PRK09077 329 ERClelgidiTKE------------PI---P--------VVPAAHYTCGGVMVDLHGRTDLD--------------GLYA 371
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 71400421 836 AGEVT-GGVHGGNRLGGNSLLECVVFGRIAGDRAATILQKKPVPLSFKTW 884
Cdd:PRK09077 372 IGEVSyTGLHGANRMASNSLLECLVYGRSAAEDILSRLPKAPMPPTLPAW 421
|
|
| PRK07804 |
PRK07804 |
L-aspartate oxidase; Provisional |
383-872 |
8.67e-35 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236102 [Multi-domain] Cd Length: 541 Bit Score: 140.88 E-value: 8.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 383 ARVIVVGGGLAGLSAAIEATACGAQVILLEKepkvggnsAKATSGINGWgtrAQ----AEQDVYDSGKYFERDTHKSGlG 458
Cdd:PRK07804 17 ADVVVVGSGVAGLTAALAARRAGRRVLVVTK--------AALDDGSTRW---AQggiaAVLDPGDSPEAHVADTLVAG-A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 459 GSTDPGLVRTLsVKSG-DAISWLSSLG------VPLTV-LSQLGGHSRKRTHRApdKADGTpvpiGFTIMQTLEQHVRtk 530
Cdd:PRK07804 85 GLCDPDAVRSL-VAEGpRAVRELVALGarfdesPDGRWaLTREGGHSRRRIVHA--GGDAT----GAEVQRALDAAVR-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 531 lADRVTIMENTTVTSLLsksrvrHDGAKqvRVYGVEVL-----QDEGVvSRILADAVILATGGfsndktpnsLLQEFAPq 605
Cdd:PRK07804 156 -ADPLDIREHALALDLL------TDGTG--AVAGVTLHvlgegSPDGV-GAVHAPAVVLATGG---------LGQLYAA- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 606 lsgfpTTNGPWATGDGVKLARELGVKLVDMDKVQLHPTGLIDPKDpANPTKYLGPEALRGSGGVLLNKKGERF---VNEL 682
Cdd:PRK07804 216 -----TTNPAGSTGDGVALALRAGAAVSDLEFVQFHPTVLFLGPA-AGGQRPLISEAVRGEGAILVDAQGNRFmagVHPL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 683 -DL--RSVVSNAII----EQGDEypdaggskfafCVLNDAavklfgvnSHGFYWKRlglfvKADTVekLAALIGCPVENV 755
Cdd:PRK07804 290 aDLapRDVVAKAIDrrmkATGDD-----------HVYLDA--------RGIEGFAR-----RFPTI--TASCRAAGIDPV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 756 RNTLgdyeqlskenrqcPktrkvvypcvvgpqgpfyvafVTPSIHYTMGGCLispsaemqleentTSPFGhRRPIFGLFG 835
Cdd:PRK07804 344 RQPI-------------P---------------------VAPAAHYSCGGVV-------------TDVYG-RTSVPGLYA 375
|
490 500 510
....*....|....*....|....*....|....*...
gi 71400421 836 AGEVTG-GVHGGNRLGGNSLLECVVFGRIAGDRAATIL 872
Cdd:PRK07804 376 AGEVACtGVHGANRLASNSLLEGLVVGERAGAAAAAHA 413
|
|
| sdhA |
PRK05945 |
succinate dehydrogenase/fumarate reductase flavoprotein subunit; |
385-878 |
1.77e-32 |
|
succinate dehydrogenase/fumarate reductase flavoprotein subunit;
Pssm-ID: 180319 [Multi-domain] Cd Length: 575 Bit Score: 134.47 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEA--TACGAQVILLEKEPKVGGNSAKATSGIngwgtrAQAEQDV--YDSGKYFERDTHKsglgGS 460
Cdd:PRK05945 6 VVIVGGGLAGCRAALEIkrLDPSLDVAVVAKTHPIRSHSVAAQGGI------AASLKNVdpEDSWEAHAFDTVK----GS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 461 ---TDPGLVRTLSVKSGDAISWLSSLGVPLTVLSQ-------LGGHSRKRTHRAPDKAdgtpvpiGFTIMQTLEQHVRTk 530
Cdd:PRK05945 76 dylADQDAVAILTQEAPDVIIDLEHLGVLFSRLPDgriaqraFGGHSHNRTCYAADKT-------GHAILHELVNNLRR- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 531 laDRVTIMENTTVTSLLsksrVRHDGAKQVRVYGVEvlqdEGVVSRILADAVILATGGFSndKTPNSLLQEFApqlsgfp 610
Cdd:PRK05945 148 --YGVTIYDEWYVMRLI----LEDNQAKGVVMYHIA----DGRLEVVRAKAVMFATGGYG--RVFNTTSNDYA------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 611 ttngpwATGDGVKLARELGVKLVDMDKVQLHPTGLIdpkdpanPTKYLGPEALRGSGGVLLNKKGERFVN-------ELD 683
Cdd:PRK05945 209 ------STGDGLAMTAIAGLPLEDMEFVQFHPTGLY-------PVGVLISEAVRGEGAYLINSEGDRFMAdyapsrmELA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 684 LRSVVSNAI---IEQGDeypdaggskfafcvlndaavklfGVNSHGfywKRLGLFVKADT----VEKLAALIGCPVENVR 756
Cdd:PRK05945 276 PRDITSRAItleIRAGR-----------------------GINPDG---SAGGPFVYLDLrhmgKEKIMSRVPFCWEEAH 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 757 NTLGdyeqlskenrqcpkTRKVVYPCvvgPqgpfyvafVTPSIHYTMGGCLISPSAEMQLEENTTSPfghrrpifGLFGA 836
Cdd:PRK05945 330 RLVG--------------VDAVTEPM---P--------VRPTVHYCMGGIPVNTDGRVRRSADGLVE--------GFFAA 376
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 71400421 837 GEVTG-GVHGGNRLGGNSLLECVVFGRIAGDRAATILQKKPVP 878
Cdd:PRK05945 377 GECACvSVHGANRLGSNSLLECVVYGRRTGAAIAEYVQGRKLP 419
|
|
| PRK08401 |
PRK08401 |
L-aspartate oxidase; Provisional |
384-876 |
3.36e-31 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236259 [Multi-domain] Cd Length: 466 Bit Score: 128.77 E-value: 3.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 384 RVIVVGGGLAGLSAAIEATACGAQVILLEKEPKvGGNSAKATSGI-----NGWGTRAQAeQDVYDSGKYFerdthksglg 458
Cdd:PRK08401 3 KVGIVGGGLAGLTAAISLAKKGFDVTIIGPGIK-KSNSYLAQAGIafpilEGDSIRAHV-LDTIRAGKYI---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 459 gsTDPGLVRTLSVKSGDAISWLSSLGVPLTVLSQLGGHSRKRThrapdkadgtpvpigFTIMQTLEQHVRTKLADRVTIM 538
Cdd:PRK08401 71 --NDEEVVWNVISKSSEAYDFLTSLGLEFEGNELEGGHSFPRV---------------FTIKNETGKHIIKILYKHAREL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 539 ENTTVTSLLSKSRVRHDGAKQVRVYGvEVLQdegvvsrilADAVILATGGFSNdktpnslLQEFapqlsgfpTTNGPWAT 618
Cdd:PRK08401 134 GVNFIRGFAEELAIKNGKAYGVFLDG-ELLK---------FDATVIATGGFSG-------LFKF--------TAGSPLNL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 619 GDGVKLARELGVKLVDMDKVQLHPTGLIDPKDpanptKYLGPEALRGSGGVLLNKKGERFVNELDLRSVVSNAIIEQGDE 698
Cdd:PRK08401 189 GTLIGDAVMKGAPARDLEFVQFHPTGFIGKRG-----TYLISEAVRGAGAKLVTGDGERFVNELETRDIVARAIYRKMQE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 699 ypdagGSkfafcvlndaavklfgvnshgfywkrlGLFVKADTVEKLAaligcpvenvRNTLGDYEQLSKENRQcPKtrKV 778
Cdd:PRK08401 264 -----GK---------------------------GVFLDATGIEDFK----------RRFPQIYAFLRKEGID-PS--RD 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 779 VYPcvvgpqgpfyvafVTPSIHYTMGGCLISPSaemqleenttspfgHRRPIFGLFGAGE-VTGGVHGGNRLGGNSLLEC 857
Cdd:PRK08401 299 LIP-------------VTPIAHYTIGGISVDTF--------------YRTGIKNLYAIGEaASNGFHGANRLASNSLLEC 351
|
490
....*....|....*....
gi 71400421 858 VVFGRiagDRAATILQKKP 876
Cdd:PRK08401 352 IVSGL---EVARTISRERP 367
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
902-1124 |
2.40e-30 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 129.80 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 902 SRVLRFNLPGALQRSGLQLGQFIAIRGEWDGQQLIGYYSPITLPDDLGVIGILAR----------SDKGTLKEWISALEP 971
Cdd:PLN02252 649 VRLFRFALPSEDHVLGLPVGKHVFLCATINGKLCMRAYTPTSSDDEVGHFELVIKvyfknvhpkfPNGGLMSQYLDSLPI 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 972 GDAVEMKG---------CGGLVI--ERRFSerylyfsghalKKLCLIAGGTGVAPMLQIIRAALKKPflENIESIRLIYA 1040
Cdd:PLN02252 729 GDTIDVKGplghieyagRGSFLVngKPKFA-----------KKLAMLAGGTGITPMYQVIQAILRDP--EDKTEMSLVYA 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1041 AEDVSELTYRELLEHHQRDSKGKFRSIFVLNRP-PPIWTDGVGFIDKKLLSSSVQPPAKDLLVAICGPPIM-QRVVKTCL 1118
Cdd:PLN02252 796 NRTEDDILLREELDRWAAEHPDRLKVWYVVSQVkREGWKYSVGRVTEAMLREHLPEGGDETLALMCGPPPMiEFACQPNL 875
|
....*.
gi 71400421 1119 KSLGYD 1124
Cdd:PLN02252 876 EKMGYD 881
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
385-870 |
5.85e-30 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 127.07 E-value: 5.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGIngwgtrAQAEQDVY--DSGKYFERDTHKSGlGGSTD 462
Cdd:PRK07803 11 VVVIGAGGAGLRAAIEARERGLRVAVVCKSLFGKAHTVMAEGGC------AAAMGNVNpkDNWQVHFRDTMRGG-KFLNN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 463 PGLVRTLSVKSGDAISWLSSLG-----VPLTVLSQ--LGGHSRKRTHRAPDKAdgtpvpiGFTIMQTLEQH-VRTKLAD- 533
Cdd:PRK07803 84 WRMAELHAKEAPDRVWELETYGalfdrTKDGRISQrnFGGHTYPRLAHVGDRT-------GLELIRTLQQKiVSLQQEDh 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 534 --------RVTIMENTTVTSLLSksrvrhDGAKQVRVYGVEVLQDEGVVSRilADAVILATGGFSNdktpnsllqefapq 605
Cdd:PRK07803 157 aelgdyeaRIKVFAECTITELLK------DGGRIAGAFGYWRESGRFVLFE--APAVVLATGGIGK-------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 606 lsGFPTTNGPWA-TGDGVKLARELGVKLVDMDKVQLHPTGLIDPkdpanPT--KYLGPEALRGSGGVLLNKKGERFVNEl 682
Cdd:PRK07803 215 --SFKVTSNSWEyTGDGHALALRAGATLINMEFVQFHPTGMVWP-----PSvkGILVTEGVRGDGGVLKNSEGKRFMFD- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 683 DLRSVVSNAIIEQGDE----YPDAGGSKFAFCVL--------NDAAVKLFGVNSHGfywkrlGLFVkaDTVEKLaaligc 750
Cdd:PRK07803 287 YIPDVFKGQYAETEEEadrwYKDNDNNRRPPELLprdevaraINSEVKAGRGSPHG------GVYL--DIASRL------ 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 751 PVENVRNTLGD-YEQLsKENRQCPKTRKvvyPCVVGPqgpfyvafvtpSIHYTMGGCLISPSAEMqleenTTSPfghrrp 829
Cdd:PRK07803 353 PAEEIKRRLPSmYHQF-KELADVDITKE---PMEVGP-----------TCHYVMGGVEVDPDTGA-----ATVP------ 406
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 71400421 830 ifGLFGAGEVTGGVHGGNRLGGNSLLECVVFGRIAGDRAAT 870
Cdd:PRK07803 407 --GLFAAGECAGGMHGSNRLGGNSLSDLLVFGRRAGLGAAD 445
|
|
| sdhA |
PRK06452 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
385-874 |
7.01e-29 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 180567 [Multi-domain] Cd Length: 566 Bit Score: 123.07 E-value: 7.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGINGWgtrAQAEQDVYDSGKYFERDTHKSGlGGSTDPG 464
Cdd:PRK06452 8 AVVIGGGLAGLMSAHEIASAGFKVAVISKVFPTRSHSAAAEGGIAAY---IPGNSDPNDNPDYMTYDTVKGG-DYLVDQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 465 LVRTLSVKSGDAISWLSSLGVPLT-------VLSQLGGHSRKRTHRAPDKAdgtpvpiGFTIMQTLEQHVRTKLADRVTi 537
Cdd:PRK06452 84 AAELLSNKSGEIVMLLERWGALFNrqpdgrvAVRYFGGQTYPRTRFVGDKT-------GMALLHTLFERTSGLNVDFYN- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 538 mENTTVTSLLSKSRVRhdgakqvrvyGVEVLQDEGVVSRIL-ADAVILATGGFSndktpnsLLQEFapqlsgfpTTNGPW 616
Cdd:PRK06452 156 -EWFSLDLVTDNKKVV----------GIVAMQMKTLTPFFFkTKAVVLATGGMG-------MLYRH--------TTNSYI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 617 ATGDGVKLARELGVKLVDMDKVQLHPTGLIdpkdpanPTKYLGPEALRGSGGVLLNKKGERFV-----NELDL--RSVVS 689
Cdd:PRK06452 210 NTGDGFGIALRAGAALKDPEFVQFHPTALY-------PSDVLISEAARGEGGILKNVKGERFMtkyapKKLDLapRDIVS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 690 NAI---IEQGDEYPdAGGSKFAFCVLNDAAVKlfgvnshgfywKRLGLFVKAdtveklaaligcpvenvrntlgdyeqlS 766
Cdd:PRK06452 283 RAIiteIREGRGFP-GGYVGLDLTHLGEEYIK-----------ERLALAVEA---------------------------A 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 767 KENRQCPKTRKVVyPcvvgpqgpfyvafVTPSIHYTMGGclispsaeMQLEENTTSPfghrrPIFGLFGAGEVTG-GVHG 845
Cdd:PRK06452 324 KSFAGVDAFTEPI-P-------------VRPAQHYYMGG--------IDVDIDGRNP-----DIVGLFSAGEAACvSVHG 376
|
490 500
....*....|....*....|....*....
gi 71400421 846 GNRLGGNSLLECVVFGRIAGDRAATILQK 874
Cdd:PRK06452 377 ANRLGSNSLLDTLVFGQVTGRTVVQFLKS 405
|
|
| PRK09231 |
PRK09231 |
fumarate reductase flavoprotein subunit; Validated |
494-869 |
4.32e-28 |
|
fumarate reductase flavoprotein subunit; Validated
Pssm-ID: 236421 [Multi-domain] Cd Length: 582 Bit Score: 120.89 E-value: 4.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 494 GGHSRKRTHRAPDKAdgtpvpiGFTIMQTLEQhvrtkladrvtimenttvTSLLSKSRVR-----------HDGakqvRV 562
Cdd:PRK09231 117 GGMKIERTWFAADKT-------GFHMLHTLFQ------------------TSLKYPQIQRfdehfvldilvDDG----HV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 563 YGVEVL-QDEGVVSRILADAVILATGGfsndktpnsllqefAPQLSGFpTTNGPWATGDGVKLARELGVKLVDMDKVQLH 641
Cdd:PRK09231 168 RGLVAMnMMEGTLVQIRANAVVMATGG--------------AGRVYRY-NTNGGIVTGDGMGMAYRHGVPLRDMEFVQYH 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 642 PTGLidpkdPAnpTKYLGPEALRGSGGVLLNKKGERFVNELDLrsvvsnaiieqGDEYPdAGGSKFAFCVLN--DaavKL 719
Cdd:PRK09231 233 PTGL-----PG--SGILMTEGCRGEGGILVNKDGYRYLQDYGL-----------GPETP-LGEPKNKYMELGprD---KV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 720 fgvnSHGFY--WKrlglfvKADTVEklaaligcpvenvrNTLGDYEQL-------SKENRQCPKTRKV------VYPcVV 784
Cdd:PRK09231 291 ----SQAFWheWR------KGNTIS--------------TPRGDVVYLdlrhlgeKKLHERLPFICELakayvgVDP-VK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 785 GPQgPfyvafVTPSIHYTMGGCLISPSAEMqleenttspfghrrPIFGLFGAGEVTG-GVHGGNRLGGNSLLECVVFGRI 863
Cdd:PRK09231 346 EPI-P-----VRPTAHYTMGGIETDQNCET--------------RIKGLFAVGECSSvGLHGANRLGSNSLAELVVFGRV 405
|
....*.
gi 71400421 864 AGDRAA 869
Cdd:PRK09231 406 AGEQAA 411
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
903-1122 |
9.23e-27 |
|
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99778 [Multi-domain] Cd Length: 223 Bit Score: 109.46 E-value: 9.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 903 RVLRFNLPGALQrsgLQLGQFIAIRGEWDGQQLIGYYSPITLPDDLGVIGIL-ARSDKGTLKEWISALEPGDAVEMKGCG 981
Cdd:cd00322 11 RLFRLQLPNGFS---FKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTvKIVPGGPFSAWLHDLKPGDEVEVSGPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 982 GlvierrFSERYLYFSGHALkklcLIAGGTGVAPMLQIIRAALKKpflENIESIRLIYAAEDVSELTYRELLEHHQRDsK 1061
Cdd:cd00322 88 G------DFFLPLEESGPVV----LIAGGIGITPFRSMLRHLAAD---KPGGEITLLYGARTPADLLFLDELEELAKE-G 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71400421 1062 GKFRSIFVLNRPPPIWTDGVGFIDKKLLSSSVQPPAKDLLVAICGPPIMQRVVKTCLKSLG 1122
Cdd:cd00322 154 PNFRLVLALSRESEAKLGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLG 214
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
883-1130 |
1.24e-25 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 106.41 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 883 TWTTVILREVREggmYGTGSRVLRFNLPGALQRSGLQLGQFIAIRGEWDGQQLIGYYSPITLPDD----LGVIgilaRSD 958
Cdd:COG1018 2 GFRPLRVVEVRR---ETPDVVSFTLEPPDGAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDgrleITVK----RVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 959 KGTLKEWI-SALEPGDAVEMKG-CGGLVIERRFSERYLyfsghalkklcLIAGGTGVAPMLQIIRAALKkpfLENIESIR 1036
Cdd:COG1018 75 GGGGSNWLhDHLKVGDTLEVSGpRGDFVLDPEPARPLL-----------LIAGGIGITPFLSMLRTLLA---RGPFRPVT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1037 LIYAAEDVSELTYRELLEHHQRDSkGKFRSIFVLNRPPPIWTdgvGFIDKKLLSSSVQPPAKDlLVAICGPPIMQRVVKT 1116
Cdd:COG1018 141 LVYGARSPADLAFRDELEALAARH-PRLRLHPVLSREPAGLQ---GRLDAELLAALLPDPADA-HVYLCGPPPMMEAVRA 215
|
250
....*....|....
gi 71400421 1117 CLKSLGYDMQLVRT 1130
Cdd:COG1018 216 ALAELGVPEERIHF 229
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
385-878 |
1.05e-24 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 110.23 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGI---NGWGTRAQAEQDVYDSGK-YFERDTHKSGLGGS 460
Cdd:PRK12844 9 VVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGSTAMSGGVLwlpNNPLMKAAGVPDSHEDALaYLDAVVGDQGPASS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 461 TDPglvRTLSVKSGDA-ISWLSSLGVPLTVL-------SQL-GGHSRKRTHRAP------------------DKADGTPV 513
Cdd:PRK12844 89 PER---REAYLRAGPAmVSFLEHQGMRFARCegwsdyyPDLpGGEARGRSLEAKpfdarklgpwfdrlnppmATPPGTVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 514 --------------PIGFT-----IMQTLEQHVRTK-----------------LADRVTIMENTTVTSLlsksrVRHDGa 557
Cdd:PRK12844 166 mtdeykwlqlikrtPRGMRtaarvGARTLAARIRGQklltngaaligrmleaaLAAGVPLWTNTPLTEL-----IVEDG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 558 kqvRVYGVEVLQDeGVVSRILA-DAVILATGGFSNDKtpnSLLQEFAPQLSGFPTTNG-PWATGDGVKLARELGVKLVDM 635
Cdd:PRK12844 240 ---RVVGVVVVRD-GREVLIRArRGVLLASGGFGHNA---EMRKRYQPQPNSGDWTNAnPGDTGEVIEAAMRLGAALDLM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 636 DKVQLHPTGLIdPKDPANPTKYLGPEALRGSggVLLNKKGERFVNEldlrsvvSNAIIEQG------DEYPdaggskfAF 709
Cdd:PRK12844 313 DEAWWVPGAPL-PNGGPRPYMHNSERSKPGS--IIVDRAGRRFVNE-------AGSYMEVGramyaqDAVP-------AW 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 710 CVLNDAAVK--LFGVNSHGFY---WKRLGLFVKADTVEKLAALIGCPVENVRNTLGDYEQLSKE---------------- 768
Cdd:PRK12844 376 MIMDSRYRKryLFGTIPPGPTpqeWLDSGYMKRADTIEELAGKTGIDPAGLAATVERFNGFAATgtdpdfhrgesaydry 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 769 -----NRQCPKTRKVVYPcvvgpqgPFYVAFVTPSIHYTMGGCLISPSAEMqLEEnttspfgHRRPIFGLFGAGEVTGGV 843
Cdd:PRK12844 456 ygdptNKPNPSLGPLDKP-------PFYAVRMVPGDVGTSGGLLTDEHARV-LRE-------DGSVIPGLYATGNCTASV 520
|
570 580 590
....*....|....*....|....*....|....*.
gi 71400421 844 HGGNRLG-GNSLLECVVFGRIAGDRAATILQKKPVP 878
Cdd:PRK12844 521 MGRTYPGaGASIGNSFVFGYIAALHAAGARSADPPP 556
|
|
| PTZ00319 |
PTZ00319 |
NADH-cytochrome B5 reductase; Provisional |
902-1123 |
5.58e-24 |
|
NADH-cytochrome B5 reductase; Provisional
Pssm-ID: 173521 [Multi-domain] Cd Length: 300 Bit Score: 103.76 E-value: 5.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 902 SRVLRFNLPGALQRSGLQLGQFIAIRGEWDG----QQLIGYYSPITLPDDLGVIGILAR----------SDKGTLKEWIS 967
Cdd:PTZ00319 48 TFIFRFALHSPTQRLGLPIGQHIVFRCDCTTpgkpETVQHSYTPISSDDEKGYVDFLIKvyfkgvhpsfPNGGRLSQHLY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 968 ALEPGDAVEMKGCGGLVIERRFSERYLYFSGHALK-----KLCLIAGGTGVAPMLQIIRAALKKPflENIESIRLIYAAE 1042
Cdd:PTZ00319 128 HMKLGDKIEMRGPVGKFEYLGNGTYTVHKGKGGLKtmhvdAFAMIAGGTGITPMLQIIHAIKKNK--EDRTKVFLVYANQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1043 DVSELTYRELLEHHQRDSkgKFRSIFVLNRP-PPIWTDGVGFIDKKLLSSSVQPPA------KDLLVAICGPPIM-QRVV 1114
Cdd:PTZ00319 206 TEDDILLRKELDEAAKDP--RFHVWYTLDREaTPEWKYGTGYVDEEMLRAHLPVPDpqnsgiKKVMALMCGPPPMlQMAV 283
|
....*....
gi 71400421 1115 KTCLKSLGY 1123
Cdd:PTZ00319 284 KPNLEKIGY 292
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
385-869 |
1.30e-22 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 103.65 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKAtsgiNGW--------GTRAQAEQDV--------------Y 442
Cdd:PRK06134 15 VLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGTTAWS----GGWmwiprnplARRAGIVEDIeqprtylrhelgarY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 443 DSGK-------------YFERDTHKSGLGG-------STDPGLV---RTLSVKSGDAI---SWLSSLGVPLTVLSQLGG- 495
Cdd:PRK06134 91 DAARidafleagphmvaFFERHTALRFADGnaipdyhGDTPGAAtggRSLIAAPFDGRelgALLERLRKPLRETSFMGMp 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 496 ---------------------HSRKRTHR-APDKA---DGTPVPIGFTIMQTLEQHVRtklaDR-VTIMENTTVTSLLsk 549
Cdd:PRK06134 171 imagadlaaflnptrsfraflHVARRFARhLIDLArhgRGMHLVNGNALVARLLKSAE----DLgVRIWESAPARELL-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 550 srvRHDGakqvRVYGVEVLQDEGVVsRILAD-AVILATGGFSNDktpNSLLQEFAPqlsGFPTTNGPWA------TGDGV 622
Cdd:PRK06134 245 ---REDG----RVAGAVVETPGGLQ-EIRARkGVVLAAGGFPHD---PARRAALFP---RAPTGHEHLSlpppgnSGDGL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 623 KLARELGVKLVD--MDKVQLHPTGLIDPKDPANPT-KYLGPEALRGSGGVLLNkkGERFVNELDLRSVVSNAIIEQGdeY 699
Cdd:PRK06134 311 RLGESAGGVVATdlASPVAWAPVSLVPHADGSVGHfPHIIERGKPGLIGVLAN--GKRFVNEADSYHDYVAAMFAAT--P 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 700 PDAGGSKFAFCvlndaavklfgvnSHGFYWK-----------------RLGLFVKADTVEKLAALIGCPVENVRNTLGDY 762
Cdd:PRK06134 387 PGQPVRSWLIC-------------DHRFLRRyglghirpaplplgpyvRSGYLKRGASLEELARACGIDPDGLEATVARY 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 763 EQLSKENR-------QCPKTRKVVYPCVVGP--------QGPFYVAFVTPSIHYTMGGCLISPSAEMqLEEnttspfgHR 827
Cdd:PRK06134 454 NRHARNGQdpdfgrgSTPYNRKQGDPAHGGPnpcvapieHGPFYAVKVLPGCLGTFAGLKTDADARV-LDQ-------AG 525
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 71400421 828 RPIFGLFGAG----EVTGGVHGGnrlGGNSLLECVVFGRIAGDRAA 869
Cdd:PRK06134 526 QPIPGLYAAGndmaSVMGGFYPS---GGITLGPALTFGYIAGRHIA 568
|
|
| PTZ00139 |
PTZ00139 |
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional |
386-879 |
4.27e-22 |
|
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional
Pssm-ID: 240286 [Multi-domain] Cd Length: 617 Bit Score: 102.51 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 386 IVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGINGwgTRAQAEQDVYdsgKYFERDTHKSG--LGgstDP 463
Cdd:PTZ00139 33 VVVGAGGAGLRAALGLVELGYKTACISKLFPTRSHTVAAQGGINA--ALGNMTEDDW---RWHAYDTVKGSdwLG---DQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 464 GLVRTLSVKSGDAISWLSSLGVPLTVLSQ-------LGGHSRK-----RTHRAPDKADGTpvpiGFTIMQTLeqhVRTKL 531
Cdd:PTZ00139 105 DAIQYMCREAPQAVLELESYGLPFSRTKDgkiyqraFGGQSLKfgkggQAYRCAAAADRT----GHAMLHTL---YGQSL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 532 ADRVTIMENTTVTSLLsksrVRHDGakqvRVYGVEVL-QDEGVVSRILADAVILATGGFSNdktpnsllqefapqlSGFP 610
Cdd:PTZ00139 178 KYDCNFFIEYFALDLI----MDEDG----ECRGVIAMsMEDGSIHRFRAHYTVIATGGYGR---------------AYFS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 611 TTNGPWATGDGVKLARELGVKLVDMDKVQLHPTGLIdpkdpanPTKYLGPEALRGSGGVLLNKKGERF-------VNELD 683
Cdd:PTZ00139 235 CTSAHTCTGDGGAMVSRAGLPLQDLEFVQFHPTGIY-------GAGCLITEGCRGEGGILRNSEGERFmeryaptAKDLA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 684 LRSVVSNAI---IEQGDeypdaggskfafcvlndaavklfgvnshgfywkrlGLFVKADTVekLAALIGCPVENVRNTLG 760
Cdd:PTZ00139 308 SRDVVSRAMtieILEGR-----------------------------------GCGPNKDHI--YLDLTHLPPETLHERLP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 761 DYEQLSKenrqcpktrkvVYPCVVGPQGPfyvAFVTPSIHYTMGGCLISPSAEMQleenTTSPFGHRRPIFGLFGAGEV- 839
Cdd:PTZ00139 351 GISETAK-----------IFAGVDVTKEP---IPVLPTVHYNMGGIPTNWKTQVL----TQRNGDDDKIVPGLLAAGEAa 412
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 71400421 840 TGGVHGGNRLGGNSLLECVVFGRIAGDRAATILQK--KPVPL 879
Cdd:PTZ00139 413 CASVHGANRLGANSLLDIVVFGRAAANTVMEILKPgrPQPDL 454
|
|
| sdhA_Bsu |
TIGR01811 |
succinate dehydrogenase or fumarate reductase, flavoprotein subunit, Bacillus subtilis ... |
385-865 |
9.47e-22 |
|
succinate dehydrogenase or fumarate reductase, flavoprotein subunit, Bacillus subtilis subgroup; This model represents the succinate dehydrogenase flavoprotein subunit as found in the low-GC Gram-positive bacteria and a few other lineages. This enzyme may act in a complete or partial TCA cycle, or act in the opposite direction as fumarate reductase. In some but not all species, succinate dehydrogenase and fumarate reductase may be encoded as separate isozymes. [Energy metabolism, TCA cycle]
Pssm-ID: 130870 [Multi-domain] Cd Length: 603 Bit Score: 101.08 E-value: 9.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVG-GNSAKATSGINGwgtrAQAEQDVYDSGKYFERDTHKSGLGGSTDP 463
Cdd:TIGR01811 1 VIVVGTGLAGGMAAAKLAELGYHVKLFSYVDAPRrAHSIAAQGGING----AVNTKGDGDSPWRHFDDTVKGGDFRARES 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 464 GlVRTLSVKSGDAISWLSSLGVP-------LTVLSQLGGHSRKRTHRApdkaDGTpvpIGFTIMQTLEQHVRTKLAD-RV 535
Cdd:TIGR01811 77 P-VKRLAVASPEIIDLMDAMGVPfareyggLLDTRSFGGVQVSRTAYA----RGQ---TGQQLLLALDSALRRQIAAgLV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 536 TIMENTTVTSLLSKSRVRHDGAkqvrvygveVLQD--EGVVSRILADAVILATGGFSNdktpnsllqefapqlSGFPTTN 613
Cdd:TIGR01811 149 EKYEGWEMLDIIVVDGNRARGI---------IARNlvTGEIETHSADAVILATGGYGN---------------VFGKSTN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 614 GPWATGDGVKLARELGVKLVDMDKVQLHPTGLidPKDPANPTKY-LGPEALRGSGGVLLNKKGERFVNELDLRSVVSNAI 692
Cdd:TIGR01811 205 AMNSNASAAWRAYEQGAYFANPEFIQIHPTAI--PVDGTWQSKLrLMSESLRNDGRIWTPKEKNDNRDPNTIPEDKRDYF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 693 IEQgdEYPDAG-------GSKFAFCVLNDAavKLFGVNSHGFYW------KRLGlfvKADTVEKLAALIGCpvenvrntl 759
Cdd:TIGR01811 283 LER--RYPAFGnlvprdiASRAIFQVCDAG--KGVGPGENAVYLdfsdadERLG---RKEIDAKYGNLFEM--------- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 760 gdYEQLSKENrqcpkTRKVvypcvvgpqgPFYVAfvtPSIHYTMGGCLISpsaemqLEENTTSPfghrrpifGLFGAGEV 839
Cdd:TIGR01811 347 --YEKFTGDD-----PYKV----------PMRIF---PAVHYTMGGLWVD------YDQMTNIP--------GLFAAGEC 392
|
490 500
....*....|....*....|....*.
gi 71400421 840 TGGVHGGNRLGGNSLLECVVFGRIAG 865
Cdd:TIGR01811 393 DFSQHGANRLGANSLLSAIADGYFAL 418
|
|
| PRK08626 |
PRK08626 |
fumarate reductase flavoprotein subunit; Provisional |
385-873 |
6.98e-21 |
|
fumarate reductase flavoprotein subunit; Provisional
Pssm-ID: 181507 [Multi-domain] Cd Length: 657 Bit Score: 98.51 E-value: 6.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGING-WGTRAQAEQDVYDSgkYFErDTHKsglgGS--- 460
Cdd:PRK08626 8 ALVIGAGLAGLRVAIAAAQRGLDTIVLSLVPAKRSHSAAAQGGMQAsLGNAVKGEGDNEDV--HFA-DTVK----GSdwg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 461 TDPGLVRTLSVKSGDAISWLSSLGVPLTVLSQ----------------------------LGGHSRKRTHRApdkADGTp 512
Cdd:PRK08626 81 CDQEVARMFVHTAPKAVRELAAWGVPWTRVTAgprtvvingekvtitekeeahglinardFGGTKKWRTCYT---ADGT- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 513 vpiGFTIMQTLEQHVrtkLADRVTIMENTTVTSLLsksrvrHDGAkqvRVYGVeVLQD--EGVVSRILADAVILATGGFS 590
Cdd:PRK08626 157 ---GHTMLYAVDNEA---IKLGVPVHDRKEAIALI------HDGK---RCYGA-VVRCliTGELRAYVAKATLIATGGYG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 591 NdktpnsLLQEfapqlsgfpTTNGPWATGDGVKLARELGV-KLVDMDKVQLHPTGLIdpkdpanPTKYLGPEALRGSGGV 669
Cdd:PRK08626 221 R------IYKV---------TTNAVICEGIGAAIALETGVaPLGNMEAVQFHPTAIV-------PSGILVTEGCRGDGGL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 670 LLNKKGERFV-------NELDLRSVVSNAIIEqgdeypdaggskfafcvlndaavklfgvnsHgfywKRLGLFVKADTVE 742
Cdd:PRK08626 279 LRDKDGYRFMpdyepekKELASRDVVSRRMTE------------------------------H----IRKGKGVKSPYGP 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 743 KLAALIgcpvenvrNTLGDyEQLSKenrqcpKTRKVVYPCV----VGPQGPFyvAFVTPSIHYTMGGClispsaemqlee 818
Cdd:PRK08626 325 HLWLDI--------RILGR-KHIET------NLREVQEICEnflgIDPAKDW--IPVRPTQHYSMGGI------------ 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 71400421 819 nTTSPFGHRRPIFGLFGAGEVT-GGVHGGNRLGGNSLLECVVFGRIAGDRAATILQ 873
Cdd:PRK08626 376 -RTNPTGESYGLKGLFSAGEAAcWDMHGFNRLGGNSLAETVVAGMIVGKYVADFCL 430
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
385-876 |
2.13e-19 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 93.60 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSakATSGINGW--GTRAQAEQDVYDSG----------------- 445
Cdd:PRK12842 12 VLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGTT--AFSGGVLWipGNPHAREAGVADSReaartylkhetgaffda 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 446 --------------KYFERDT-----------HKSGLGGSTDPGlvRTLSVKSGDAISW---LSSLGVPLTVLSQLGG-- 495
Cdd:PRK12842 90 aaveafldngpemvEFFERETevkfvptlypdYHPDAPGGVDIG--RSILAAPYDIRGLgkdMARLRPPLKTITFIGMmf 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 496 HSRK-------RTHRAPDKA------------------DGTPVPIGFTIMQTLeqhVRTKLADRVTIMENTTVTSLLSKS 550
Cdd:PRK12842 168 NSSNadlkhffNATRSLTSFiyvakrlathlkdlalyrRGTQVTSGNALAARL---AKSALDLGIPILTGTPARELLTEG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 551 RvrhdgakqvRVYGVEVlQDEGVVSRILAD-AVILATGGFSNDktPNSLLQEF------APQLSGFPTTNgpwaTGDGVK 623
Cdd:PRK12842 245 G---------RVVGARV-IDAGGERRITARrGVVLACGGFSHD--LARIARAYphlargGEHLSPVPAGN----TGDGIR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 624 LARELGVKL----------VDMDKVqlhPTGlidpkdpaNPTKYLGPEAL-RGSGGVL-LNKKGERFVNELDLRSVVSNA 691
Cdd:PRK12842 309 LAEAVGGAVdirfpdaaawMPVSKV---PLG--------GGRTGVFPHLLdRYKPGVIgVLRNGKRFTNESNSYHDVGAA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 692 IIEQGDEYPDAGgskfAFCVLNDAAVKLFGVnshGF---------YWKRLGLFVKADTVEKLAALIGCPVENVRNTLGDY 762
Cdd:PRK12842 378 MIRACEGQKETA----MWLICDRATLRKYGL---GYakpapmpvgPLLRNGYLIKGDTLAELAGKAGIDAAGLEATVRRY 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 763 EQ-------------LSKENRQCPKTRKVVYPCvVGP--QGPFYVAFVTPSIHYTMGGCLISPSAEMqleentTSPFGhr 827
Cdd:PRK12842 451 NEgavkgidpafgrgSTSFNRYLGDPDHKPNPC-VAPigSGPFYAVKVIMGDLGTFDGLRTDVTGEV------LDADG-- 521
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 71400421 828 RPIFGLFGAGEVTGGVHGGNRLG-GNSLLECVVFGRIAGDRAATILQKKP 876
Cdd:PRK12842 522 TPIAGLYAVGNDRASIMGGNYPGaGITLGPIMTFGYITGRHLAGVAGGRK 571
|
|
| NAD_binding_1 |
pfam00175 |
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
1006-1115 |
1.31e-18 |
|
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.
Pssm-ID: 425503 [Multi-domain] Cd Length: 109 Bit Score: 82.31 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1006 LIAGGTGVAPMLQIIRAALKKPflENIESIRLIYAAEDVSELTYRELLEHHQRDSKGKFRSIFVLNRPPPIWTDGVGFID 1085
Cdd:pfam00175 1 MIAGGTGIAPVRSMLRAILEDP--KDPTQVVLVFGNRNEDDILYREELDELAEKHPGRLTVVYVVSRPEAGWTGGKGRVQ 78
|
90 100 110
....*....|....*....|....*....|
gi 71400421 1086 KKLLSSSVQPPAKDLLVAICGPPIMQRVVK 1115
Cdd:pfam00175 79 DALLEDHLSLPDEETHVYVCGPPGMIKAVR 108
|
|
| PLN00128 |
PLN00128 |
Succinate dehydrogenase [ubiquinone] flavoprotein subunit |
570-919 |
6.83e-18 |
|
Succinate dehydrogenase [ubiquinone] flavoprotein subunit
Pssm-ID: 177739 [Multi-domain] Cd Length: 635 Bit Score: 89.15 E-value: 6.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 570 DEGVVSRILADAVILATGGFSNdktpnsllqefapqlSGFPTTNGPWATGDGVKLARELGVKLVDMDKVQLHPTGLIDpk 649
Cdd:PLN00128 230 EDGTLHRFRAHSTILATGGYGR---------------AYFSATSAHTCTGDGNAMVARAGLPLQDLEFVQFHPTGIYG-- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 650 dpanpTKYLGPEALRGSGGVLLNKKGERFVN-------ELDLRSVVSNAIIEQGDEYPDAGGSK-FAFCVLNDAAVKLFG 721
Cdd:PLN00128 293 -----AGCLITEGSRGEGGILRNSEGERFMEryaptakDLASRDVVSRSMTMEIREGRGVGPEKdHIYLHLNHLPPEVLK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 722 vnshgfywKRLglfvkADTVEKLAALIGCPVenvrntlgdyeqlSKEnrQCPktrkvvypcvvgpqgpfyvafVTPSIHY 801
Cdd:PLN00128 368 --------ERL-----PGISETAAIFAGVDV-------------TKE--PIP---------------------VLPTVHY 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 802 TMGGClisPSAEMQlEENTTSPFGHRRPIFGLFGAGEVT-GGVHGGNRLGGNSLLECVVFGRIAGDRAATILQ----KKP 876
Cdd:PLN00128 399 NMGGI---PTNYHG-EVVTIKGDDPDAVVPGLMAAGEAAcASVHGANRLGANSLLDIVVFGRACANRVAEIAKpgekQKP 474
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 71400421 877 VPLSFKTWTTVILREVReggmYGTGSrvlrfnLPGALQRSGLQ 919
Cdd:PLN00128 475 LPKDAGEKTIAWLDKLR----NANGS------LPTSKIRLNMQ 507
|
|
| FNR_iron_sulfur_binding_3 |
cd06217 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
903-1130 |
3.19e-17 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99813 [Multi-domain] Cd Length: 235 Bit Score: 82.31 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 903 RVLRFNLPGALQrSGLQLGQFIAIRGEW-DGQQLIGYYSPITLPDDLGVIGI-LARSDKGTLKEWI-SALEPGDAVEMKG 979
Cdd:cd06217 17 KTFRLAVPDGVP-PPFLAGQHVDLRLTAiDGYTAQRSYSIASSPTQRGRVELtVKRVPGGEVSPYLhDEVKVGDLLEVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 980 CGGlvierrfserYLYFSGHALKKLCLIAGGTGVAPMLQIIRAALkkpFLENIESIRLIYAAEDVSELTYRELLEHHQRD 1059
Cdd:cd06217 96 PIG----------TFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRR---DLGWPVPFRLLYSARTAEDVIFRDELEQLARR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71400421 1060 SKGKFRSIFVLNRPPPIWTDGVGFIDKKLLSSSVqPPAKDLLVAICGPPIMQRVVKTCLKSLGYDMQLVRT 1130
Cdd:cd06217 163 HPNLHVTEALTRAAPADWLGPAGRITADLIAELV-PPLAGRRVYVCGPPAFVEAATRLLLELGVPRDRIRT 232
|
|
| sdhA |
PRK08641 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
382-870 |
3.75e-17 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236319 [Multi-domain] Cd Length: 589 Bit Score: 86.57 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 382 PARVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGINGwGTRAQAEQDvyDSGKYFErDTHKSGLGGST 461
Cdd:PRK08641 3 KGKVIVVGGGLAGLMATIKAAEAGVHVDLFSLVPVKRSHSVCAQGGING-AVNTKGEGD--SPWIHFD-DTVYGGDFLAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 462 DPGlVRTLSVKSGDAISWLSSLGVP-------LTVLSQLGGHSRKRTHRApdkadgtpvpiGFTIMQTL-----EQHVRT 529
Cdd:PRK08641 79 QPP-VKAMCEAAPGIIHLLDRMGVMfnrtpegLLDFRRFGGTLHHRTAFA-----------GATTGQQLlyaldEQVRRY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 530 KLADRVTIMENTTVTSLlsksrvrhdgakqvrvygveVLQDEGVVSRILA-------------DAVILATGGfsndktpn 596
Cdd:PRK08641 147 EVAGLVTKYEGWEFLGA--------------------VLDDEGVCRGIVAqdlftmeiesfpaDAVIMATGG-------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 597 sllqefaPQLSGFPTTNGPWATGDGVKLARELGVKLVDMDKVQLHPTGLidpkdPANPTKYLGPEALRGSGG-VLLNKKG 675
Cdd:PRK08641 199 -------PGIIFGKSTNSTINTGSAASRVYQQGAYYANGEFIQIHPTAI-----PGDDKLRLMSESARGEGGrVWTYKDG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 676 ER--FVNELdlrsvvsnaiieqgdeYPDAGGskfafCVLND-AAVKLFGVNSHgfywKRLGL----FVKADTVEKlaali 748
Cdd:PRK08641 267 KPwyFLEEK----------------YPAYGN-----LVPRDiATREIFDVCVE----QKLGIngenMVYLDLSHK----- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 749 gcPVENVRNTLGD----YEQLSKENrqcPktRKVvypcvvgPQGPFyvafvtPSIHYTMGGclispsAEMQLEENTTSPf 824
Cdd:PRK08641 317 --DPKELDIKLGGileiYEKFTGDD---P--RKV-------PMKIF------PAVHYSMGG------LWVDYDQMTNIP- 369
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 71400421 825 ghrrpifGLFGAGEVTGGVHGGNRLGGNSLLECVVFGRIAGDRAAT 870
Cdd:PRK08641 370 -------GLFAAGECDYSYHGANRLGANSLLSAIYGGMVAGPNAVE 408
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
385-878 |
1.30e-16 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 84.79 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSakATSGINGW--GTRAQAEQDVYDS---GKYFERDThksgLGG 459
Cdd:PRK12843 19 VIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTT--ATSAGTTWipGTRHGLAVGPDDSleaARTYLDAL----VGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 460 STDPGLVRTLSVKSGDAISWLS--------SLGVPLTVLSQLGGHSRKRTHRAPDKADG-----------TPVPiGFTIM 520
Cdd:PRK12843 93 RSPEELRDAFLASGPRAIAFLEansevkfrAYASHPDYESDLPGATLRGRALEPLPFDGrklgadfalirPPIP-EFTVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 521 ---------------------------QTLEQHVRTKLADR-----------------------VTIMENTTVTSLlsks 550
Cdd:PRK12843 172 ggmmvdrtdvghllaltkswrafrhavRLLARYARDRISYArgtrlvmgnaligrllyslrargVRILTQTDVESL---- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 551 RVRHDgakqvRVYGVEVLQDeGVVSRILAD-AVILATGGFSNDKTpnsLLQEFAPQLSGFPTTNGPWATGDGVKLARELG 629
Cdd:PRK12843 248 ETDHG-----RVIGATVVQG-GVRRRIRARgGVVLATGGFNRHPQ---LRRELLPAAVARYSPGAPGHTGAAIDLALDAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 630 VKLV--DMDKVQLHPTGLIDPKDPAN---PTKYLGpealRGSGGVL-LNKKGERFVNELDLRSVVSNAIIEQGDEYPdag 703
Cdd:PRK12843 319 ARYGrgLLSNAFWAPVSVRRRADGSTavfPHFYLD----RGKPGTIaVNQQGRRFVNESTSYHLFGTAMFAAGKTSP--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 704 gSKFAFCVLNDAAVKLFGV------NSHGFYWKRLGLFVKADTVEKLAALIGCPVENVRNTLGDYEQLSKE--------- 768
Cdd:PRK12843 392 -GIPAYLITDAEFLRKYGLgmvrpgGRGLAPFLRDGYLTVASTLDELAPKLGIDPAALAATVQRHNQYARTgidpdfgrg 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 769 ----NRQCPKTRKVVYPCvVGP--QGPFYVAFVTPSIHYTMGGCLISPSAEMqLEENttspfghRRPIFGLFGAGEVTGG 842
Cdd:PRK12843 471 atayQRMNGDAMIGPNPN-LGPieTAPFYAVRLYPGDIGAATGLVTDASARV-LNAD-------GQPISGLYACGNDMAS 541
|
570 580 590
....*....|....*....|....*....|....*..
gi 71400421 843 VHGGNRLGGNSLL-ECVVFGRIAGDRAATILQKKPVP 878
Cdd:PRK12843 542 IMGGTYPGPGITLgPAIVFAYLAARHAAKRTLARRAA 578
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
385-869 |
4.62e-16 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 82.95 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGnsAKATSGINGWGTR---AQAEQDVYDS-----------GKYFER 450
Cdd:PRK12839 11 VVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGG--ATAWSGGWMWTPGnslARADGVVEDKeeprtylehrlGENYDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 451 DTHKSGLGGStdPGLVRTLSVKSgdAISWLS-------------------SLGVPLTVLSQLGGHSRKRTHR-------- 503
Cdd:PRK12839 89 DKVDALLDGA--PEMVDFFEKKT--ALQFVPgakiadiygdlpgagtghrSVGPKPVNLRKLGPDVAALLRHqlyetsfl 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 504 ------APDKA---DGTPVPIGF--------TIMQTLEQHVR-------TKLADR---------VTIMENTTVTSLLSKS 550
Cdd:PRK12839 165 gmgimaGPDLQaflHATQDPKGFvhaarrviVHMWDLATHRRgmqlvngTALTGRllrsaddlgVDLRVSTSATSLTTDK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 551 rvrhDGakqvRVYGVEVLQDEGVVSRILADAVILATGGFSNDKtpnSLLQEFAPQLsgfPTTNGPWA------TGDGVKL 624
Cdd:PRK12839 245 ----NG----RVTGVRVQGPDGAVTVEATRGVVLATGGFPNDV---DRRKELFPRT---PTGREHWTlapaetTGDGISL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 625 ARELGVKLVDMDK--VQLHPTGLIDPKDPANPT-KYLGPEALRGSGGVLLNkkGERFVNELDLRSVVSNAIIEQGDEypd 701
Cdd:PRK12839 311 AESVGARLDRDLAspAAWCPVSLVPYRNGKVGTfPHIMDRGKPGSIGVLAT--GKRFVNEANGYYDYTLAMVKAAPE--- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 702 aGGSKFAFCVLNDAAVKLFGVNSHG------FYWKRLGLFVKADTVEKLAALIGCPVENVRNTLGDYEQLSKENrQCPKT 775
Cdd:PRK12839 386 -GEPVCSWLIADSRFVRKYPLGMAKplpvplTPYLRSGYLTRGRTIEELAEKCGIDPAGLEATVAEFNENARDG-EDPEF 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 776 RKVVYPCVVG---------------PQGPFYVAFVTPSIHYTMGGcLISPSAEMQLEEnttspfgHRRPIFGLFGAGEVT 840
Cdd:PRK12839 464 GRGTTPFNRGsgdpdngpnpslaplEKGPFYAVKVVPGSFGTFAG-LVADGKSRVLRD-------DDTPIDGLYAAGNDQ 535
|
570 580 590
....*....|....*....|....*....|
gi 71400421 841 GGVHGGNR-LGGNSLLECVVFGRIAGDRAA 869
Cdd:PRK12839 536 ASVMGGHYpSGGINLGPAMTFGYIAGRELA 565
|
|
| PA_degradation_oxidoreductase_like |
cd06214 |
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ... |
902-1130 |
4.25e-15 |
|
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation oxidoreductase. PA oxidoreductases of E. coli hydroxylate PA-CoA in the second step of PA degradation. Members of this group typically fuse a ferredoxin reductase-like domain with an iron-sulfur binding cluster domain. Ferredoxins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal portion may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99810 [Multi-domain] Cd Length: 241 Bit Score: 76.04 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 902 SRVLRFNLPGALQ-RSGLQLGQFIAIRGEWDGQQLIGYYSPITLPDDLGV-IGIlARSDKGTLKEWI-SALEPGDAVEMK 978
Cdd:cd06214 16 AVSITFDVPEELRdAFRYRPGQFLTLRVPIDGEEVRRSYSICSSPGDDELrITV-KRVPGGRFSNWAnDELKAGDTLEVM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 979 GCGGlvierRFSERYLYFSGHalkkLCLIAGGTGVAPMLQIIRAALKKpflENIESIRLIYAAEDVSELTYRELLEHHQR 1058
Cdd:cd06214 95 PPAG-----RFTLPPLPGARH----YVLFAAGSGITPVLSILKTALAR---EPASRVTLVYGNRTEASVIFREELADLKA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71400421 1059 DSKGKFRSIFVLNRPPPIWTDGVGFIDKKLLSSSVQ---PPAKDLLVAICGPPIMQRVVKTCLKSLGYDMQLVRT 1130
Cdd:cd06214 163 RYPDRLTVIHVLSREQGDPDLLRGRLDAAKLNALLKnllDATEFDEAFLCGPEPMMDAVEAALLELGVPAERIHR 237
|
|
| NADH_quinone_reductase |
cd06188 |
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ... |
965-1122 |
4.43e-15 |
|
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain of this group typically contains an iron-sulfur cluster binding domain.
Pssm-ID: 99785 [Multi-domain] Cd Length: 283 Bit Score: 76.96 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 965 WISALEPGDAVEMKGcgglvierRFSErylYFSGHALKKLCLIAGGTGVAPMLQIIRAALKKpfLENIESIRLIYAAEDV 1044
Cdd:cd06188 125 YIFNLKPGDKVTASG--------PFGE---FFIKDTDREMVFIGGGAGMAPLRSHIFHLLKT--LKSKRKISFWYGARSL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1045 SELTYRELLEHHQRDSKgKFRSIFVLNRPPPI--WTDGVGFIDKKLLS--SSVQPPAKDLLVAICGPPIMQRVVKTCLKS 1120
Cdd:cd06188 192 KELFYQEEFEALEKEFP-NFKYHPVLSEPQPEdnWDGYTGFIHQVLLEnyLKKHPAPEDIEFYLCGPPPMNSAVIKMLDD 270
|
..
gi 71400421 1121 LG 1122
Cdd:cd06188 271 LG 272
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
385-870 |
6.05e-15 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 79.31 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGI----NGWGTRAQAEQDVYDSGKYFerdthKSGLGGS 460
Cdd:PRK07843 10 VVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGSTARSGGGVwipnNEVLKRAGVPDTPEAARTYL-----HSIVGDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 461 TDPGLVRTLSVKSGDAISWL---SSLGV----------PLTVLSQLGGHSRKrthraPDKADG--------------TPV 513
Cdd:PRK07843 85 VPPERIDAYLDRGPEMLSFVlahSPLKLcwvpgysdyyPEAPGGRPGGRSIE-----PKPFDArklgadlagleppyGKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 514 PIGFTIMQ-------TLEQHVR-----TKLADR------------------------------VTIMENTTVTSLlsksr 551
Cdd:PRK07843 160 PLNMVVMQqdyvwlnLLKRHPRgvlraLKVGARtlwakatgknllgmgqalaaglriglqragVPVLLNTPLTDL----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 552 VRHDGakqvRVYGVEVLQDEgvvSRILADA---VILATGGFSNDKtpnSLLQEFAPQLSGFPTTNGPWA-TGDGVKLARE 627
Cdd:PRK07843 235 YVEDG----RVTGVHAAESG---EPQLIRArrgVILASGGFEHNE---QMRAKYQRAPIGTEWTVGAKAnTGDGILAGEK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 628 LGVKLVDMDKVQLHPTGLIdpkdPANPTKYLgpeALRGS-GGVLLNKKGERFVNELDLRSVVSNAIIeqGDEYPDAGGSK 706
Cdd:PRK07843 305 LGAALDLMDDAWWGPTIPL----PGGPWFAL---SERNLpGSIIVNMSGKRFMNESAPYVEAVHHMY--GGEYGQGPGPG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 707 fafcvLNDAAVKLFGVNSHGFY--------------WKRLGLFVKADTVEKLAALIGCPVENVRNTLGDYEQLSKENRQC 772
Cdd:PRK07843 376 -----ENIPAWLVFDQRYRDRYlfaglqprqpipsrWLESGVIVKADTLAELAAKIGVPADALTATVQRFNGFARSGVDE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 773 PKTRKV-VY------------PCvVGP--QGPFYVAFVTPSIHYTMGGCLISPSAEMQLEENTtspfghrrPIFGLFGAG 837
Cdd:PRK07843 451 DFHRGEsAYdryygdptnkpnPN-LGElsHAPFYAAKMVPGDLGTKGGLRTDVRGRVLRDDGS--------VIEGLYAAG 521
|
570 580 590
....*....|....*....|....*....|....
gi 71400421 838 EVTGGVHGGNRLG-GNSLLECVVFGRIAGDRAAT 870
Cdd:PRK07843 522 NVSAPVMGHTYAGpGATIGPAMTFGYLAALDIAA 555
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
921-1122 |
1.79e-14 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 74.51 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 921 GQFIAIRgeWDGQQLIGYYSPITLPDDLGVIGILAR-SDKGTlkEWISALEPGDAVEMKG-CG-GLVIErrfserylyfs 997
Cdd:COG0543 29 GQFVMLR--VPGDGLRRPFSIASAPREDGTIELHIRvVGKGT--RALAELKPGDELDVRGpLGnGFPLE----------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 998 gHALKKLCLIAGGTGVAPMLQIIRAALKKPfleniESIRLIYAAEDVSELTYRELLEhhqrdSKGKFRSIFVLNRPppiW 1077
Cdd:COG0543 94 -DSGRPVLLVAGGTGLAPLRSLAEALLARG-----RRVTLYLGARTPEDLYLLDELE-----ALADFRVVVTTDDG---W 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 71400421 1078 TDGVGFIDKKLLssSVQPPAKDLLVAICGPPIMQRVVKTCLKSLG 1122
Cdd:COG0543 160 YGRKGFVTDALK--ELLAEDSGDDVYACGPPPMMKAVAELLLERG 202
|
|
| sulfite_reductase_like |
cd06221 |
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ... |
960-1126 |
2.06e-14 |
|
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.
Pssm-ID: 99817 [Multi-domain] Cd Length: 253 Bit Score: 74.57 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 960 GTLKEWISALEPGDAVEMKGCGGlvieRRFSERYLYfsGHalkKLCLIAGGTGVAPMLQIIRAALKKPflENIESIRLIY 1039
Cdd:cd06221 66 GRVTEALHELKPGDTVGLRGPFG----NGFPVEEMK--GK---DLLLVAGGLGLAPLRSLINYILDNR--EDYGKVTLLY 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1040 AAEDVSELTYRELLEHHQRdsKGKFRSIFVLNRPPPIWTDGVGFIDKKLLSSSVQPpaKDLLVAICGPPIMQRVVKTCLK 1119
Cdd:cd06221 135 GARTPEDLLFKEELKEWAK--RSDVEVILTVDRAEEGWTGNVGLVTDLLPELTLDP--DNTVAIVCGPPIMMRFVAKELL 210
|
....*..
gi 71400421 1120 SLGYDMQ 1126
Cdd:cd06221 211 KLGVPEE 217
|
|
| FNR_iron_sulfur_binding_1 |
cd06215 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
969-1126 |
4.40e-12 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99811 [Multi-domain] Cd Length: 231 Bit Score: 67.23 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 969 LEPGDAVEMKGCGGlvierRFserylYFSGHALKKLCLIAGGTGVAPMLQIIRAALKkpfLENIESIRLIYAAEDVSELT 1048
Cdd:cd06215 81 LKVGDELWASGPAG-----EF-----TLIDHPADKLLLLSAGSGITPMMSMARWLLD---TRPDADIVFIHSARSPADII 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1049 YR-ELLEHHQRDSkgKFRSIFVLNRP-PPIWTDGVGFIDKKLLSSSVqPPAKDLLVAICGP-PIMQrVVKTCLKSLGYDM 1125
Cdd:cd06215 148 FAdELEELARRHP--NFRLHLILEQPaPGAWGGYRGRLNAELLALLV-PDLKERTVFVCGPaGFMK-AVKSLLAELGFPM 223
|
.
gi 71400421 1126 Q 1126
Cdd:cd06215 224 S 224
|
|
| FNR_iron_sulfur_binding |
cd06191 |
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
903-1130 |
8.04e-12 |
|
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR was intially identified as a chloroplast reductase activity catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methnae assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99788 [Multi-domain] Cd Length: 231 Bit Score: 66.40 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 903 RVLRFNLPGALQRsGLQLGQFIAIRGEWDGQQLIGYYSpITLPDDLGVIGI-LARSDKGTLKEWISA-LEPGDAVEMKGC 980
Cdd:cd06191 14 VTIVFAVPGPLQY-GFRPGQHVTLKLDFDGEELRRCYS-LCSSPAPDEISItVKRVPGGRVSNYLREhIQPGMTVEVMGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 981 GG-LVIERRFSERYLyfsghalkklcLIAGGTGVAPMLQIIRAALKkpfLENIESIRLIYAAEDVSELTYRELLEhHQRD 1059
Cdd:cd06191 92 QGhFVYQPQPPGRYL-----------LVAAGSGITPLMAMIRATLQ---TAPESDFTLIHSARTPADMIFAQELR-ELAD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71400421 1060 SKGKFRSIFVLNR--PPPIWTDGVGFIDKKLLSSSVqPPAKDLLVAICGPPIMQRVVKTCLKSLGYDMQLVRT 1130
Cdd:cd06191 157 KPQRLRLLCIFTRetLDSDLLHGRIDGEQSLGAALI-PDRLEREAFICGPAGMMDAVETALKELGMPPERIHT 228
|
|
| FNR1 |
cd06195 |
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ... |
921-1134 |
8.56e-12 |
|
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99792 [Multi-domain] Cd Length: 241 Bit Score: 66.43 E-value: 8.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 921 GQFIAIR-GEWDGQQLIGYYSPITLPDD--LGVIGILARSdkGTLKEWISALEPGDAVEM-KGCGG-LVIERRFSERYLY 995
Cdd:cd06195 28 GQFTKLGlPNDDGKLVRRAYSIASAPYEenLEFYIILVPD--GPLTPRLFKLKPGDTIYVgKKPTGfLTLDEVPPGKRLW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 996 fsghalkklcLIAGGTGVAPMLQIIRAALKKpflENIESIRLIYAAEDVSELTYRELLEHHQRDSKGKFRSIFVLNRPPP 1075
Cdd:cd06195 106 ----------LLATGTGIAPFLSMLRDLEIW---ERFDKIVLVHGVRYAEELAYQDEIEALAKQYNGKFRYVPIVSREKE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71400421 1076 IW------TDgvgFIDKKLLSSSV--QPPAKDLLVAICGPPIMQRVVKTCLKSLGYDMQLVRTVDEV 1134
Cdd:cd06195 173 NGaltgriPD---LIESGELEEHAglPLDPETSHVMLCGNPQMIDDTQELLKEKGFSKNHRRKPGNI 236
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
386-634 |
9.91e-12 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 68.15 E-value: 9.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 386 IVVGGGLAGLSAAIEATACGAQVILLEKEPKVGgnsAK-ATSGiNGwG---TRAQAEQDVYdsgKYFERDTH--KSGLgg 459
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG---RKiLISG-GG-RcnfTNSEPLPEFL---NYYGGNPHflKSAL-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 460 stdpglvRTLSVKsgDAISWLSSLGVPLTVlsqlgGHSRK---RTHRAPDkadgtpvpigftIMQTLEQHVRtklADRVT 536
Cdd:COG2081 71 -------SRFTPE--DLIAFFEGLGIETKE-----ESSGRvfpDSSKASD------------ILRALLAELR---EAGVE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 537 IMENTTVTSLLsksrvRHDGAKQVRVygvevlqDEGVVsrILADAVILATGGFSndktpnsllqefAPQLsGfpttngpw 616
Cdd:COG2081 122 IRLRTRVTGIE-----KEDGGFGVET-------PDGET--VRADAVVLATGGLS------------YPKL-G-------- 166
|
250
....*....|....*...
gi 71400421 617 ATGDGVKLARELGVKLVD 634
Cdd:COG2081 167 STGDGYRLAEQFGHTITP 184
|
|
| FAD_binding_6 |
pfam00970 |
Oxidoreductase FAD-binding domain; |
903-979 |
1.04e-11 |
|
Oxidoreductase FAD-binding domain;
Pssm-ID: 425968 [Multi-domain] Cd Length: 99 Bit Score: 62.21 E-value: 1.04e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71400421 903 RVLRFNLPGALQRSGLQLGQFIAIRGEWDGQQLIGYYSPITLPDDLGVIGILARSDK-GTLKEWISALEPGDAVEMKG 979
Cdd:pfam00970 15 RIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVYPgGKMSQYLDELKIGDTIDFKG 92
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
384-643 |
1.26e-11 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 67.99 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 384 RVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGgnsAKAtsGINGWG----TRAQAEQDVYDSGKYFERDTHKSGLgg 459
Cdd:pfam03486 2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG---RKI--LISGGGrcnvTNLSEEPDNFLSRYPGNPKFLKSAL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 460 stdpglvRTLSvkSGDAISWLSSLGVPLTVLSqLGghsrkRTHRAPDKADgtpvpigfTIMQTLEQhvrtKLADR-VTIM 538
Cdd:pfam03486 75 -------SRFT--PWDFIAFFESLGVPLKEED-HG-----RLFPDSDKAS--------DIVDALLN----ELKELgVKIR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 539 ENTTVTSLLSKSrvrhDGAKQVRVYGvevlqdegvvSRILADAVILATGGFSndktpnsllqefAPQLSgfpttngpwAT 618
Cdd:pfam03486 128 LRTRVLSVEKDD----DGRFRVKTGG----------EELEADSLVLATGGLS------------WPKTG---------ST 172
|
250 260
....*....|....*....|....*
gi 71400421 619 GDGVKLARELGVKLVDmdkvqLHPT 643
Cdd:pfam03486 173 GFGYPLAEQFGHTIIP-----LRPA 192
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
383-592 |
1.55e-11 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 67.24 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 383 ARVIVVGGGLAGLSAAIEATACGAQVILLEKEPKV----GGNSAKATSGINGWGTRAQAE-----QDVYDSgkyFERDTH 453
Cdd:COG0665 3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGsgasGRNAGQLRPGLAALADRALVRlareaLDLWRE---LAAELG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 454 KSgLGGSTDPGLVRTLSVKSGDAI----SWLSSLGVPLTVLSQLGGHSRKRTHRAPDKADGTPVPIGFTI-----MQTLE 524
Cdd:COG0665 80 ID-CDFRRTGVLYLARTEAELAALraeaEALRALGLPVELLDAAELREREPGLGSPDYAGGLYDPDDGHVdpaklVRALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71400421 525 QHVRtklADRVTIMENTTVTSLlsksrvRHDGAkqvRVYGVEVlqDEGVVSrilADAVILATGGFSND 592
Cdd:COG0665 159 RAAR---AAGVRIREGTPVTGL------EREGG---RVTGVRT--ERGTVR---ADAVVLAAGAWSAR 209
|
|
| O2ase_reductase_like |
cd06187 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
938-1122 |
5.54e-11 |
|
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.
Pssm-ID: 99784 [Multi-domain] Cd Length: 224 Bit Score: 63.77 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 938 YYSPITLPDDLGVIG-ILARSDKGTLKEWI-SALEPGDAVEMKGCGGLVIERRFSERylyfsghalkKLCLIAGGTGVAP 1015
Cdd:cd06187 43 AYSPANPPNEDGEIEfHVRAVPGGRVSNALhDELKVGDRVRLSGPYGTFYLRRDHDR----------PVLCIAGGTGLAP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1016 MLQIIRAALKKPFlENieSIRLIYAAEDVSELTYRELLEHHQRdSKGKFRSIFVLNRPPPIWTDGVGFIDKKLLssSVQP 1095
Cdd:cd06187 113 LRAIVEDALRRGE-PR--PVHLFFGARTERDLYDLEGLLALAA-RHPWLRVVPVVSHEEGAWTGRRGLVTDVVG--RDGP 186
|
170 180
....*....|....*....|....*..
gi 71400421 1096 PAKDLLVAICGPPIMQRVVKTCLKSLG 1122
Cdd:cd06187 187 DWADHDIYICGPPAMVDATVDALLARG 213
|
|
| PRK12837 |
PRK12837 |
FAD-binding protein; |
385-864 |
7.52e-11 |
|
FAD-binding protein;
Pssm-ID: 237222 [Multi-domain] Cd Length: 513 Bit Score: 66.00 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGlAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSG-----INGWGTRAQAEQDVYDSGKYFE--------RD 451
Cdd:PRK12837 10 VLVAGSG-GGVAGAYTAAREGLSVALVEATDKFGGTTAYSGGGgmwfpCNPVLRRAGTDDTIEDALEYYHavvgdrtpRD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 452 THKSGLGGStdPGLVRTLSVKSGDAIS---WLSSLG-------------VPLTVLSQLGGHSRKRThRAPDKAD--GTPV 513
Cdd:PRK12837 89 LQETYVRGG--APLIEYLEQDEHFEFAelpWPDYFGkapkaradgqrhiVPKPLPAAALGELREQI-RGPLDTErlGAPP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 514 PIGFTIMQTLEQHVRTKLAD--RVTIMENTTVTSLlsksrVRHDGakqvRVYGVEVLQDeGVVSRILA-DAVILATGGFS 590
Cdd:PRK12837 166 PDYLVGGRALIGRFLAALARfpNARLRLNTPLVEL-----VVEDG----RVVGAVVERG-GERRRVRArRGVLLAAGGFE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 591 NDKTpnsLLQEFAPQLSGFPTTNGPWATGDGVKLARELGVKLVDMDKVQLHPtGLIDPKDPAnptkylgPEALRGSGGVL 670
Cdd:PRK12837 236 QNDD---MRARYGVPGSARDTMGGPGNTGLAHQAAIAVGADTDLMDQAWWSP-GLTHPDGRS-------AFALWFTGGIF 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 671 LNKKGERFVNELDLRSVVSNAIIEQgdeyPDAGGSKFAFCVLND------AAVKLFGVN-SHGFYWKRLGLFVKADTVEK 743
Cdd:PRK12837 305 VDQHGERFVNESAPYDRLGRAVIAE----MDSGGMTLPFWMIYDdregevPPVKATNVSmVETAQYVAAGLWRTADTLEE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 744 LAALIGCPVENVRNTLGDYEQLSKENRQC-------PKTRKV---VYPCVVGPQGPFYVAFVTPSIHYTMGGclispsae 813
Cdd:PRK12837 381 LAAKIGVPADALTATVARFNGFAAAGVDEdfgrgdeAYDRAFsggASPLVPIDTPPFHAAAFGVSDLGTKGG-------- 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 71400421 814 mqLEENTTSPFGHR--RPIFGLFGAGE----VTGGVHGGnrlGGNSLLECVVFGRIA 864
Cdd:PRK12837 453 --LRTDTAARVLDTdgRPIPGLYAAGNtmaaVSGTTYPG---GGNPIGASMLFSHLA 504
|
|
| FNR_like_1 |
cd06196 |
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ... |
939-1122 |
3.31e-10 |
|
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99793 [Multi-domain] Cd Length: 218 Bit Score: 61.10 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 939 YSPITLPDD--LGVIgILARSDKGTLKEWISALEPGD---------AVEMKGCGglvierrfserylYFsghalkklclI 1007
Cdd:cd06196 50 FTFTSLPEDdvLEFV-IKSYPDHDGVTEQLGRLQPGDtlliedpwgAIEYKGPG-------------VF----------I 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1008 AGGTGVAPMLQIIRAALKKpflENIESIRLIYAAEDVSELTYRELLEHHQRDskgkfRSIFVLNR-PPPIWTDgvGFIDK 1086
Cdd:cd06196 106 AGGAGITPFIAILRDLAAK---GKLEGNTLIFANKTEKDIILKDELEKMLGL-----KFINVVTDeKDPGYAH--GRIDK 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 71400421 1087 KLLSSSVQPPAKDLLVaiCGPPIMQRVVKTCLKSLG 1122
Cdd:cd06196 176 AFLKQHVTDFNQHFYV--CGPPPMEEAINGALKELG 209
|
|
| T4MO_e_transfer_like |
cd06190 |
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ... |
921-1110 |
4.73e-10 |
|
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family.
Pssm-ID: 99787 Cd Length: 232 Bit Score: 61.11 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 921 GQFIAIRGEwdgqQLIGY--YSPITLPDDLGVIG-ILARSDKGTLKEWI-SALEPGDAVEMKGCGGLVIERRFSERylyf 996
Cdd:cd06190 27 GQYALLALP----GVEGAraYSMANLANASGEWEfIIKRKPGGAASNALfDNLEPGDELELDGPYGLAYLRPDEDR---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 997 sghalKKLClIAGGTGVAPMLQIIRAALKKPFLENiESIRLIYAAEDVSELTYRELLEHHqRDSKGKFRSIFVLNRPP-- 1074
Cdd:cd06190 99 -----DIVC-IAGGSGLAPMLSILRGAARSPYLSD-RPVDLFYGGRTPSDLCALDELSAL-VALGARLRVTPAVSDAGsg 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 71400421 1075 --PIWTDGVGFIdKKLLSSSVQPPAKDLLVAICGPPIM 1110
Cdd:cd06190 171 saAGWDGPTGFV-HEVVEATLGDRLAEFEFYFAGPPPM 207
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
385-679 |
7.70e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 62.76 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATAC--GAQVILLEKEP-KVGGNSAKATSGIN-----GWGTraqAEQdvydsgkYFERDTHKSg 456
Cdd:PRK08275 12 ILVIGGGTAGPMAAIKAKERnpALRVLLLEKANvKRSGAISMGMDGLNnavipGHAT---PEQ-------YTKEITIAN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 457 lGGSTDPGLVRTLSVKSGDAISWLSSLGVPLTVlSQLGGHSRKRTHRApdkadGT---PVPIGFTIMQTLEQHVRTKlad 533
Cdd:PRK08275 81 -DGIVDQKAVYAYAEHSFETIQQLDRWGVKFEK-DETGDYAVKKVHHM-----GSyvlPMPEGHDIKKVLYRQLKRA--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 534 RVTIMENTTVTSLLSKSRVRHDGAkqvrvYGVEVLQDEGVVSRilADAVILATGGFSNDKTPNsllqefapqlSG--FPT 611
Cdd:PRK08275 151 RVLITNRIMATRLLTDADGRVAGA-----LGFDCRTGEFLVIR--AKAVILCCGAAGRLGLPA----------SGylFGT 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71400421 612 TNGPWATGDGVKLARELGVKLVDMDKVQLHPtgLI-DPKDPANPTkYLGPealrgSGGVLLNKKGERFV 679
Cdd:PRK08275 214 YENPTNAGDGYAMAYHAGAELANLECFQINP--LIkDYNGPACAY-VTGP-----LGGYTANAKGERFI 274
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
966-1122 |
9.18e-10 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 62.22 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 966 ISALEPGDAVEMKG-CGGLVIERRFSERylyfsghalkKLCLIAGGTGVAPMLQIIRAALKKPFLENieSIRLIYAAEDV 1044
Cdd:COG4097 292 LGRLKPGTRVYVEGpYGRFTFDRRDTAP----------RQVWIAGGIGITPFLALLRALAARPGDQR--PVDLFYCVRDE 359
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71400421 1045 SELTYRELLEHHQRDskgkfRSIFVLNrppPIWTDGVGFIDKKLLSSSVqPPAKDLLVAICGPPIMQRVVKTCLKSLG 1122
Cdd:COG4097 360 EDAPFLEELRALAAR-----LAGLRLH---LVVSDEDGRLTAERLRRLV-PDLAEADVFFCGPPGMMDALRRDLRALG 428
|
|
| flavohem_like_fad_nad_binding |
cd06184 |
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
969-1125 |
1.16e-09 |
|
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.
Pssm-ID: 99781 Cd Length: 247 Bit Score: 60.26 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 969 LEPGDAVEMKG-CGGLVIERrfserylyfsgHALKKLCLIAGGTGVAPMLQIIRAALKKpflENIESIRLIYAAEDVSEL 1047
Cdd:cd06184 91 VKVGDVLEVSApAGDFVLDE-----------ASDRPLVLISAGVGITPMLSMLEALAAE---GPGRPVTFIHAARNSAVH 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1048 TYRELLEHHqRDSKGKFRSIFVLNRP----PPIWTDGVGFIDKKLLSSSVQPPAKDllVAICGPPIMQRVVKTCLKSLGY 1123
Cdd:cd06184 157 AFRDELEEL-AARLPNLKLHVFYSEPeagdREEDYDHAGRIDLALLRELLLPADAD--FYLCGPVPFMQAVREGLKALGV 233
|
..
gi 71400421 1124 DM 1125
Cdd:cd06184 234 PA 235
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
384-423 |
1.75e-09 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 61.80 E-value: 1.75e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 71400421 384 RVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAK 423
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQ 181
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
966-1129 |
1.83e-09 |
|
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99795 [Multi-domain] Cd Length: 216 Bit Score: 59.19 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 966 ISALEPGDAVEMKGCGGlvierRFSerylyfSGHALKKLCLIAGGTGVAPMLQIIRAALKKPfleNIESIRLIYAAEDVS 1045
Cdd:cd06198 71 AERLKPGTRVTVEGPYG-----RFT------FDDRRARQIWIAGGIGITPFLALLEALAARG---DARPVTLFYCVRDPE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1046 ELTYRELLEhhqRDSKGKFRSIFVLNRPPPIWTDGVGFIDKKLlsssvqPPAKDLLVAICGPPIMQRVVKTCLKSLGYDM 1125
Cdd:cd06198 137 DAVFLDELR---ALAAAAGVVLHVIDSPSDGRLTLEQLVRALV------PDLADADVWFCGPPGMADALEKGLRALGVPA 207
|
....
gi 71400421 1126 QLVR 1129
Cdd:cd06198 208 RRFH 211
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
385-876 |
2.63e-09 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 61.36 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGIngW--GTRAQAEQDVYDSG----KYFERDThksglG 458
Cdd:PRK12835 14 VLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGSTALSGGGI--WvpGAPAQRREGYVPDPedvrRYLKQIT-----G 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 459 GSTDPGLVRTLsVKSGDAI--------SWL----------------------SSLGVPLTVLSQLGG---HSRKRTHRAP 505
Cdd:PRK12835 87 GLVSAARLRAY-VDAAPQMmeflenlsPWLefvwkpgyadyypelpggsplgSTINVPPIDLRKLGEdeqHLLPPLALAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 506 --------DKAD---------GTPVPIGF---------------TIMQTLEQHVRTKLADR-VTIMENTTVTSLLsksrV 552
Cdd:PRK12835 166 kgiwftpkDLRLfymvrqtwaGKAVLLKLiwrmvrarvfgrrmaAIGQSLVARLRLALKDAgVPLWLDSPMTELI----T 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 553 RHDGAkqvrVYGVEVlQDEGVVSRILAD-AVILATGGFSNDktpNSLLQEFAPQLSGFPTTNG-PWATGDGVKLARELG- 629
Cdd:PRK12835 242 DPDGA----VVGAVV-EREGRTLRIGARrGVILATGGFDHD---MDWRKEYLPELERKDWSFGnPANTGDGIRAGEKVGa 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 630 -VKLVD----MDKVQlHPTGLIDPkdpanptkYLGPEALRGSggVLLNKKGERFVNE----LDL--------RSVVSNAI 692
Cdd:PRK12835 314 aTDLLDeawwFPAIC-WPDGRMQF--------MLNERMMPAQ--FIVNGAGKRFINEaapyMDFvhamiagqRSGVGHIP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 693 ------IEQGDEYPDAGgskfafcVLNDAAVKLFGVNSHGFY---WKRLGLFVKADTVEKLAALIGCPVENVRNTLGDYE 763
Cdd:PRK12835 383 cwlvtdIRSFSRYVFGG-------HLPIPKIPFAPVPTGRKFpqaWLESGVVKKADTWDELAAKIGVPAENLRATAERFN 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 764 QLSKENRQCPKTR-KVVY------PCVVGP------QGPFYVAFVTPSIHYTMGGCLISPSAEMQLEENTtspfghrrPI 830
Cdd:PRK12835 456 GLARKGHDDDFNRgDSAYdnyygdPTLPNPnldplgKPPYYAFRIELGDLGTSGGLRTDEHARVLREDDS--------VI 527
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 71400421 831 FGLFGAGEVTGGVHGGNRLG-GNSLLECVVFGRIAGDRAATILQKKP 876
Cdd:PRK12835 528 PGLYAVGNTSASVMGRSYAGaGATIGPAMTFGYVAARHAAAVVAAAA 574
|
|
| PRK13800 |
PRK13800 |
fumarate reductase/succinate dehydrogenase flavoprotein subunit; |
385-680 |
3.29e-09 |
|
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
Pssm-ID: 237512 [Multi-domain] Cd Length: 897 Bit Score: 61.40 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEK-EPKVGGNSAKATSGINGWGTRAQAEQDVYDSGKYFERDthksglgGSTDP 463
Cdd:PRK13800 16 VLVIGGGTAGTMAALTAAEHGANVLLLEKaHVRHSGALAMGMDGVNNAVIPGKAEPEDYVAEITRAND-------GIVNQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 464 GLVRTLSVKSGDAISWLSSLGVPLTVlSQLGGHSRKRTHRAPDKAdgTPVPIGFTIMQTLEQHVRTK-LADRVTImENTt 542
Cdd:PRK13800 89 RTVYQTATRGFAMVQRLERYGVKFEK-DEHGEYAVRRVHRSGSYV--LPMPEGKDVKKALYRVLRQRsMRERIRI-ENR- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 543 vtslLSKSRVRHDGAKQVRVYGVEVLQDEGVVSRilADAVILATGGFSNDKTPNSllqefaPQLSGfpTTNGPWATGDGV 622
Cdd:PRK13800 164 ----LMPVRVLTEGGRAVGAAALNTRTGEFVTVG--AKAVILATGPCGRLGLPAS------GYLYG--TYENPTNAGDGY 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71400421 623 KLARELGVKLVDMDKVQLHPtgLIdpKDpanptkYLGPEALRGS---GGVLLNKKGERFVN 680
Cdd:PRK13800 230 SMAYHAGAELSGIECFQINP--LI--KD------YNGPACAYVAnpfGGYQVNAQGERFVD 280
|
|
| NqrF |
COG2871 |
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ... |
965-1122 |
5.57e-09 |
|
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase
Pssm-ID: 442118 [Multi-domain] Cd Length: 396 Bit Score: 59.49 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 965 WISALEPGDAVEMKGCGGlvierRF----SERYLYFsghalkklclIAGGTGVAPMLQIIRAALKKpfLENIESIRLIYA 1040
Cdd:COG2871 236 YIFSLKPGDKVTISGPYG-----EFflrdSDREMVF----------IGGGAGMAPLRSHIFDLLER--GKTDRKITFWYG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1041 AEDVSELTYRELLEHHQRDSKgKFRSIFVLNRPPP--IWTDGVGFIDKKLLSS--SVQPPAKDLLVAICGPPIM-QRVVK 1115
Cdd:COG2871 299 ARSLRELFYLEEFRELEKEHP-NFKFHPALSEPLPedNWDGETGFIHEVLYENylKDHPAPEDCEAYLCGPPPMiDAVIK 377
|
....*..
gi 71400421 1116 TcLKSLG 1122
Cdd:COG2871 378 M-LDDLG 383
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
384-591 |
4.18e-08 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 56.64 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 384 RVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSGI--NGWGTRAQAEQD--VYDSGKYFERDTHKSGLgg 459
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGASGRNAGLihPGLRYLEPSELArlALEALDLWEELEEELGI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 460 stDPGLVRT--LSVKSGDA-------ISWLSSLGVPLTVLSqlGGHSRKRTHRAPDKADGTPVPIGFTI-----MQTLEQ 525
Cdd:pfam01266 79 --DCGFRRCgvLVLARDEEeealeklLAALRRLGVPAELLD--AEELRELEPLLPGLRGGLFYPDGGHVdparlLRALAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71400421 526 HVRtklADRVTIMENTTVTSLlsksrVRHDGAKQVRVYGVevlqdegvvsrilADAVILATGGFSN 591
Cdd:pfam01266 155 AAE---ALGVRIIEGTEVTGI-----EEEGGVWGVVTTGE-------------ADAVVNAAGAWAD 199
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
382-426 |
4.25e-08 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 57.17 E-value: 4.25e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 71400421 382 PARVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGnsaKATS 426
Cdd:COG3349 3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG---RARS 44
|
|
| phenol_2-monooxygenase_like |
cd06211 |
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ... |
903-1121 |
7.22e-08 |
|
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.
Pssm-ID: 99807 Cd Length: 238 Bit Score: 54.64 E-value: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 903 RVLRFNLPGAlQRSGLQLGQFIAIR-GEWDGQQLigyYSPITLPDDLGVIGILAR-SDKGTLKEWI-SALEPGDAVEMKG 979
Cdd:cd06211 22 KGVRLKLDEP-EEIEFQAGQYVNLQaPGYEGTRA---FSIASSPSDAGEIELHIRlVPGGIATTYVhKQLKEGDELEISG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 980 CGGlvierRFserylYFSGHALKKLCLIAGGTGVAPMLQIIRAALKKPFLENiesIRLIYAAEDVSELTYRELLEHHQRD 1059
Cdd:cd06211 98 PYG-----DF-----FVRDSDQRPIIFIAGGSGLSSPRSMILDLLERGDTRK---ITLFFGARTRAELYYLDEFEALEKD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71400421 1060 SKgKFRSIFVLNRPPP--IWTDGVGFID---KKLLSSSVQPPAKDLlvaiCGPPIMqrvVKTCLKSL 1121
Cdd:cd06211 165 HP-NFKYVPALSREPPesNWKGFTGFVHdaaKKHFKNDFRGHKAYL----CGPPPM---IDACIKTL 223
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
382-422 |
1.04e-07 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 55.61 E-value: 1.04e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 71400421 382 PARVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSA 422
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIR 41
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
384-585 |
2.26e-07 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 54.11 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 384 RVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAkatsgingwgTRaQAEQDVYDSG-KYFE-RDTH-KSGLGGS 460
Cdd:COG3380 5 DIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRMA----------TR-RLDGGRFDHGaQYFTaRDPRfQALVEEW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 461 TDPGLVRTlsvksgdaisWlsslgvPLTVLSQLGGHSRKRTHRAPDKADGTPvpiGftiMQTLEQHvrtkLADRVTIMEN 540
Cdd:COG3380 74 LAAGLVAP----------W------TFDFVVLDADGLVSPRDDGEPRYVGVP---G---MNALAKH----LAAGLDVRLG 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 71400421 541 TTVTSLlsksrVRHDGAKQvrvygvevLQDEGVVSRILADAVILA 585
Cdd:COG3380 128 TRVTAL-----ERDGDGWR--------LTDEDGEEYGPFDAVVLA 159
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
385-427 |
3.51e-07 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 54.15 E-value: 3.51e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNsakATSG 427
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM---LTSG 41
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
384-590 |
4.07e-07 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 53.40 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 384 RVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSakATSGINGWGTRAqaeqdvydsgkyFERdthksgLGgstdp 463
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDG--RGIALSPRSLEL------------LRR------LG----- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 464 glvrtlsvkSGDAIswlSSLGVPLTVLSQLGGHSRKRTHRAPdkADGTPVPIGFTIMQT-LEQHVRTKLADR-VTIMENT 541
Cdd:COG0654 60 ---------LWDRL---LARGAPIRGIRVRDGSDGRVLARFD--AAETGLPAGLVVPRAdLERALLEAARALgVELRFGT 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 71400421 542 TVTSLlsksrvrHDGAKQVRVygveVLQDEGVVSrilADAVILATGGFS 590
Cdd:COG0654 126 EVTGL-------EQDADGVTV----TLADGRTLR---ADLVVGADGARS 160
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
921-1122 |
5.72e-07 |
|
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.
Pssm-ID: 99786 [Multi-domain] Cd Length: 224 Bit Score: 51.78 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 921 GQFIAIRGEwDGQQLigYYSPITLPDDLGVIGI-LARSDKGTL-KEWISALEPGDAVEMKGCGGLVIERRFSERylyfsg 998
Cdd:cd06189 29 GQYLDLLLD-DGDKR--PFSIASAPHEDGEIELhIRAVPGGSFsDYVFEELKENGLVRIEGPLGDFFLREDSDR------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 999 halkKLCLIAGGTGVAPMLQIIRAALKKPFlenIESIRLIYAAEDVSELTYRELL----EHHQrdskgKFRSIFVLNRPP 1074
Cdd:cd06189 100 ----PLILIAGGTGFAPIKSILEHLLAQGS---KRPIHLYWGARTEEDLYLDELLeawaEAHP-----NFTYVPVLSEPE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 71400421 1075 PIWTDGVGFIDKKLLSSSVqppakDL---LVAICGPPIMQRVVKTCLKSLG 1122
Cdd:cd06189 168 EGWQGRTGLVHEAVLEDFP-----DLsdfDVYACGSPEMVYAARDDFVEKG 213
|
|
| PTZ00274 |
PTZ00274 |
cytochrome b5 reductase; Provisional |
938-1121 |
6.10e-07 |
|
cytochrome b5 reductase; Provisional
Pssm-ID: 140300 Cd Length: 325 Bit Score: 52.61 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 938 YYSPITLPDDLGVIGILA-RSDKGTLKEWISALEPGDAVEMKGCGglvierrFSERYlyfSGHALKKLCLIAGGTGVAPM 1016
Cdd:PTZ00274 105 FYTPVTANHTKGYFDIIVkRKKDGLMTNHLFGMHVGDKLLFRSVT-------FKIQY---RPNRWKHVGMIAGGTGFTPM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1017 LQIIRAALKKPFLEN-IESIRLIYAAEDVSE--LTYRELLEHHQRDSKGKFRSIFVLNRP--PPIWTDGVGFIDKKLLSS 1091
Cdd:PTZ00274 175 LQIIRHSLTEPWDSGeVDRTKLSFLFCNRTErhILLKGLFDDLARRYSNRFKVYYTIDQAvePDKWNHFLGYVTKEMVRR 254
|
170 180 190
....*....|....*....|....*....|..
gi 71400421 1092 SVQPP-AKDLLVAICGP-PIMQRVVKTCLKSL 1121
Cdd:PTZ00274 255 TMPAPeEKKKIIMLCGPdQLLNHVAGTPMGTM 286
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
384-419 |
6.30e-07 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 53.31 E-value: 6.30e-07
10 20 30
....*....|....*....|....*....|....*.
gi 71400421 384 RVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGG 419
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
383-419 |
9.91e-07 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 52.87 E-value: 9.91e-07
10 20 30
....*....|....*....|....*....|....*....
gi 71400421 383 ARVIVVGGGLAGLSAAIEATACGAQVILLEKEP--KVGG 419
Cdd:COG3573 6 ADVIVVGAGLAGLVAAAELADAGRRVLLLDQEPeaNLGG 44
|
|
| PRK06854 |
PRK06854 |
adenylyl-sulfate reductase subunit alpha; |
385-635 |
1.95e-06 |
|
adenylyl-sulfate reductase subunit alpha;
Pssm-ID: 235879 [Multi-domain] Cd Length: 608 Bit Score: 51.85 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 385 VIVVGGGLAGLSAAIEAT--ACGAQVILLEKEP-KVGGNSAKATSGINGW-GTRAQAEQDVydsgKYFERDThksglggs 460
Cdd:PRK06854 14 ILIIGGGMAGCGAAFEAKewAPDLKVLIVEKANiKRSGAVAQGLSAINAYiGEGETPEDYV----RYVRKDL-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 461 tdPGLVR-----TLSVKSGDAISWLSSLGVPLtvlsqlgghsrkrthraPDKADGTPVPIG-FTIMQTLEQHVR-----T 529
Cdd:PRK06854 82 --MGIVRedlvyDIARHVDSVVHLFEEWGLPI-----------------WKDENGKYVRRGrWQIMINGESYKPivaeaA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 530 KLADRVTIMENTTVTSLLsksrvrHDGAKQVRVYGVEVlqDEGVVSRILADAVILATGGFSNDKTPNSllQEFAPQLSGF 609
Cdd:PRK06854 143 KKALGDNVLNRVFITDLL------VDDNRIAGAVGFSV--RENKFYVFKAKAVIVATGGAAGIYRPRS--PGEGRGRMWY 212
|
250 260
....*....|....*....|....*.
gi 71400421 610 PttngPWATGDGVKLARELGVKLVDM 635
Cdd:PRK06854 213 P----PFNTGSGYAMGIRAGAEMTTF 234
|
|
| FNR_N-term_Iron_sulfur_binding |
cd06194 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
921-1054 |
2.35e-06 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99791 [Multi-domain] Cd Length: 222 Bit Score: 49.96 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 921 GQFIAIRGEwDGqqLIGYYSPITLPDDLGVIGI-LARSDKGTLKEWI-SALEPGDAVEMKGcgglvierrfserylyFSG 998
Cdd:cd06194 27 GQYVNLRRA-GG--LARSYSPTSLPDGDNELEFhIRRKPNGAFSGWLgEEARPGHALRLQG----------------PFG 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71400421 999 HAL-------KKLCLIAGGTGVAPMLQIIRAALkkpFLENIESIRLIYAAEDVSELTYRELLE 1054
Cdd:cd06194 88 QAFyrpeygeGPLLLVGAGTGLAPLWGIARAAL---RQGHQGEIRLVHGARDPDDLYLHPALL 147
|
|
| MMO_FAD_NAD_binding |
cd06210 |
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ... |
921-1122 |
2.42e-06 |
|
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water.
Pssm-ID: 99806 Cd Length: 236 Bit Score: 50.03 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 921 GQFIAIrgEWDGQQLIGYYSPITLPDDLGVIGILAR-SDKGTLKEWI-SALEPGDAVEMKGCGGlvierRFSERylyfsG 998
Cdd:cd06210 38 GQFVEI--EIPGTDTRRSYSLANTPNWDGRLEFLIRlLPGGAFSTYLeTRAKVGQRLNLRGPLG-----AFGLR-----E 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 999 HALKKLCLIAGGTGVAPMLQIIRAAlkKPFLENIESiRLIYAAEDVSELTYRELLEHHQRDSKGkFRSIFVLNRPPPIWT 1078
Cdd:cd06210 106 NGLRPRWFVAGGTGLAPLLSMLRRM--AEWGEPQEA-RLFFGVNTEAELFYLDELKRLADSLPN-LTVRICVWRPGGEWE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 71400421 1079 DGVG-FID--KKLLSSSVQPPakDLLVaiCGPPIMQRVVKTCLKSLG 1122
Cdd:cd06210 182 GYRGtVVDalREDLASSDAKP--DIYL--CGPPGMVDAAFAAAREAG 224
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
387-422 |
4.73e-06 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 45.21 E-value: 4.73e-06
10 20 30
....*....|....*....|....*....|....*.
gi 71400421 387 VVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSA 422
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAY 36
|
|
| PRK10926 |
PRK10926 |
ferredoxin-NADP reductase; Provisional |
921-1119 |
5.70e-06 |
|
ferredoxin-NADP reductase; Provisional
Pssm-ID: 182844 Cd Length: 248 Bit Score: 48.93 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 921 GQFIAIRGEWDGQQLIGYYSPITLPDDLGVIGILARSDKGTLKEWISALEPGDAVEM--KGCGGLVIERRFSerylyfsg 998
Cdd:PRK10926 34 GQFTKLGLEIDGERVQRAYSYVNAPDNPDLEFYLVTVPEGKLSPRLAALKPGDEVQVvsEAAGFFVLDEVPD-------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 999 haLKKLCLIAGGTGVAPMLQIIRAALKkpfLENIESIRLIYAAEDVSELTYRELLEHHQRDSKGKFRSIFVLNR--PPPI 1076
Cdd:PRK10926 106 --CETLWMLATGTAIGPYLSILQEGKD---LERFKNLVLVHAARYAADLSYLPLMQELEQRYEGKLRIQTVVSRetAPGS 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 71400421 1077 WTDGV-GFIDKKLLSSSVQPP--AKDLLVAICGPPIMQRVVKTCLK 1119
Cdd:PRK10926 181 LTGRVpALIESGELEAAVGLPmdAETSHVMLCGNPQMVRDTQQLLK 226
|
|
| PRK12845 |
PRK12845 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
542-869 |
7.03e-06 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237226 [Multi-domain] Cd Length: 564 Bit Score: 50.15 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 542 TVTSLLsksRVRHDGAkqvRVYGVEVLQDEGVVSRILADAVILATGGFSND-----KTPNSLLQEfapQLSGFPTTNgpw 616
Cdd:PRK12845 236 TETSLV---RLTDDGG---RVTGAVVDHRGREVTVTARRGVVLAAGGFDHDmemrwKFQSESLGE---HASLGAEGN--- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 617 aTGDGVKLARELGVKLVDMDKVQLHPTglIDPKDPANPTKYLGPEALRGSggVLLNKKGERFVNE-LDLRSvVSNAIIEQ 695
Cdd:PRK12845 304 -TGDAIRIAQDLGAAIGLMDQAWWFPA--VAPLPGGAPAVMLAERSLPGS--LIVDQTGRRFVNEaTDYMS-FGQRVLER 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 696 gdeyPDAGGSKFAFCVLNDAAVKLFGVNSHGFY--------WKRLGLFVKADTVEKLAALIGCPVENVRNTLGDYEQLSK 767
Cdd:PRK12845 378 ----ERAGDPVESMWIVFDQQYRNSYVFAAELFprmpipqaWYDAGIAHRADSLADLARKIGVPVDTFVATMRRFNEMAA 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 768 EN---------------------RQCPKTRKVVypcvvgpQGPFYVAFVTPSIHYTMGGCLISPSAEMQLEENTtspfgh 826
Cdd:PRK12845 454 AGvdsdfgrgrsaydryygdptvTPNPNLRPLD-------KGPFYAVKMVLSDLGTCGGLRADERARVLREDGS------ 520
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 71400421 827 rrPIFGLFGAGEVTGGVHGGNRLG-GNSLLECVVFGRIAGDRAA 869
Cdd:PRK12845 521 --VIDGLYAIGNTAANAFGATYPGaGATIGQGLVYGYIAAQDAA 562
|
|
| DHOD_e_trans |
cd06218 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ... |
921-1115 |
7.88e-06 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.
Pssm-ID: 99814 [Multi-domain] Cd Length: 246 Bit Score: 48.70 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 921 GQFIAIRGEWDGQQL----IGYYSpITLPDdlGVIGIL-ARSDKGTlkEWISALEPGDAVEMKGCGGlvieRRFSeryly 995
Cdd:cd06218 28 GQFVMLRVPDGSDPLlrrpISIHD-VDPEE--GTITLLyKVVGKGT--RLLSELKAGDELDVLGPLG----NGFD----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 996 fSGHALKKLCLIAGGTGVAPMLQIIRAALKKPFlenieSIRLIYAAEDVSELTYREllehhqrdskgKFRSIFVLNRppp 1075
Cdd:cd06218 94 -LPDDDGKVLLVGGGIGIAPLLFLAKQLAERGI-----KVTVLLGFRSADDLFLVE-----------EFEALGAEVY--- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 71400421 1076 IWTDgVGFIDKK-----LLSSSVQPPAKDLLVAiCGPPIMQRVVK 1115
Cdd:cd06218 154 VATD-DGSAGTKgfvtdLLKELLAEARPDVVYA-CGPEPMLKAVA 196
|
|
| FNR_iron_sulfur_binding_2 |
cd06216 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
917-1113 |
1.18e-05 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99812 [Multi-domain] Cd Length: 243 Bit Score: 47.99 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 917 GLQLGQFIAIRGEWDGQQLIGYYSPITLPDDL-GVIGIL-ARSDKGTLKEWISA-LEPGDAVEM---KGCGGLVIERRfs 990
Cdd:cd06216 45 GHRAGQHVRLGVEIDGVRHWRSYSLSSSPTQEdGTITLTvKAQPDGLVSNWLVNhLAPGDVVELsqpQGDFVLPDPLP-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 991 erylyfsghalKKLCLIAGGTGVAPMLQIIRAALKKPFLENIESIRLIYAAEDV---SELtyRELLEHHQRdskgkFRSI 1067
Cdd:cd06216 123 -----------PRLLLIAAGSGITPVMSMLRTLLARGPTADVVLLYYARTREDVifaDEL--RALAAQHPN-----LRLH 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 71400421 1068 FVLNRPPPIwtdgvGFIDKKLLSSSVqPPAKDLLVAICGPP-IMQRV 1113
Cdd:cd06216 185 LLYTREELD-----GRLSAAHLDAVV-PDLADRQVYACGPPgFLDAA 225
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
377-417 |
1.18e-05 |
|
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.
Pssm-ID: 426165 [Multi-domain] Cd Length: 213 Bit Score: 47.49 E-value: 1.18e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 71400421 377 IAGSLPARVIVVGGGLAGLSAAIEATACGAQVILLEKEPKV 417
Cdd:pfam01262 23 VPGVAPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPAR 63
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
383-419 |
1.54e-05 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 49.13 E-value: 1.54e-05
10 20 30
....*....|....*....|....*....|....*....
gi 71400421 383 ARVIVVGGGLAGLSAAIEATACGAQVILLEKEPK--VGG 419
Cdd:PRK12834 5 ADVIVVGAGLAGLVAAAELADAGKRVLLLDQENEanLGG 43
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
1004-1115 |
2.20e-05 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 45.79 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1004 LCLIAGGTGVAPMLQIIRAALKKPFLENIESIRLIYAAEDVSEL-----TYRELLEHHQR------------DSKGKFRS 1066
Cdd:pfam08030 4 VLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLewfkdVLNELEELKELnieihiyltgeyEAEDASDQ 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71400421 1067 IFVLNRPPPIW--------TDGVGFIDKK------LLSSSVQPPAKDLLVAICGPPIMQRVVK 1115
Cdd:pfam08030 84 SDSSIRSENFDslmnevigVDFVEFHFGRpnwkevLKDIAKQHPNGSIGVFSCGPPSLVDELR 146
|
|
| sdhA |
PRK07573 |
fumarate reductase/succinate dehydrogenase flavoprotein subunit; |
797-861 |
2.98e-05 |
|
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
Pssm-ID: 236054 [Multi-domain] Cd Length: 640 Bit Score: 48.28 E-value: 2.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71400421 797 PSIHYTMGGCLISpsaemqLEENTTSPfghrrpifGLFGAGEVTGGVHGGNRLGGNSLLECVVFG 861
Cdd:PRK07573 400 PAVHYTMGGLWVD------YNLMSTIP--------GLFVIGEANFSDHGANRLGASALMQGLADG 450
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
385-433 |
6.89e-05 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 46.69 E-value: 6.89e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKatsgingWGT 433
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTH-------TGT 49
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
382-419 |
7.73e-05 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 46.45 E-value: 7.73e-05
10 20 30
....*....|....*....|....*....|....*...
gi 71400421 382 PARVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGG 419
Cdd:COG1231 7 GKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
385-431 |
1.09e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 46.04 E-value: 1.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSAKATSgiNGW 431
Cdd:PRK07208 7 VVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTY--KGN 51
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
384-420 |
1.25e-04 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 46.01 E-value: 1.25e-04
10 20 30
....*....|....*....|....*....|....*..
gi 71400421 384 RVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGN 420
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
|
|
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
363-438 |
1.45e-04 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 46.14 E-value: 1.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71400421 363 FEIATDNAEIRKKRIAGSLPARVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSakATSGINGWGTRAQAE 438
Cdd:PLN02328 219 FGVAPVIKEAQLRSFEGVEPANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRV--KTMKMKGDGVVAAAD 292
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
385-419 |
1.57e-04 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 45.11 E-value: 1.57e-04
10 20 30
....*....|....*....|....*....|....*
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKePKVGG 419
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGG 36
|
|
| monooxygenase_like |
cd06212 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
969-1110 |
1.98e-04 |
|
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.
Pssm-ID: 99808 [Multi-domain] Cd Length: 232 Bit Score: 44.24 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 969 LEPGDAVEMKGCGGLVIERRFSERylyfsghalkKLCLIAGGTGVAPMLQIIRAALKKpflENIESIRLIYAAEDVSELT 1048
Cdd:cd06212 81 LAVGDPVTVTGPYGTCTLRESRDR----------PIVLIGGGSGMAPLLSLLRDMAAS---GSDRPVRFFYGARTARDLF 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71400421 1049 YRELLEHHQRDSKGkFRSIFVLNRPPPI--WTDGVGFIDKKLLSSSVQPPAKDllVAICGPPIM 1110
Cdd:cd06212 148 YLEEIAALGEKIPD-FTFIPALSESPDDegWSGETGLVTEVVQRNEATLAGCD--VYLCGPPPM 208
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
376-427 |
3.37e-04 |
|
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;
Pssm-ID: 234978 [Multi-domain] Cd Length: 662 Bit Score: 44.84 E-value: 3.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 71400421 376 RIAGSLPARVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVggnsAKATSG 427
Cdd:PRK01747 254 RPGSPKARDAAIIGGGIAGAALALALARRGWQVTLYEADEAP----AQGASG 301
|
|
| BenDO_FAD_NAD |
cd06209 |
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ... |
1004-1122 |
3.59e-04 |
|
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group.
Pssm-ID: 99805 [Multi-domain] Cd Length: 228 Bit Score: 43.35 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1004 LCLIAGGTGVAP---MLQIIRAALKKPflenieSIRLIYAAEDVSELTYRELLEHHQRDsKGKFRSIFVLNRPPPiWTDG 1080
Cdd:cd06209 105 LLMLAGGTGLAPflsMLDVLAEDGSAH------PVHLVYGVTRDADLVELDRLEALAER-LPGFSFRTVVADPDS-WHPR 176
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 71400421 1081 VGFIDKKLLSSSVQPPAKDllVAICGPPIMQRVVKTCLKSLG 1122
Cdd:cd06209 177 KGYVTDHLEAEDLNDGDVD--VYLCGPPPMVDAVRSWLDEQG 216
|
|
| PRK08345 |
PRK08345 |
cytochrome-c3 hydrogenase subunit gamma; Provisional |
921-1123 |
3.82e-04 |
|
cytochrome-c3 hydrogenase subunit gamma; Provisional
Pssm-ID: 236247 [Multi-domain] Cd Length: 289 Bit Score: 43.64 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 921 GQFI--AIRGewdgqqlIGYYsPITL---PDDLGVIGILARSdKGTLKEWISALEPGDAVEMKG--CGGLVIERrfsery 993
Cdd:PRK08345 41 GQFVqvTIPG-------VGEV-PISIcssPTRKGFFELCIRR-AGRVTTVIHRLKEGDIVGVRGpyGNGFPVDE------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 994 lyFSGHalkKLCLIAGGTGVAPMLQIIRAALKKPFleNIESIRLIYAAEDVSELTYRELLEHHQRDSKGkFRSIFVLNRP 1073
Cdd:PRK08345 106 --MEGM---DLLLIAGGLGMAPLRSVLLYAMDNRW--KYGNITLIYGAKYYEDLLFYDELIKDLAEAEN-VKIIQSVTRD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71400421 1074 PPiwTDGVGFIDKKLLSSSVQPPAKDLLV-----------AICGPPIMQRVVKTCLKSLGY 1123
Cdd:PRK08345 178 PE--WPGCHGLPQGFIERVCKGVVTDLFReantdpkntyaAICGPPVMYKFVFKELINRGY 236
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
384-422 |
3.97e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 44.11 E-value: 3.97e-04
10 20 30
....*....|....*....|....*....|....*....
gi 71400421 384 RVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNSA 422
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAA 39
|
|
| antC |
PRK11872 |
anthranilate 1,2-dioxygenase electron transfer component AntC; |
999-1118 |
4.20e-04 |
|
anthranilate 1,2-dioxygenase electron transfer component AntC;
Pssm-ID: 183350 [Multi-domain] Cd Length: 340 Bit Score: 43.96 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 999 HALKKLCLIAGGTGVAPMLQIIRAALKKPfleNIESIRLIYAAEDVSELTYRELLEHHQRDSKGkFRSIFVLNRPPPIWT 1078
Cdd:PRK11872 207 EVERPLVFVAGGTGLSAFLGMLDELAEQG---CSPPVHLYYGVRHAADLCELQRLAAYAERLPN-FRYHPVVSKASADWQ 282
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 71400421 1079 DGVGFIDKKLLSSSVQPPAKDLLVaiCGPPIMQRVVKTCL 1118
Cdd:PRK11872 283 GKRGYIHEHFDKAQLRDQAFDMYL--CGPPPMVEAVKQWL 320
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
384-419 |
5.27e-04 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 44.07 E-value: 5.27e-04
10 20 30
....*....|....*....|....*....|....*...
gi 71400421 384 RVIVVGGGLAGLSAA--IEATACGAQVILLEKEPKVGG 419
Cdd:PRK11883 2 KVAIIGGGITGLSAAyrLHKKGPDADITLLEASDRLGG 39
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
372-513 |
6.17e-04 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 43.86 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 372 IRKKRIAGSLPARVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGGNsakatsgingwgtraqaeqdVYDSGKYFERD 451
Cdd:PLN03000 174 IKDKFPAQSSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGR--------------------VYTKKMEANRV 233
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71400421 452 THKSGLGGSTDPGlvrtlsvksgdaiswlsSLGVPLTVLS-QLGGHSRKRTHRAP-DKADGTPV 513
Cdd:PLN03000 234 GAAADLGGSVLTG-----------------TLGNPLGIIArQLGSSLYKVRDKCPlYRVDGKPV 280
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
384-415 |
6.78e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 43.08 E-value: 6.78e-04
10 20 30
....*....|....*....|....*....|..
gi 71400421 384 RVIVVGGGLAGLSAAIEATACGAQVILLEKEP 415
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEG 33
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
385-419 |
6.91e-04 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 43.54 E-value: 6.91e-04
10 20 30
....*....|....*....|....*....|....*
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILLEKEpKVGG 419
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKG-RLGG 39
|
|
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
1006-1069 |
7.13e-04 |
|
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.
Pssm-ID: 99783 [Multi-domain] Cd Length: 210 Bit Score: 42.29 E-value: 7.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71400421 1006 LIAGGTGVAPMLQIIRAALKKPFLEN-IESIRLIYAAEDVSELT-YRELLEHHQRDSKGKFRSIFV 1069
Cdd:cd06186 111 LVAGGSGITFVLPILRDLLRRSSKTSrTRRVKLVWVVRDREDLEwFLDELRAAQELEVDGEIEIYV 176
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
377-415 |
9.10e-04 |
|
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.
Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 42.78 E-value: 9.10e-04
10 20 30
....*....|....*....|....*....|....*....
gi 71400421 377 IAGSLPARVIVVGGGLAGLSAAIEATACGAQVILLEKEP 415
Cdd:cd05305 163 VPGVPPAKVVILGAGVVGENAARVALGLGAEVTVLDINL 201
|
|
| oxygenase_e_transfer_subunit |
cd06213 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
960-1110 |
1.02e-03 |
|
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate while mono-oxygenases add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.
Pssm-ID: 99809 Cd Length: 227 Bit Score: 41.91 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 960 GTLKEWI-SALEPGDAVEMKGCGGlvierRFSERylyfSGHAlkKLCLIAGGTGVAPML----QIIRAALKKPFLenies 1034
Cdd:cd06213 69 GAFSGWLfGADRTGERLTVRGPFG-----DFWLR----PGDA--PILCIAGGSGLAPILaileQARAAGTKRDVT----- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 1035 irLIYAAEDVSELTYRELLEHHQRDSKGKFRSIFVLNRPPP--IWTDGVGFIDKKLlsssvqppAKDLLVA----ICGPP 1108
Cdd:cd06213 133 --LLFGARTQRDLYALDEIAAIAARWRGRFRFIPVLSEEPAdsSWKGARGLVTEHI--------AEVLLAAteayLCGPP 202
|
..
gi 71400421 1109 IM 1110
Cdd:cd06213 203 AM 204
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
385-411 |
1.06e-03 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 42.92 E-value: 1.06e-03
10 20
....*....|....*....|....*..
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILL 411
Cdd:pfam01134 2 VIVIGGGHAGCEAALAAARMGAKVLLI 28
|
|
| PRK10461 |
PRK10461 |
thiamine biosynthesis lipoprotein ApbE; Provisional |
188-322 |
1.19e-03 |
|
thiamine biosynthesis lipoprotein ApbE; Provisional
Pssm-ID: 182478 Cd Length: 350 Bit Score: 42.43 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 188 DLGGVSKGYIVDYVVERLNAAGIVDVYFEWGGDCRASGTNARRTPWMVGIIRPPSLEQlrnppkdpSYIRVLPLNDEALC 267
Cdd:PRK10461 182 DLSTVGEGYAADHLARLMEQEGISRYLVSVGGALSSRGMNGEGQPWRVAIQKPTDKEN--------AVQAVVDINGHGIS 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 71400421 268 TSGDYENLTEGSNKKLYTSIFDWKKRsllePVESELAQVSIRCYSAMYADALATA 322
Cdd:PRK10461 254 TSGSYRNYYELDGKRLSHVIDPQTGR----PIEHNLVSVTVIAPTALEADGWDTG 304
|
|
| CYPOR_like_FNR |
cd06208 |
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ... |
1004-1075 |
1.40e-03 |
|
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but lack the FAD-binding region connecting sub-domain. Ferredoxin-NADP+ reductase (FNR) is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins, such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2, which then transfers two electrons and a proton to NADP+ to form NADPH. CYPOR serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases, sulfite reducatase, and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal FNR-like FAD and NAD binding module, an FMN-binding domain, and an additional connecting domain (inserted within the FAD binding region) that orients the FNR and FMN -binding domains. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99804 [Multi-domain] Cd Length: 286 Bit Score: 41.92 E-value: 1.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71400421 1004 LCLIAGGTGVAPMlqiiRAALKKPFLENIESIR------LIYAAEDVSELTYRELLEHHQRDSKGKFRSIFVLNRPPP 1075
Cdd:cd06208 138 LIMIATGTGIAPF----RSFLRRLFREKHADYKftglawLFFGVPNSDSLLYDDELEKYPKQYPDNFRIDYAFSREQK 211
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
385-411 |
2.40e-03 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 41.76 E-value: 2.40e-03
10 20
....*....|....*....|....*..
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILL 411
Cdd:PRK05329 5 VLVIGGGLAGLTAALAAAEAGKRVALV 31
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
384-419 |
3.24e-03 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 41.30 E-value: 3.24e-03
10 20 30
....*....|....*....|....*....|....*.
gi 71400421 384 RVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGG 419
Cdd:PRK12810 145 KVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
385-428 |
3.30e-03 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 41.28 E-value: 3.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 71400421 385 VIVVGGGLAGLSAAIE-ATACGAQVILLEKEPKVGGNSAKATSGI 428
Cdd:COG0579 7 VVIIGAGIVGLALARElSRYEDLKVLVLEKEDDVAQESSGNNSGV 51
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
370-419 |
3.30e-03 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 41.32 E-value: 3.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71400421 370 AEIRKKRIAgslparviVVGGGLAGLSAAIEATACGAQVILLEKEPKVGG 419
Cdd:PRK11749 136 APKTGKKVA--------VIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
382-417 |
5.18e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 38.64 E-value: 5.18e-03
10 20 30
....*....|....*....|....*....|....*.
gi 71400421 382 PARVIVVGGGLAGLSAAIEATACGAQVILLEKEPKV 417
Cdd:smart01002 20 PAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPAR 55
|
|
| PRK11728 |
PRK11728 |
L-2-hydroxyglutarate oxidase; |
384-428 |
5.20e-03 |
|
L-2-hydroxyglutarate oxidase;
Pssm-ID: 183292 [Multi-domain] Cd Length: 393 Bit Score: 40.58 E-value: 5.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 71400421 384 RVIVVGGGLAGLSAAIEATAC--GAQVILLEKEPKV-----GGNSAKATSGI 428
Cdd:PRK11728 4 DFVIIGGGIVGLSTAMQLQERypGARIAVLEKESGParhqtGHNSGVIHAGV 55
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
382-420 |
5.47e-03 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 40.77 E-value: 5.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 71400421 382 PARVIVVGGGLAGLSAAIE-ATACGAQVILLEKEPKVGGN 420
Cdd:PLN02576 12 SKDVAVVGAGVSGLAAAYAlASKHGVNVLVTEARDRVGGN 51
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
921-1053 |
7.11e-03 |
|
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99789 [Multi-domain] Cd Length: 243 Bit Score: 39.62 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71400421 921 GQFIAIRGEWDGQqliGYYSPITLPD---DLGVIGILARsDKGTLKEWISALEPGDAVEMKGCGGlvieRRFserylyFS 997
Cdd:cd06192 28 GQFVFLRNFESPG---LERIPLSLAGvdpEEGTISLLVE-IRGPKTKLIAELKPGEKLDVMGPLG----NGF------EG 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71400421 998 GHALKKLCLIAGGTGVAPMLQIIRA-----------ALKKPFLENI-------ESIRLIYAAEDvSELTYRELL 1053
Cdd:cd06192 94 PKKGGTVLLVAGGIGLAPLLPIAKKlaangnkvtvlAGAKKAKEEFldeyfelPADVEIWTTDD-GELGLEGKV 166
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
381-417 |
7.69e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 39.61 E-value: 7.69e-03
10 20 30
....*....|....*....|....*....|....*..
gi 71400421 381 LPARVIVVGGGLAGLSAAIEATACGAQVILLEKEPKV 417
Cdd:pfam07992 151 LPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL 187
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
385-411 |
8.07e-03 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 40.16 E-value: 8.07e-03
10 20
....*....|....*....|....*..
gi 71400421 385 VIVVGGGLAGLSAAIEATACGAQVILL 411
Cdd:COG3075 5 VVVIGGGLAGLTAAIRAAEAGLRVAIV 31
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
384-419 |
8.54e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 40.24 E-value: 8.54e-03
10 20 30
....*....|....*....|....*....|....*.
gi 71400421 384 RVIVVGGGLAGLSAAIEATACGAQVILLEKEPKVGG 419
Cdd:PRK12771 139 RVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
|
|
| |
