|
Name |
Accession |
Description |
Interval |
E-value |
| mam_aldehyde_ox |
TIGR02969 |
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ... |
5-703 |
0e+00 |
|
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, closely related to xanthine dehydrogenase/oxidase.
Pssm-ID: 132014 [Multi-domain] Cd Length: 1330 Bit Score: 1437.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 5 QLLFYVNGQKVVEKNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISRYNPSTKAIRHHPVNACLTPICSLHGTA 84
Cdd:TIGR02969 2 ELLFYVNGRKVVEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPSTKSIRHHPVNACLTPICSLYGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 85 VTTVEGLGNTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFC 164
Cdd:TIGR02969 82 VTTVEGIGSTRTRLHPVQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 165 KASGCCQSKENGVCCLDQEINGLAESQEEDKTSPELFSEEEFLPLDPTQELIFPPELMRIAEKQPPKTRVFYGERVTWIS 244
Cdd:TIGR02969 162 KTSGCCQSKENGVCCLDQGINGLPEFEEGDETSPELFSEEEFLPLDPTQELIFPPELMRMAEKQPQRTRVFYSERMMWIS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 245 PVTLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDGLTLGAGLSLDQVKDILADIVQK 324
Cdd:TIGR02969 242 PVTLKELLEAKFKYPQAPVVMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHTGDGLTLGAGLSLAQVKDILADVVQK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 325 LPEEKTQTYRALLKHLRTLAGSQIRNMASLGGHIVSRHLDSDLNPLLAVGNCTLNLLSKDGERRIPLSEEFLRKCPEADL 404
Cdd:TIGR02969 322 LPEETTQTYRALLKHLGTLAGSQIRNMASLGGHIISRHLDSDLNPLLAVGNCTLNLLSKEGKRQIPLSEQFLSKCPDADL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 405 KPQEVLVSVNIPWSRKWEFVSAFRQAQRQQNALAIVNSGMRVLFREGGGVIEELSILYGGVGSTIISAKNSCQRLIGRPW 484
Cdd:TIGR02969 402 KPQEILVSVNIPYSRKWEFVSAFRQAQRQQNALAIVNSGMRVFFGEGDGIIRELSISYGGVGPTTICAKNSCQKLIGRPW 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 485 NEGMLDTACRLVLDEVTLAASAPGGKVEFKRTLIISFLFKFYLEVSQGLKREDPGHSPSLAGNHESALDDLHSKHPWRTL 564
Cdd:TIGR02969 482 NEEMLDTACRLILDEVSLAGSAPGGKVEFKRTLIISFLFKFYLEVSQILKRMDPGHYPSLADKYESALEDLHSKHHWSTL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 565 THQNVDPAQLPQDPIGRPIMHLSGIKHATGEAIYCDDMPAVDRELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITAD 644
Cdd:TIGR02969 562 KHQNVDSMQLPQDPIGHPIMHLSGVKHATGEAIYCDDMPAVDQELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITAE 641
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 568905650 645 HLQEANTFGTETFLATDEVHCVGHLVCAVIADSETRAKQAAKQVKVVYQDLAPLILTIE 703
Cdd:TIGR02969 642 HLQDANTFGTEKLLATDKVHCVGQLVCAVIADSEVQAKQAAKHVKIVYRDLEPLILTIE 700
|
|
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
23-703 |
0e+00 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 609.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 23 EMMLLPYLRkNLRLTGTKYGCGGGGCGACTVMISRYNPSTKAIRHHPVNACLTPICSLHGTAVTTVEGLGNTRTRLHPIQ 102
Cdd:PLN02906 1 HQTLLEYLR-DLGLTGTKLGCGEGGCGACTVMVSHYDRKTGKCVHYAVNACLAPLYSVEGMHVITVEGIGNRRDGLHPVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 103 ERIAKCHGTQCGFCTPGMVMSMYALLRNHPE-PTLDQLTDALGGNLCRCTGYRPIIDACKTFCKA--------SGCCQSK 173
Cdd:PLN02906 80 EALASMHGSQCGFCTPGFIMSMYALLRSSKTpPTEEQIEECLAGNLCRCTGYRPILDAFRVFAKTddalytgvSSLSLQD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 174 ENGVC--------CLDQEINGLAESQEeDKTSPELFSEEEFlPLDPTQELIFPPELMRIAEkQPPKTRVFYGerVTWISP 245
Cdd:PLN02906 160 GEPICpstgkpcsCGSKTTSAAGTCKS-DRFQPISYSEIDG-SWYTEKELIFPPELLLRKL-TPLKLLGNGG--LTWYRP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 246 VTLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDGLTLGAGLSLDQVKDILADIVQKL 325
Cdd:PLN02906 235 TSLQHLLELKAEYPDAKLVVGNTEVGIEMRFKNAQYPVLISPTHVPELNAIKVKDDGLEIGAAVRLSELQNLFRKVVKER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 326 PEEKTQTYRALLKHLRTLAGSQIRNMASLGGHIVSRHLDSDLNPLLAVGNCTLNLLSKDG-ERRIPLSEEFL--RKcpeA 402
Cdd:PLN02906 315 PAHETSACKAFIEQLKWFAGTQIRNVASIGGNICTASPISDLNPLWMAAGATFVIISCDGdIRSVPASDFFLgyRK---V 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 403 DLKPQEVLVSVNIPWSRKWEFVSAFRQAQRQQNALAIVNSGMRVLFREGGG--VIEELSILYGGVGSTIISAKNSCQRLI 480
Cdd:PLN02906 392 DLKPDEILLSVFLPWTRPFEYVKEFKQAHRRDDDIAIVNAGMRVKLEEKDGewIVSDASIAYGGVAPLSVSARKTEEFLI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 481 GRPWNEGMLDTACRLVLDEVTLAASAPGGKVEFKRTLIISFLFKFYLEVSQGLKredpGHSPSLAGNHE---SALDDLHs 557
Cdd:PLN02906 472 GKPWNKETLQDALKVLQKDILIKEDAPGGMVEFRKSLALSFFFKFFLWVSHQLE----ADGSTIETFPEshlSAAQPFP- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 558 khpwRTLTHQNVDPAQLPQ-DPIGRPIMHLSGIKHATGEAIYCDDMPAVDRELFLTFVTSSRAHAKIVSIDLSEALSLPG 636
Cdd:PLN02906 547 ----RPSSVGMQDYETVKQgTAVGQPEVHLSAELQVTGEAEYADDIPMPPNTLHAALVLSTKPHARILSIDDSEAKSSPG 622
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568905650 637 VVDIITADHLQEANTFGT----ETFLATDEVHCVGHLVCAVIADSETRAKQAAKQVKVVYQDLaPLILTIE 703
Cdd:PLN02906 623 FAGIFLAKDVPGDNMIGPvvhdEELFATDVVTCVGQVIGVVVADTQENAKAAARKVKVEYEEL-PAILSIE 692
|
|
| XdhA |
COG4630 |
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ... |
8-532 |
8.84e-93 |
|
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];
Pssm-ID: 443668 [Multi-domain] Cd Length: 476 Bit Score: 296.66 E-value: 8.84e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 8 FYVNGQKVVEKNVDPEMMLLPYLRKNLRLtgtkygcggggcgactVMISRynPSTKAIRHHPVNACLTPICSLHGTAVTT 87
Cdd:COG4630 3 FLLNGELVELSDVPPTTTLLDWLREDRGLtgtkegcaegdcgactVVVGE--LDDGGLRYRAVNACILFLPQLDGKALVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 88 VEGLGNTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTfckas 167
Cdd:COG4630 81 VEGLAGPDGALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYERGPAPDRADIEDALSGNLCRCTGYRPIIDAARA----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 168 gccqskengvccldqeingLAESQEEDKtspelFSEEEflpldptQELIfpPELMRIAEKQPpktrVFYGERV-TWISPV 246
Cdd:COG4630 156 -------------------MAEAPAPDP-----FAADR-------AAVA--AALRALADGET----VELGAGGsRFLAPA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 247 TLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDGLTLGAGLSLDQVKDILADIvqkLP 326
Cdd:COG4630 199 TLDELAALLAAHPDARLVAGATDVGLWVTKQLRDLPPVIFLGRVAELRRIEETDDGLEIGAAVTLSDAEAALAAH---FP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 327 EektqtYRALlkhLRTLAGSQIRNMASLGGHIVSrhlDS---DLNPLLAVGNCTLNLLSKDGERRIPLSEEFL--RKcpe 401
Cdd:COG4630 276 E-----LAEL---LRRFASRQIRNAGTLGGNIAN---GSpigDSPPALIALGAELVLRSGDGRRTLPLEDFFLgyRK--- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 402 ADLKPQEVLVSVNIPWSRKWEFVSAFRQAQRQQNALAIVNSGMRVlfREGGGVIEELSILYGGVGSTIISAKNSCQRLIG 481
Cdd:COG4630 342 TDLQPGEFVEAIRIPLPAAGQRLRAYKVSKRFDDDISAVCAAFAL--TLDDGTVTEARIAFGGMAATPKRARAAEAALLG 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 568905650 482 RPWNEGMLDTACRLVLDEVT----LAASApggkvEFKRTLIISFLFKFYLEVSQG 532
Cdd:COG4630 420 QPWTEATVAAAAAALAQDFTplsdMRASA-----EYRLAVAANLLRRFFLETQGE 469
|
|
| FAD_binding_5 |
pfam00941 |
FAD binding domain in molybdopterin dehydrogenase; |
239-418 |
2.67e-51 |
|
FAD binding domain in molybdopterin dehydrogenase;
Pssm-ID: 460007 [Multi-domain] Cd Length: 170 Bit Score: 175.81 E-value: 2.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 239 RVTWISPVTLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDGLTLGAGLSLDQVKDIL 318
Cdd:pfam00941 2 KFGYYRPASLAEALELLAAGPDAKLVAGGTSLGPLMKLRLARPDHLIDINGIPELRGIEETDGGLEIGAAVTLSEIAEPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 319 adIVQKLPeektqtyrALLKHLRTLAGSQIRNMASLGGHIVSRHLDSDLNPLLAVGNCTLNLLSKDGERRIPLsEEFLRK 398
Cdd:pfam00941 82 --LREAYP--------ALSEALRKIASPQIRNVGTIGGNIANASPISDLPPALLALDAKVELRSGEGERTVPL-EDFFLG 150
|
170 180
....*....|....*....|
gi 568905650 399 CPEADLKPQEVLVSVNIPWS 418
Cdd:pfam00941 151 YGKTALEPGELITAVIIPLP 170
|
|
| Ald_Xan_dh_C |
smart01008 |
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses ... |
593-695 |
1.79e-37 |
|
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups.
Pssm-ID: 214971 [Multi-domain] Cd Length: 107 Bit Score: 135.34 E-value: 1.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 593 TGEAIYCDDMPaVDRELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITADHLQEANTFG----TETFLATDEVHCVGH 668
Cdd:smart01008 1 TGEARYGDDIR-LPGMLHAAVVRSPVAHARIKSIDTSAARAMPGVVAVLTAKDVPGLNDFGplgpDEPVLADDKVRYVGQ 79
|
90 100
....*....|....*....|....*..
gi 568905650 669 LVCAVIADSETRAKQAAKQVKVVYQDL 695
Cdd:smart01008 80 PVAAVVAETEEAARDAAEAVKVEYEEL 106
|
|
| glyceraldDH_gamma |
NF041020 |
glyceraldehyde dehydrogenase subunit gamma; |
10-161 |
6.77e-29 |
|
glyceraldehyde dehydrogenase subunit gamma;
Pssm-ID: 468949 [Multi-domain] Cd Length: 162 Bit Score: 112.97 E-value: 6.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 10 VNGqKVVEKNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISrynpstkairHHPVNACLTPICSLHGTAVTTVE 89
Cdd:NF041020 15 VNG-VWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMN----------GKSVKSCTVLAVQADGAEITTIE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568905650 90 GLGnTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACK 161
Cdd:NF041020 84 GLS-KDGKLHPIQEAFWENHALQCGYCTPGMIMQAYFLLKENPNPTEEEIRDGIHGNLCRCTGYQNIVKAVK 154
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mam_aldehyde_ox |
TIGR02969 |
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ... |
5-703 |
0e+00 |
|
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, closely related to xanthine dehydrogenase/oxidase.
Pssm-ID: 132014 [Multi-domain] Cd Length: 1330 Bit Score: 1437.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 5 QLLFYVNGQKVVEKNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISRYNPSTKAIRHHPVNACLTPICSLHGTA 84
Cdd:TIGR02969 2 ELLFYVNGRKVVEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPSTKSIRHHPVNACLTPICSLYGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 85 VTTVEGLGNTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFC 164
Cdd:TIGR02969 82 VTTVEGIGSTRTRLHPVQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 165 KASGCCQSKENGVCCLDQEINGLAESQEEDKTSPELFSEEEFLPLDPTQELIFPPELMRIAEKQPPKTRVFYGERVTWIS 244
Cdd:TIGR02969 162 KTSGCCQSKENGVCCLDQGINGLPEFEEGDETSPELFSEEEFLPLDPTQELIFPPELMRMAEKQPQRTRVFYSERMMWIS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 245 PVTLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDGLTLGAGLSLDQVKDILADIVQK 324
Cdd:TIGR02969 242 PVTLKELLEAKFKYPQAPVVMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHTGDGLTLGAGLSLAQVKDILADVVQK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 325 LPEEKTQTYRALLKHLRTLAGSQIRNMASLGGHIVSRHLDSDLNPLLAVGNCTLNLLSKDGERRIPLSEEFLRKCPEADL 404
Cdd:TIGR02969 322 LPEETTQTYRALLKHLGTLAGSQIRNMASLGGHIISRHLDSDLNPLLAVGNCTLNLLSKEGKRQIPLSEQFLSKCPDADL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 405 KPQEVLVSVNIPWSRKWEFVSAFRQAQRQQNALAIVNSGMRVLFREGGGVIEELSILYGGVGSTIISAKNSCQRLIGRPW 484
Cdd:TIGR02969 402 KPQEILVSVNIPYSRKWEFVSAFRQAQRQQNALAIVNSGMRVFFGEGDGIIRELSISYGGVGPTTICAKNSCQKLIGRPW 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 485 NEGMLDTACRLVLDEVTLAASAPGGKVEFKRTLIISFLFKFYLEVSQGLKREDPGHSPSLAGNHESALDDLHSKHPWRTL 564
Cdd:TIGR02969 482 NEEMLDTACRLILDEVSLAGSAPGGKVEFKRTLIISFLFKFYLEVSQILKRMDPGHYPSLADKYESALEDLHSKHHWSTL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 565 THQNVDPAQLPQDPIGRPIMHLSGIKHATGEAIYCDDMPAVDRELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITAD 644
Cdd:TIGR02969 562 KHQNVDSMQLPQDPIGHPIMHLSGVKHATGEAIYCDDMPAVDQELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITAE 641
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 568905650 645 HLQEANTFGTETFLATDEVHCVGHLVCAVIADSETRAKQAAKQVKVVYQDLAPLILTIE 703
Cdd:TIGR02969 642 HLQDANTFGTEKLLATDKVHCVGQLVCAVIADSEVQAKQAAKHVKIVYRDLEPLILTIE 700
|
|
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
23-703 |
0e+00 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 609.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 23 EMMLLPYLRkNLRLTGTKYGCGGGGCGACTVMISRYNPSTKAIRHHPVNACLTPICSLHGTAVTTVEGLGNTRTRLHPIQ 102
Cdd:PLN02906 1 HQTLLEYLR-DLGLTGTKLGCGEGGCGACTVMVSHYDRKTGKCVHYAVNACLAPLYSVEGMHVITVEGIGNRRDGLHPVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 103 ERIAKCHGTQCGFCTPGMVMSMYALLRNHPE-PTLDQLTDALGGNLCRCTGYRPIIDACKTFCKA--------SGCCQSK 173
Cdd:PLN02906 80 EALASMHGSQCGFCTPGFIMSMYALLRSSKTpPTEEQIEECLAGNLCRCTGYRPILDAFRVFAKTddalytgvSSLSLQD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 174 ENGVC--------CLDQEINGLAESQEeDKTSPELFSEEEFlPLDPTQELIFPPELMRIAEkQPPKTRVFYGerVTWISP 245
Cdd:PLN02906 160 GEPICpstgkpcsCGSKTTSAAGTCKS-DRFQPISYSEIDG-SWYTEKELIFPPELLLRKL-TPLKLLGNGG--LTWYRP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 246 VTLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDGLTLGAGLSLDQVKDILADIVQKL 325
Cdd:PLN02906 235 TSLQHLLELKAEYPDAKLVVGNTEVGIEMRFKNAQYPVLISPTHVPELNAIKVKDDGLEIGAAVRLSELQNLFRKVVKER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 326 PEEKTQTYRALLKHLRTLAGSQIRNMASLGGHIVSRHLDSDLNPLLAVGNCTLNLLSKDG-ERRIPLSEEFL--RKcpeA 402
Cdd:PLN02906 315 PAHETSACKAFIEQLKWFAGTQIRNVASIGGNICTASPISDLNPLWMAAGATFVIISCDGdIRSVPASDFFLgyRK---V 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 403 DLKPQEVLVSVNIPWSRKWEFVSAFRQAQRQQNALAIVNSGMRVLFREGGG--VIEELSILYGGVGSTIISAKNSCQRLI 480
Cdd:PLN02906 392 DLKPDEILLSVFLPWTRPFEYVKEFKQAHRRDDDIAIVNAGMRVKLEEKDGewIVSDASIAYGGVAPLSVSARKTEEFLI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 481 GRPWNEGMLDTACRLVLDEVTLAASAPGGKVEFKRTLIISFLFKFYLEVSQGLKredpGHSPSLAGNHE---SALDDLHs 557
Cdd:PLN02906 472 GKPWNKETLQDALKVLQKDILIKEDAPGGMVEFRKSLALSFFFKFFLWVSHQLE----ADGSTIETFPEshlSAAQPFP- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 558 khpwRTLTHQNVDPAQLPQ-DPIGRPIMHLSGIKHATGEAIYCDDMPAVDRELFLTFVTSSRAHAKIVSIDLSEALSLPG 636
Cdd:PLN02906 547 ----RPSSVGMQDYETVKQgTAVGQPEVHLSAELQVTGEAEYADDIPMPPNTLHAALVLSTKPHARILSIDDSEAKSSPG 622
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568905650 637 VVDIITADHLQEANTFGT----ETFLATDEVHCVGHLVCAVIADSETRAKQAAKQVKVVYQDLaPLILTIE 703
Cdd:PLN02906 623 FAGIFLAKDVPGDNMIGPvvhdEELFATDVVTCVGQVIGVVVADTQENAKAAARKVKVEYEEL-PAILSIE 692
|
|
| xanthine_xdhA |
TIGR02963 |
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ... |
8-529 |
2.61e-135 |
|
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit (or, in eukaryotes, the N-terminal domain) of xanthine dehydrogenase, an enzyme of purine catabolism via urate. The small subunit contains both an FAD and a 2Fe-2S cofactor. Aldehyde oxidase (retinal oxidase) appears to have arisen as a neofunctionalization among xanthine dehydrogenases in eukaryotes and [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 274365 [Multi-domain] Cd Length: 467 Bit Score: 406.66 E-value: 2.61e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 8 FYVNGQKVVEKNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISRYNPSTKaIRHHPVNACLTPICSLHGTAVTT 87
Cdd:TIGR02963 3 FFLNGETVTLSDVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVGELVDGGK-LRYRSVNACIQFLPSLDGKAVVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 88 VEGLGNTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACkTFCKAS 167
Cdd:TIGR02963 82 VEDLRQPDGRLHPVQQAMVECHGSQCGFCTPGFVMSLYALYKNSPAPSRADIEDALQGNLCRCTGYRPILDAA-EAAFDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 168 GCCQskengvccldqeinglaesqeedktspelfseeeflPLDPTQELIFpPELMRIAEKQpPKTRVFYGERVtwISPVT 247
Cdd:TIGR02963 161 PCSD------------------------------------PLDADRAPII-ERLRALRAGE-TVELNFGGERF--IAPTT 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 248 LKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDGLTLGAGLSLDQVKDILADIVQKLPE 327
Cdd:TIGR02963 201 LDDLAALKAAHPDARIVAGSTDVGLWVTKQMRDLPDVIYVGQVAELKRIEETDDGIEIGAAVTLTDAYAALAKRYPELGE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 328 EktqtyrallkhLRTLAGSQIRNMASLGGHIVSRHLDSDLNPLLAVGNCTLNLLSKDGERRIPLSEEFL--RKcpeADLK 405
Cdd:TIGR02963 281 L-----------LRRFASLQIRNAGTLGGNIANGSPIGDSPPALIALGARLTLRKGEGRRTLPLEDFFIdyGK---TDRQ 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 406 PQEVLVSVNIPWSRKWEFVSAFRQAQRQQNALAIVNSGMRVLFRegGGVIEELSILYGGVGSTIISAKNSCQRLIGRPWN 485
Cdd:TIGR02963 347 PGEFVEALHVPRPTPGERFRAYKISKRFDDDISAVCAAFNLELD--GGVVAEIRIAFGGMAATPKRAAATEAALLGKPWN 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 568905650 486 EGMLDTACRLVLDEVT-LAASAPGGkvEFKRTLIISFLFKFYLEV 529
Cdd:TIGR02963 425 EATVEAAMAALAGDFTpLSDMRASA--EYRLLTAKNLLRRFFLET 467
|
|
| PLN00192 |
PLN00192 |
aldehyde oxidase |
6-703 |
9.32e-99 |
|
aldehyde oxidase
Pssm-ID: 215096 [Multi-domain] Cd Length: 1344 Bit Score: 331.30 E-value: 9.32e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 6 LLFYVNGQKVVEKNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISRYNPSTKAIRHHPVNACLTPICSLHGTAV 85
Cdd:PLN00192 6 LVFAVNGERFELSSVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVLLSKYDPVLDQVEDFTVSSCLTLLCSVNGCSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 86 TTVEGLGNTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALL-------RNHPEPTLDQLT-----DALGGNLCRCTGY 153
Cdd:PLN00192 86 TTSEGLGNSKDGFHPIHKRFAGFHASQCGFCTPGMCISLFSALvnadktdRPEPPSGFSKLTvveaeKAVSGNLCRCTGY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 154 RPIIDACKTFckASGccqskengvccLDQEINGL------AESQEEDKTSpelfseeefLPL-DPTQELIFPPELMRIAE 226
Cdd:PLN00192 166 RPIVDACKSF--AAD-----------VDIEDLGLnsfwkkGESEEAKLSK---------LPPyNHSDHICTFPEFLKKEI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 227 KqppKTRVFYGERVTWISPVTLKELVE----AKFKYPQAPIVMGYTSVG--PEVKFKGVFhpIIISpdRIEELGVISQAR 300
Cdd:PLN00192 224 K---SSLLLDSSRYRWYTPVSVEELQSllesNNFDGVSVKLVVGNTGTGyyKDEELYDKY--IDIR--HIPELSMIRRDE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 301 DGLTLGAGLSLDQVKDILADivqklpEEKTQ-TYRALLKHLRTLAGSQIRNMASLGGHIV---SRHLDSDLNP-LLAVGN 375
Cdd:PLN00192 297 KGIEIGAVVTISKAIEALRE------ESKSEyVFKKIADHMEKIASRFVRNTGSIGGNLVmaqRKQFPSDIATiLLAAGS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 376 cTLNLLSKDGERRIPLsEEFLRKcPEADLKpqEVLVSVNIP-WSRKWE-----FVSAFRQAQRQQ-NALAIVNSGM--RV 446
Cdd:PLN00192 371 -TVNIQNASKREKLTL-EEFLER-PPLDSK--SLLLSVEIPsWTSSSGsdtklLFETYRAAPRPLgNALPYLNAAFlaEV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 447 LFRE--GGGVIEELSILYGGVGST-IISAKNSCQRLIGRPWNEGMLDTACRLVLDEVTLA--ASAPggkvEFKRTLIISF 521
Cdd:PLN00192 446 SQDAssGGIVVNDCRLAFGAYGTKhAIRARKVEEFLTGKVLSDSVLYEAVRLLKGIVVPEdgTSHP----EYRSSLAVGF 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 522 LFKFYLEVSQGLKREDPGHSPSLAGNHESALDDLHSKHPWRTLTHQNVDPAQLPQDPIGRPIMHLSGIKHATGEAIYCDD 601
Cdd:PLN00192 522 LFDFLSPLIESNAKSSNGWLDGGSNTKQNPDQHDDVKKPTLLLSSKQQVEENNEYHPVGEPIKKVGAALQASGEAVYVDD 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 602 MPAVDRELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITADHLQE------ANT-FGTETFLATDEVHCVGHLVCAVI 674
Cdd:PLN00192 602 IPSPKNCLYGAFIYSTKPLARVKGIKFKSNLVPQGVLAVITFKDIPKggqnigSKTiFGPEPLFADEVTRCAGQRIALVV 681
|
730 740 750
....*....|....*....|....*....|.
gi 568905650 675 ADSETRAKQAAKQVKVVY--QDLAPLILTIE 703
Cdd:PLN00192 682 ADTQKHADMAANLAVVEYdtENLEPPILTVE 712
|
|
| XdhA |
COG4630 |
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ... |
8-532 |
8.84e-93 |
|
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];
Pssm-ID: 443668 [Multi-domain] Cd Length: 476 Bit Score: 296.66 E-value: 8.84e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 8 FYVNGQKVVEKNVDPEMMLLPYLRKNLRLtgtkygcggggcgactVMISRynPSTKAIRHHPVNACLTPICSLHGTAVTT 87
Cdd:COG4630 3 FLLNGELVELSDVPPTTTLLDWLREDRGLtgtkegcaegdcgactVVVGE--LDDGGLRYRAVNACILFLPQLDGKALVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 88 VEGLGNTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTfckas 167
Cdd:COG4630 81 VEGLAGPDGALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYERGPAPDRADIEDALSGNLCRCTGYRPIIDAARA----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 168 gccqskengvccldqeingLAESQEEDKtspelFSEEEflpldptQELIfpPELMRIAEKQPpktrVFYGERV-TWISPV 246
Cdd:COG4630 156 -------------------MAEAPAPDP-----FAADR-------AAVA--AALRALADGET----VELGAGGsRFLAPA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 247 TLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDGLTLGAGLSLDQVKDILADIvqkLP 326
Cdd:COG4630 199 TLDELAALLAAHPDARLVAGATDVGLWVTKQLRDLPPVIFLGRVAELRRIEETDDGLEIGAAVTLSDAEAALAAH---FP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 327 EektqtYRALlkhLRTLAGSQIRNMASLGGHIVSrhlDS---DLNPLLAVGNCTLNLLSKDGERRIPLSEEFL--RKcpe 401
Cdd:COG4630 276 E-----LAEL---LRRFASRQIRNAGTLGGNIAN---GSpigDSPPALIALGAELVLRSGDGRRTLPLEDFFLgyRK--- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 402 ADLKPQEVLVSVNIPWSRKWEFVSAFRQAQRQQNALAIVNSGMRVlfREGGGVIEELSILYGGVGSTIISAKNSCQRLIG 481
Cdd:COG4630 342 TDLQPGEFVEAIRIPLPAAGQRLRAYKVSKRFDDDISAVCAAFAL--TLDDGTVTEARIAFGGMAATPKRARAAEAALLG 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 568905650 482 RPWNEGMLDTACRLVLDEVT----LAASApggkvEFKRTLIISFLFKFYLEVSQG 532
Cdd:COG4630 420 QPWTEATVAAAAAALAQDFTplsdMRASA-----EYRLAVAANLLRRFFLETQGE 469
|
|
| FAD_binding_5 |
pfam00941 |
FAD binding domain in molybdopterin dehydrogenase; |
239-418 |
2.67e-51 |
|
FAD binding domain in molybdopterin dehydrogenase;
Pssm-ID: 460007 [Multi-domain] Cd Length: 170 Bit Score: 175.81 E-value: 2.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 239 RVTWISPVTLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDGLTLGAGLSLDQVKDIL 318
Cdd:pfam00941 2 KFGYYRPASLAEALELLAAGPDAKLVAGGTSLGPLMKLRLARPDHLIDINGIPELRGIEETDGGLEIGAAVTLSEIAEPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 319 adIVQKLPeektqtyrALLKHLRTLAGSQIRNMASLGGHIVSRHLDSDLNPLLAVGNCTLNLLSKDGERRIPLsEEFLRK 398
Cdd:pfam00941 82 --LREAYP--------ALSEALRKIASPQIRNVGTIGGNIANASPISDLPPALLALDAKVELRSGEGERTVPL-EDFFLG 150
|
170 180
....*....|....*....|
gi 568905650 399 CPEADLKPQEVLVSVNIPWS 418
Cdd:pfam00941 151 YGKTALEPGELITAVIIPLP 170
|
|
| CutS |
COG2080 |
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ... |
8-159 |
5.82e-44 |
|
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441683 [Multi-domain] Cd Length: 155 Bit Score: 154.86 E-value: 5.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 8 FYVNGQKVvEKNVDPEMMLLPYLRKNLRLtgtkygcggggcgactvmisrynPSTKA-------------IRHHPVNACL 74
Cdd:COG2080 6 LTVNGKPV-EVDVDPDTPLLDVLRDDLGL-----------------------TGTKFgcghgqcgactvlVDGKAVRSCL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 75 TPICSLHGTAVTTVEGLGnTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYR 154
Cdd:COG2080 62 TLAVQADGKEITTIEGLA-EDGELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYV 140
|
....*
gi 568905650 155 PIIDA 159
Cdd:COG2080 141 RIVRA 145
|
|
| Ald_Xan_dh_C |
pfam01315 |
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; |
593-695 |
4.49e-38 |
|
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain;
Pssm-ID: 426197 [Multi-domain] Cd Length: 107 Bit Score: 136.98 E-value: 4.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 593 TGEAIYCDDMPAVDRElFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITADHL----QEANTFGTETFLATDEVHCVGH 668
Cdd:pfam01315 1 TGEAVYVDDIPAPGNL-YGAFVRSTIAHAKIVSIDTSAALALPGVVAVITAKDLpggnYNIGPIPLDPLFATDKVRHVGQ 79
|
90 100
....*....|....*....|....*..
gi 568905650 669 LVCAVIADSETRAKQAAKQVKVVYQDL 695
Cdd:pfam01315 80 PIAAVVADDEETARRAAKLVKVEYEEL 106
|
|
| Ald_Xan_dh_C |
smart01008 |
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses ... |
593-695 |
1.79e-37 |
|
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups.
Pssm-ID: 214971 [Multi-domain] Cd Length: 107 Bit Score: 135.34 E-value: 1.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 593 TGEAIYCDDMPaVDRELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITADHLQEANTFG----TETFLATDEVHCVGH 668
Cdd:smart01008 1 TGEARYGDDIR-LPGMLHAAVVRSPVAHARIKSIDTSAARAMPGVVAVLTAKDVPGLNDFGplgpDEPVLADDKVRYVGQ 79
|
90 100
....*....|....*....|....*..
gi 568905650 669 LVCAVIADSETRAKQAAKQVKVVYQDL 695
Cdd:smart01008 80 PVAAVVAETEEAARDAAEAVKVEYEEL 106
|
|
| Fer2_2 |
pfam01799 |
[2Fe-2S] binding domain; |
87-160 |
3.65e-36 |
|
[2Fe-2S] binding domain;
Pssm-ID: 460336 [Multi-domain] Cd Length: 73 Bit Score: 130.24 E-value: 3.65e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568905650 87 TVEGLGNTRTrlHPIQERIAKCHGTQCGFCTPGMVMSMYALL-RNHPEPTLDQLTDALGGNLCRCTGYRPIIDAC 160
Cdd:pfam01799 1 TIEGLAESGG--EPVQQAFAEAGAVQCGYCTPGMIMSAYALLeRNPPPPTEAEIREALSGNLCRCTGYRRIVDAV 73
|
|
| CutB |
COG1319 |
Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit [Energy production and conversion] ... |
241-518 |
3.76e-33 |
|
Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440930 [Multi-domain] Cd Length: 285 Bit Score: 129.09 E-value: 3.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 241 TWISPVTLKELVEAKFKY-PQAPIVMGYTSVGPEVKFkGVFHP---IIISpdRIEELGVISQARDGLTLGAGLSLDqvkD 316
Cdd:COG1319 5 EYHRPTSLEEALALLAEHgPDARVLAGGTDLLPLMKL-RLARPehlVDIN--RIPELRGIEEEGGGLRIGALVTHA---E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 317 ILAD-IVQKLpeektqtYRALLKHLRTLAGSQIRNMASLGGHIVsrHLD--SDLNPLLAVGNCTLNLLSKDGERRIPLsE 393
Cdd:COG1319 79 LAASpLVRER-------YPLLAEAARAIASPQIRNRGTIGGNLA--NADpaADLPPALLALDATVELAGPDGERTIPA-A 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 394 EFLRKCPEADLKPQEVLVSVNIPWSRKWEfVSAFRQ-AQRQQNALAIVNSGmrVLFREGGGVIEELSILYGGVGSTIISA 472
Cdd:COG1319 149 DFFLGPGETALEPGELITAVRLPAPPAGA-GSAYLKvGRRASDAIALVSVA--VALRLDGGTIRDARIALGGVAPTPWRA 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568905650 473 KNSCQRLIGRPWNEGMLDTACRLVLDEVTLAASAPGGKvEFKRTLI 518
Cdd:COG1319 226 REAEAALAGKPLSEEAIEAAAEAAAAAADPIDDVRASA-EYRRHLA 270
|
|
| CO_deh_flav_C |
pfam03450 |
CO dehydrogenase flavoprotein C-terminal domain; |
425-529 |
1.32e-32 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 460921 [Multi-domain] Cd Length: 102 Bit Score: 121.13 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 425 SAFRQAQRQQNALAIVNSGMRVLFreGGGVIEELSILYGGVGSTIISAKNSCQRLIGRPWNEGMLDTACRLVLDEVTLaA 504
Cdd:pfam03450 1 AAYKQAKRRDDDIAIVNAAFRVRL--DGGTVEDARIAFGGVAPTPIRATEAEAALIGKPWDEETLEAAAALLLEDLSP-L 77
|
90 100
....*....|....*....|....*
gi 568905650 505 SAPGGKVEFKRTLIISFLFKFYLEV 529
Cdd:pfam03450 78 SDPRGSAEYRRHLARSLLFRFLLEA 102
|
|
| glyceraldDH_gamma |
NF041020 |
glyceraldehyde dehydrogenase subunit gamma; |
10-161 |
6.77e-29 |
|
glyceraldehyde dehydrogenase subunit gamma;
Pssm-ID: 468949 [Multi-domain] Cd Length: 162 Bit Score: 112.97 E-value: 6.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 10 VNGqKVVEKNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISrynpstkairHHPVNACLTPICSLHGTAVTTVE 89
Cdd:NF041020 15 VNG-VWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMN----------GKSVKSCTVLAVQADGAEITTIE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568905650 90 GLGnTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACK 161
Cdd:NF041020 84 GLS-KDGKLHPIQEAFWENHALQCGYCTPGMIMQAYFLLKENPNPTEEEIRDGIHGNLCRCTGYQNIVKAVK 154
|
|
| CoxL |
COG1529 |
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ... |
579-699 |
1.93e-27 |
|
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441138 [Multi-domain] Cd Length: 741 Bit Score: 118.41 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 579 IGRPIMHLSGIKHATGEAIYCDDMPaVDRELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITADHLqEANTFGTETF- 657
Cdd:COG1529 10 IGKPVPRVDGPAKVTGRARYTDDIR-LPGMLYAAVVRSPHAHARIKSIDTSAALALPGVVAVLTGEDL-PGLKFGLPGPd 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568905650 658 -----LATDEVHCVGHLVCAVIADSETRAKQAAKQVKVVYQDLAPLI 699
Cdd:COG1529 88 pdqppLADDKVRYVGEPVAAVVAETREAARDAAELIKVEYEPLPAVV 134
|
|
| 4hydroxCoAred |
TIGR03193 |
4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts ... |
62-162 |
9.91e-25 |
|
4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts 4-hydroxybenzoyl-CoA to benzoyl-CoA, a common intermediate in the degradation of aromatic compounds. This protein family represents the gamma chain of this three-subunit enzyme.
Pssm-ID: 132237 [Multi-domain] Cd Length: 148 Bit Score: 100.72 E-value: 9.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 62 TKAIRHHPVNACLTPICSLHGTAVTTVEGLGnTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTD 141
Cdd:TIGR03193 47 TVLVDGRPRLACSTLAHRVAGRKVETVEGLA-TNGRLSRLQQAFHERLGTQCGFCTPGMIMAAEALLRRNPSPSRDEIRA 125
|
90 100
....*....|....*....|.
gi 568905650 142 ALGGNLCRCTGYRPIIDACKT 162
Cdd:TIGR03193 126 ALAGNLCRCTGYVKIIESVEA 146
|
|
| CO_deh_flav_C |
smart01092 |
CO dehydrogenase flavoprotein C-terminal domain; |
426-529 |
1.81e-24 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 215021 [Multi-domain] Cd Length: 102 Bit Score: 98.07 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 426 AFRQAQRQQNALAIVNSGMRVLFRegGGVIEELSILYGGVGSTIISAKNSCQRLIGRPWNEGMLDTACRLVLDEVTLAAS 505
Cdd:smart01092 1 AYKKSRRRDGDIALVSAAVALTLD--GGRVTEARIALGGVAPTPKRAAEAEAALVGKPLTDEALARAAAAALAQDFTPLS 78
|
90 100
....*....|....*....|....
gi 568905650 506 APGGKVEFKRTLIISFLFKFYLEV 529
Cdd:smart01092 79 DMRASAEYRRQLAANLLRRALLEA 102
|
|
| pucE |
TIGR03198 |
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ... |
5-165 |
4.73e-24 |
|
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the Iron-sulfur cluster binding-subunit of xanthine dehydrogenase (pucE), acting in conjunction with pucC, the FAD-binding subunit and pucD, the molybdopterin binding subunit. The more common XDH complex (GenProp0640) includes the xdhA gene as the Fe-S cluster binding component.
Pssm-ID: 132242 [Multi-domain] Cd Length: 151 Bit Score: 98.77 E-value: 4.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 5 QLLFYVNGQKVvEKNVDPEMMLLPYLRKNLRLTGTKYGCGgggcgactvmISRYNPSTKAIRHHPVNACLTPICSLHGTA 84
Cdd:TIGR03198 3 QFRFTVNGQAW-EVAAVPTTRLSDLLRKELQLTGTKVSCG----------IGRCGACSVLIDGKLANACLTMAYQADGHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 85 VTTVEGLgnTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFC 164
Cdd:TIGR03198 72 ITTIEGI--AENELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRETPQPSDEDMEEGLSGNLCRCTGYGGIIRSACRIR 149
|
.
gi 568905650 165 K 165
Cdd:TIGR03198 150 R 150
|
|
| Se_dep_XDH |
TIGR03311 |
selenium-dependent xanthine dehydrogenase; Members of this protein resemble conventional ... |
8-166 |
7.27e-23 |
|
selenium-dependent xanthine dehydrogenase; Members of this protein resemble conventional xanthine dehydrogenase enzymes, which depend on molybdenum cofactor - molybdopterin bound to molybdate with two sulfur atoms as ligands. But all members of this family occur in species that contain markers for the biosynthesis of enzymes with a selenium-containing form of molybdenum cofactor. The member of this family from Enterococcus faecalis has been shown to act as a xanthine dehydrogenenase, and its activity if dependent on SelD (selenophosphate synthase), selenium, and molybdenum. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132354 [Multi-domain] Cd Length: 848 Bit Score: 104.15 E-value: 7.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 8 FYVNGQKVVeknVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISrynpsTKAIRhhpvnACLTPICSLHGTAVTT 87
Cdd:TIGR03311 3 FIVNGREVD---VNEEKKLLEFLREDLRLTGVKNGCGEGACGACTVIVN-----GKAVR-----ACRFTTAKLAGKEITT 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568905650 88 VEGLGNTRTRLHPIQerIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKA 166
Cdd:TIGR03311 70 VEGLTEREKDVYAWA--FAKAGAVQCGFCIPGMVISAKALLDKNPNPTEAEIKKALKGNICRCTGYVKIIKAVRLAAKA 146
|
|
| PRK09971 |
PRK09971 |
xanthine dehydrogenase subunit XdhB; Provisional |
245-518 |
4.82e-22 |
|
xanthine dehydrogenase subunit XdhB; Provisional
Pssm-ID: 182175 [Multi-domain] Cd Length: 291 Bit Score: 97.03 E-value: 4.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 245 PVTLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQARDG-LTLGAGLSLDQVkdILADIVQ 323
Cdd:PRK09971 10 AATLEEAIELLADNPQAKLIAGGTDVLIQLHHHNDRYRHLVSIHNIAELRGITLAEDGsIRIGAATTFTQI--IEDPIIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 324 K-LPeektqtyrALLKHLRTLAGSQIRNMASLGGHIVSRHLDSDLNPLLAVGNCTLNLLSKDGERRIPLSeEFLRKCPEA 402
Cdd:PRK09971 88 KhLP--------ALAEAAVSIGGPQIRNVATIGGNICNGATSADSAPPLFALDAKLEIHSPNGVRFVPIN-GFYTGPGKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 403 DLKPQEVLVSVNIPWSRKWEFVSA-FRQAQRqqNALAIVNSGMRVLFREGGGVIEELSILYGGVGSTIISAKNSCQRLIG 481
Cdd:PRK09971 159 SLEHDEILVAFIIPPEPYEHAGGAyIKYAMR--DAMDIATIGCAVLCRLDNGNFEDLRLAFGVAAPTPIRCQHAEQTAKG 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 568905650 482 RPWNEGMLDTACRLVLDEVTLAASAPGGKvEFKRTLI 518
Cdd:PRK09971 237 APLNLETLEAIGELVLQDVAPRSSWRASK-EFRLHLI 272
|
|
| PRK11433 |
PRK11433 |
aldehyde oxidoreductase 2Fe-2S subunit; Provisional |
5-159 |
5.35e-18 |
|
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
Pssm-ID: 236910 [Multi-domain] Cd Length: 217 Bit Score: 83.28 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 5 QLLFYVNGqKVVEKNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISrynpstkairHHPVNACLTPICSLHGTA 84
Cdd:PRK11433 51 PVTLKVNG-KTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVN----------GRRLNACLTLAVMHQGAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 85 VTTVEGLGnTRTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLR-------NH--------PEPTLDQLTDALGGNLCR 149
Cdd:PRK11433 120 ITTIEGLG-SPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKeikdgipSHvtvdltaaPELTADEIRERMSGNICR 198
|
170
....*....|
gi 568905650 150 CTGYRPIIDA 159
Cdd:PRK11433 199 CGAYSNILEA 208
|
|
| PRK09970 |
PRK09970 |
xanthine dehydrogenase subunit XdhA; Provisional |
579-703 |
1.05e-17 |
|
xanthine dehydrogenase subunit XdhA; Provisional
Pssm-ID: 236637 [Multi-domain] Cd Length: 759 Bit Score: 87.45 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 579 IGRPIMHLSGIKHATGEAIYCDDMPAVDReLFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITADHLqEANTFGT---- 654
Cdd:PRK09970 3 IGKSIMRVDAIAKVTGRAKYTDDYVMAGM-LYAKYVRSPIAHGKVKSIDTEEARSLPGVEAVFTWEDV-PDIPFPTaghp 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 655 -----------ETFLATDEVHCVGHLVCAVIADSETRAKQAAKQVKVVYQDLaPLILTIE 703
Cdd:PRK09970 81 wsldpnhrdiaDRALLTRHVRHHGDAVAAVVARDELTAEKALKLIKVEYEEL-PVITDPE 139
|
|
| PRK09908 |
PRK09908 |
xanthine dehydrogenase iron sulfur-binding subunit XdhC; |
70-165 |
2.96e-17 |
|
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
Pssm-ID: 182139 [Multi-domain] Cd Length: 159 Bit Score: 79.57 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 70 VNACLTPICSLHGTAVTTVEGLGNTrTRLHPIQERIAKCHGTQCGFCTPGMVMSMYALL---RNHPePTLDQLTDALGGN 146
Cdd:PRK09908 61 IDSCLYLAAWAEGKEIRTLEGEAKG-GKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLakpREKP-LTITEIRRGLAGN 138
|
90
....*....|....*....
gi 568905650 147 LCRCTGYRPIIDACKTFCK 165
Cdd:PRK09908 139 LCRCTGYQMIVNTVLDCEK 157
|
|
| PRK09800 |
PRK09800 |
putative hypoxanthine oxidase; Provisional |
577-703 |
4.83e-08 |
|
putative hypoxanthine oxidase; Provisional
Pssm-ID: 182084 [Multi-domain] Cd Length: 956 Bit Score: 56.38 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 577 DPIGRPIMHLSGIKHATGEAIYCDDMPAVDrELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITadHLQEAN---TFG 653
Cdd:PRK09800 170 EVIGKHYPKTDAAKMVQAKPCYVEDRVTAD-ACVIKMLRSPHAHALITHLDVSKAEALPGVVHVIT--HLNCPDiyyTPG 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568905650 654 TETF---------LATDEVHCVGHLVCAVIADSETRAKQAAKQVKVVYQDLAPlILTIE 703
Cdd:PRK09800 247 GQSApepspldrrMFGKKMRHVGDRVAAVVAESEEIALEALKLIDVEYEVLKP-VMSID 304
|
|
| PRK09800 |
PRK09800 |
putative hypoxanthine oxidase; Provisional |
69-154 |
1.98e-06 |
|
putative hypoxanthine oxidase; Provisional
Pssm-ID: 182084 [Multi-domain] Cd Length: 956 Bit Score: 51.37 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 69 PVNACLTPICSLHGTAVTTVEGLGNTRtRLHPIQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLC 148
Cdd:PRK09800 55 IVNASLLIAAQLEKADIRTAESLGKWN-ELSLVQQAMVDVGVVQSGYNDPAAALIITDLLDRIAAPTREEIDDALSGLFS 133
|
....*.
gi 568905650 149 RCTGYR 154
Cdd:PRK09800 134 RDAGWQ 139
|
|
| LAL_C2 |
pfam18603 |
L-amino acid ligase C-terminal domain 2; l-amino-acid ligases (LALs; EC 6.3.2.28) were ... |
613-692 |
2.90e-03 |
|
L-amino acid ligase C-terminal domain 2; l-amino-acid ligases (LALs; EC 6.3.2.28) were discovered to be ATP-grasp superfamily enzymes that catalyze the formation of an alpha-peptide bond between two l-amino acids in an ATP-dependent manner. The members of this family share a common structural architecture that consists of three domains referred to as the A-domain, B-domain and C-domain. The C domain can be further divided into the C1-subdomain and the C2-subdomain. This entry represents the C2 subdomain.
Pssm-ID: 436613 Cd Length: 78 Bit Score: 37.15 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905650 613 FVTSSRAhAKIVSID-LSEALSLPGVVDI-ITA---DHLQEantfgtetflATDEVHCVGHlvcaVIADSET------RA 681
Cdd:pfam18603 2 FLTAPRP-GRLRAVEgLEEARALPGVVEVeITVkpgDRVRP----------PRSSGDRLGY----VIATGDTpeealaAA 66
|
90
....*....|.
gi 568905650 682 KQAAKQVKVVY 692
Cdd:pfam18603 67 EAAAALIRIEV 77
|
|
| |
