|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-1145 |
0e+00 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 2296.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1 MKQIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDLGPAESYLNIERIIDVAKQANVDA 80
Cdd:COG1038 1 MKKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 81 IHPGYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMI 160
Cdd:COG1038 81 IHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 161 KATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQK 240
Cdd:COG1038 161 KAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 241 VVEVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLV-SGDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAA 319
Cdd:COG1038 241 VVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVdDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 320 GADLFGEEINMPQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAGDGFQGAEISPYYDSLLVKLS 399
Cdd:COG1038 321 GYSLDDPEIGIPSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDSLLVKVT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 400 THAISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEETPELFDIQPSLDRGTKTLEYIGNVTIN 479
Cdd:COG1038 401 AWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 480 GFPNVEKRPKPDYELASIPTVSSSKIASfSGTKQLLDEVGPKGVAEWVKKQDDVLLTDTTFRDAHQSLLATRVRTKDMIN 559
Cdd:COG1038 481 GPPGVKGRPKPDFPKPKLPKVDLGAPPP-KGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 560 IASKTADVFKDGFSLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQMLLRASNAVGYKNYPDNVIHKFVQESAKA 639
Cdd:COG1038 560 IAPATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAAEA 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 640 GIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTGDILNPERSnIYTLEYYVKLAKELEREGFHILAIKDMAGLLK 719
Cdd:COG1038 640 GIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRT-KYTLDYYVDLAKELEKAGAHILAIKDMAGLLK 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 720 PKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASMSGLTSQPSANSLYYALNGFPRHLRTDIE 799
Cdd:COG1038 719 PYAAYKLVKALKEEVDLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLDLD 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 800 GMESLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGLGERFDEVKDMYRRVNFLFGDIVKVTPSS 879
Cdd:COG1038 799 ALQELSNYWEAVRKYYAPFESGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTPSS 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 880 KVVGDMALYMVQNDLDEQSVITDGYKLDFPESVVSFFKGEIGQPVNGFNKDLQAVILKGQEALTARPGEYLEPVDFEKVR 959
Cdd:COG1038 879 KVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPVDFDALR 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 960 ELLEEEQQGPVTEQDIISYVLYPKVYEQYIQTRNQYGNLSLLDTPTFFFGMRNGETVEIEIDKGKRLIIKLETISEPDEN 1039
Cdd:COG1038 959 AELEEKLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPDED 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1040 GNRTIYYAMNGQARRIYIKDENVHTNANVKPKADKSNPSHIGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQA 1119
Cdd:COG1038 1039 GMRTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITA 1118
|
1130 1140
....*....|....*....|....*.
gi 586172456 1120 PFDGVIKQVTVNNGDTIATGDLLIEI 1145
Cdd:COG1038 1119 PRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-1147 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 2231.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1 MKQIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDLGPAESYLNIERIIDVAKQANVDA 80
Cdd:PRK12999 2 MKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 81 IHPGYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMI 160
Cdd:PRK12999 82 IHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIML 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 161 KATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQK 240
Cdd:PRK12999 162 KASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 241 VVEVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGD-EFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAA 319
Cdd:PRK12999 242 VVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADgNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 320 GADLFGEEINMPQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAGDGFQGAEISPYYDSLLVKLS 399
Cdd:PRK12999 322 GATLHDLEIGIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDSLLVKLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 400 THAISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEETPELFDIQPSLDRGTKTLEYIGNVTIN 479
Cdd:PRK12999 402 AWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTVN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 480 GFPNVEKRPkPDYELASIPTVSSSKIASfSGTKQLLDEVGPKGVAEWVKKQDDVLLTDTTFRDAHQSLLATRVRTKDMIN 559
Cdd:PRK12999 482 GFPGVKKKP-PVFPDPRLPKVDLSAPPP-AGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLLR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 560 IASKTADVFKDGFSLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQMLLRASNAVGYKNYPDNVIHKFVQESAKA 639
Cdd:PRK12999 560 IAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAAA 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 640 GIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTGDILNPERSNiYTLEYYVKLAKELEREGFHILAIKDMAGLLK 719
Cdd:PRK12999 640 GIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAK-YDLDYYVDLAKELEKAGAHILAIKDMAGLLK 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 720 PKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASMSGLTSQPSANSLYYALNGFPRHLRTDIE 799
Cdd:PRK12999 719 PAAAYELVSALKEEVDLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDLD 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 800 GMESLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGLGERFDEVKDMYRRVNFLFGDIVKVTPSS 879
Cdd:PRK12999 799 AIRKLSPYWEAVRPYYAPFESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVTPSS 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 880 KVVGDMALYMVQNDLDEQSVITDGYKLDFPESVVSFFKGEIGQPVNGFNKDLQAVILKGQEALTARPGEYLEPVDFEKVR 959
Cdd:PRK12999 879 KVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDFEAER 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 960 ELLEEEQQGPVTEQDIISYVLYPKVYEQYIQTRNQYGNLSLLDTPTFFFGMRNGETVEIEIDKGKRLIIKLETISEPDEN 1039
Cdd:PRK12999 959 AELEEKLGREVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEPDED 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1040 GNRTIYYAMNGQARRIYIKDENVHTNANVKPKADKSNPSHIGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQA 1119
Cdd:PRK12999 1039 GMRTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITA 1118
|
1130 1140
....*....|....*....|....*...
gi 586172456 1120 PFDGVIKQVTVNNGDTIATGDLLIEIEK 1147
Cdd:PRK12999 1119 PVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
6-1146 |
0e+00 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 1716.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 6 KLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVG--SDLGPAESYLNIERIIDVAKQANVDAIHP 83
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGegPDLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 84 GYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKAT 163
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 164 SGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVE 243
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 244 VAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGD-EFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAGAD 322
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDgKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 323 LFGEEINMPQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAGDGFQGAEISPYYDSLLVKLSTHA 402
Cdd:TIGR01235 321 LPTPQLGVPNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 403 ISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEETPELFDIQPSLDRGTKTLEYIGNVTINGFP 482
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNGHP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 483 NVEKRPKPDYELASIPTVSSSKIASFSGTKQLLDEVGPKGVAEWVKKQDDVLLTDTTFRDAHQSLLATRVRTKDMINIAS 562
Cdd:TIGR01235 481 EAKDKLKPLENAPRVVVLYADQNPVPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIAP 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 563 KTADVFKDGFSLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQMLLRASNAVGYKNYPDNVIHKFVQESAKAGID 642
Cdd:TIGR01235 561 TTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGID 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 643 VFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTGDILNPERSNiYTLEYYVKLAKELEREGFHILAIKDMAGLLKPKA 722
Cdd:TIGR01235 641 IFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPK-YDLKYYTNLAVELEKAGAHILGIKDMAGLLKPAA 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 723 AYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASMSGLTSQPSANSLYYALNGFPRHLRTDIEGME 802
Cdd:TIGR01235 720 AKLLIKALREKTDLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVAWIR 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 803 SLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGLGERFDEVKDMYRRVNFLFGDIVKVTPSSKVV 882
Cdd:TIGR01235 800 ELSAYWEAVRNLYAAFESDLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSSKVV 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 883 GDMALYMVQNDLDEQSVITDGYKLDFPESVVSFFKGEIGQPVNGFNKDLQAVILKGQEALTARPGEYLEPVDFEKVRELL 962
Cdd:TIGR01235 880 GDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAIRKDL 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 963 EEEQQGPVTEQDIISYVLYPKVYEQYIQTRNQYGNLSLLDTPTFFFGMRNGETVEIEIDKGKRLIIKLETISEPDENGNR 1042
Cdd:TIGR01235 960 QEKHEREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQGER 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1043 TIYYAMNGQARRIYIKDENVHTNANVKPKADKSNPSHIGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFD 1122
Cdd:TIGR01235 1040 EVFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKD 1119
|
1130 1140
....*....|....*....|....
gi 586172456 1123 GVIKQVTVNNGDTIATGDLLIEIE 1146
Cdd:TIGR01235 1120 GTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
4-452 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 737.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 4 IKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDLgPAESYLNIERIIDVAKQANVDAIHP 83
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAP-AAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 84 GYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKAT 163
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 164 SGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVE 243
Cdd:COG4770 161 AGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 244 VAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGD-EFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAgad 322
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADgNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAA--- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 323 lfGEEINMpQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAGdGFQGAEISPYYDSLLVKLSTHA 402
Cdd:COG4770 318 --GEPLPF-TQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDSMIAKLIVWG 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 586172456 403 ISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEE 452
Cdd:COG4770 394 PDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIER 443
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
3-452 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 640.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 3 QIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGsdlgPA---ESYLNIERIIDVAKQANVD 79
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIG----PApskKSYLNIPAIISAAEITGAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 80 AIHPGYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLM 159
Cdd:PRK08591 77 AIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 160 IKATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQ 239
Cdd:PRK08591 157 IKATAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 240 KVVEVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGD-EFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVA 318
Cdd:PRK08591 237 KVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNgEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 319 AGADL-FgeeinmpQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAGdGFQGAEISPYYDSLLVK 397
Cdd:PRK08591 317 AGEPLsI-------KQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMIGK 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 586172456 398 LSTHAISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEE 452
Cdd:PRK08591 389 LIVHGETREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEK 443
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
5-456 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 628.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 5 KKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDlGPAESYLNIERIIDVAKQANVDAIHPG 84
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPA-PPSKSYLNIERIIDVAKKAGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 85 YGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKATS 164
Cdd:PRK08654 82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 165 GGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVEV 244
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 245 APSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAGADL- 323
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELs 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 324 FGeeinmpqQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAGDgFQGAEISPYYDSLLVKLSTHAI 403
Cdd:PRK08654 322 FK-------QEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGV-HMGYEIPPYYDSMISKLIVWGR 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 586172456 404 SFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEETPEL 456
Cdd:PRK08654 394 TREEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTI 446
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
4-458 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 572.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 4 IKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDlgPAESYLNIERIIDVAKQANVDAIHP 83
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD--PLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 84 GYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKAT 163
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 164 SGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVE 243
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 244 VAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLV-SGDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAGAD 322
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 323 LfgeeinMPQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAGDgFQGAEISPYYDSLLVKLSTHA 402
Cdd:PRK07178 320 L------SYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAI-YTGYTIPPYYDSMCAKLIVWA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 586172456 403 ISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEETPELFD 458
Cdd:PRK07178 393 LTWEEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTN 448
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
4-451 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 569.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 4 IKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDlGPAESYLNIERIIDVAKQANVDAIHP 83
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGP-RVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 84 GYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKAT 163
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 164 SGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVE 243
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 244 VAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGDE-FFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAGAD 322
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 323 LfgeeinMPQQKDITTLGYAIQCRITTEDPlNDFMPDTGTIIAYRSSGGFGVRLDAGDGfQGAEISPYYDSLLVKLSTHA 402
Cdd:PRK06111 321 L------SFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVE-NGVTVTPFYDPMIAKLIAHG 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 586172456 403 ISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIE 451
Cdd:PRK06111 393 ETREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLT 441
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
533-1147 |
0e+00 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 564.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 533 VLLTDTTFRDAHQSLLATRVRTKDMINIASKTADVfkdGF-SLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQM 611
Cdd:PRK09282 4 VKITDTTLRDAHQSLLATRMRTEDMLPIAEKLDKV---GFwSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPLQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 612 LLRASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTgdilnpeRSNIYTL 691
Cdd:PRK09282 81 LLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT-------TSPVHTI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 692 EYYVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASM 771
Cdd:PRK09282 154 EKYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEVDLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 772 SGLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGL 851
Cdd:PRK09282 234 AFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTIVDTRVLIHQVPGGMISNLVSQLKEQNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 852 GERFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMAlymVQNdldeqsVITDG-YKLdFPESVVSFFKGEIGQPVNGFNKD 930
Cdd:PRK09282 314 LDKLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQA---VLN------VLTGErYKV-ITKEVKDYVKGLYGRPPAPINEE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 931 LQAVILKGQEALTARPGEYLEPvDFEKVREllEEEQQGPVTEQDIISYVLYPKVYEQYIQTRNQYGNLSLLDTPTFFFGM 1010
Cdd:PRK09282 384 LRKKIIGDEEPITCRPADLLEP-ELEKARK--EAEELGKSEKEDVLTYALFPQIAKKFLEEREAGELKPEPEPKEAAAAG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1011 RNGETVEIEID-KGKRLIIKLETISEPdenGNRTIYYAMNGQARRIYIKdenVHTNANVKPKADKSNPSHIGAQMPGSVT 1089
Cdd:PRK09282 461 AEGIPTEFKVEvDGEKYEVKIEGVKAE---GKRPFYLRVDGMPEEVVVE---PLKEIVVGGRPRASAPGAVTSPMPGTVV 534
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 586172456 1090 EVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIEK 1147
Cdd:PRK09282 535 KVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
4-452 |
1.32e-175 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 523.12 E-value: 1.32e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 4 IKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSdLGPAESYLNIERIIDVAKQANVDAIHP 83
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGP-ASSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 84 GYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKAT 163
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 164 SGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVE 243
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 244 VAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGD-EFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAagad 322
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDgNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIA---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 323 lFGEEINMpQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAGdGFQGAEISPYYDSLLVKLSTHA 402
Cdd:PRK05586 317 -YGEKLSI-KQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSA-VYSGYTIPPYYDSMIGKLIVYG 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 586172456 403 ISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEE 452
Cdd:PRK05586 394 KDREEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
4-452 |
1.18e-174 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 520.86 E-value: 1.18e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 4 IKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGsDLGPAESYLNIERIIDVAKQANVDAIHP 83
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIG-PAPSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 84 GYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKAT 163
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 164 SGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVE 243
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 244 VAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGD-EFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAgad 322
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNgEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAA--- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 323 lfGEEINMpQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDaGDGFQGAEISPYYDSLLVKLSTHA 402
Cdd:TIGR00514 318 --GEPLSL-KQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWD-SHVYSGYTVPPYYDSMIGKLITYG 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 586172456 403 ISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEE 452
Cdd:TIGR00514 394 KTREVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
535-818 |
5.21e-165 |
|
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes the carboxyltransferase domains of pyruvate carboxylase (PC) and the transcarboxylase (TC) 5S subunit. Transcarboxylase 5S is a cobalt-dependent metalloenzyme subunit of the biotin-dependent transcarboxylase multienzyme complex. Transcarboxylase 5S transfers carbon dioxide from the 1.3S biotin to pyruvate in the second of two carboxylation reactions catalyzed by TC. The first reaction involves the transfer of carbon dioxide from methylmalonyl-CoA to the 1.3S biotin, and is catalyzed by the 12S subunit. These two steps allow a carboxylate group to be transferred from oxaloacetate to propionyl-CoA to yield pyruvate and methylmalonyl-CoA. The catalytic domain of transcarboxylase 5S has a canonical TIM-barrel fold with a large C-terminal extension that forms a funnel leading to the active site. Transcarboxylase 5S forms a homodimer and there are six dimers per complex. In addition to the catalytic domain, transcarboxylase 5S has several other domains including a carbamoyl-phosphate synthase domain, a biotin carboxylase domain, a carboxyltransferase domain, and an ATP-grasp domain. Pyruvate carboxylase, like TC, is a biotin-dependent enzyme that catalyzes the carboxylation of pyruvate to produce oxaloacetate. In mammals, PC has critical roles in gluconeogenesis, lipogenesis, glyceroneogenesis, and insulin secretion. Inherited PC deficiencies are linked to serious diseases in humans such as lactic acidemia, hypoglycemia, psychomotor retardation, and death. PC is a single-chain enzyme and is active only in its homotetrameric form. PC has three domains, an N-terminal biotin carboxylase domain, a carboxyltransferase domain (this alignment model), and a C-terminal biotin-carboxyl carrier protein domain. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163675 Cd Length: 275 Bit Score: 488.86 E-value: 5.21e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 535 LTDTTFRDAHQSLLATRVRTKDMINIASKTADVFkdGFSLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQMLLR 614
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 615 ASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTGdilnperSNIYTLEYY 694
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTG-------SPVHTLEYY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 695 VKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASMSGL 774
Cdd:cd07937 152 VKLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVGLPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 586172456 775 TSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYYSDF 818
Cdd:cd07937 232 TSQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
2-451 |
2.03e-162 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 489.65 E-value: 2.03e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 2 KQIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDLGpAESYLNIERIIDVAKQANVDAI 81
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHA-AKSYLNPAAILAAARQCGADAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 82 HPGYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIK 161
Cdd:PRK12833 82 HPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 162 ATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHgNIVHLFERDCSVQRRHQKV 241
Cdd:PRK12833 162 AAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 242 VEVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLV--SGDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAA 319
Cdd:PRK12833 241 LEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFddARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 320 GADLfgeeinMPQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAgDGFQGAEISPYYDSLLVKLS 399
Cdd:PRK12833 321 GEPL------RFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDS-LLYPGYRVPPFYDSLLAKLI 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 586172456 400 THAISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIE 451
Cdd:PRK12833 394 VHGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-452 |
1.25e-161 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 486.94 E-value: 1.25e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1 MKQIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDLGpAESYLNIERIIDVAKQANVDA 80
Cdd:PRK08462 1 KKEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKS-SESYLNIPAIISAAEIFEADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 81 IHPGYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMI 160
Cdd:PRK08462 80 IFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 161 KATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQK 240
Cdd:PRK08462 160 KAAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 241 VVEVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLV-SGDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAA 319
Cdd:PRK08462 240 LIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLdSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 320 GADLfgeeinmPQQKDITTLGYAIQCRITTEDPlNDFMPDTGTIIAYRSSGGFGVRLDAgDGFQGAEISPYYDSLLVKLS 399
Cdd:PRK08462 320 GEEL-------PSQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMDS-HAYAGYVVPPYYDSMIGKLI 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 586172456 400 THAISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEE 452
Cdd:PRK08462 391 VWGEDRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
533-994 |
9.80e-161 |
|
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate/oxaloacetate carboxyltransferase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 444040 [Multi-domain] Cd Length: 540 Bit Score: 488.25 E-value: 9.80e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 533 VLLTDTTFRDAHQSLLATRVRTKDMINIASKTADVfkdGF-SLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQM 611
Cdd:COG5016 4 VKITDTTLRDGHQSLFATRMRTEDMLPIAEKLDEA---GFwSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 612 LLRASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTGdilnperSNIYTL 691
Cdd:COG5016 81 LLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYTI-------SPVHTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 692 EYYVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASM 771
Cdd:COG5016 154 EYYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEALDIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 772 SGLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGL 851
Cdd:COG5016 234 AGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGVDPRVLVHQVPGGMLSNLVSQLKEQGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 852 GERFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMAlymVQNdldeqsVITDG-YKLdFPESVVSFFKGEIGQPVNGFNKD 930
Cdd:COG5016 314 LDRLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQA---VLN------VLTGErYKM-ITKEVKDYVLGYYGKTPAPIDPE 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586172456 931 LQAVILKGQEALTARPGEYLEPvDFEKVRelleeEQQGPVTEQDIISYVLYPKVYEQYIQTRNQ 994
Cdd:COG5016 384 VRKKALGDEEPITCRPADLLEP-ELEKLR-----KEGLAKSDEDVLTYALFPQVAIKFLKGRAA 441
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
535-1142 |
4.57e-160 |
|
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate decarboxylase alpha subunit and its equivalents in archaea. The oxaloacetate decarboxylase Na+ pump is the paradigm of the family of Na+ transport decarboxylases that present in bacteria and archaea. It a multi subunit enzyme consisting of a peripheral alpha-subunit and integral membrane subunits beta and gamma. The energy released by the decarboxylation reaction of oxaloacetate is coupled to Na+ ion pumping across the membrane. [Transport and binding proteins, Cations and iron carrying compounds, Energy metabolism, Other]
Pssm-ID: 273447 [Multi-domain] Cd Length: 582 Bit Score: 488.15 E-value: 4.57e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 535 LTDTTFRDAHQSLLATRVRTKDMINIASKTADVfkdGF-SLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQMLL 613
Cdd:TIGR01108 1 ITDVVLRDAHQSLFATRMRTEDMLPIAEKLDDV---GYwSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 614 RASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTgdilnpeRSNIYTLEY 693
Cdd:TIGR01108 78 RGQNLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT-------TSPVHTLET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 694 YVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASMSG 773
Cdd:TIGR01108 151 YLDLAEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRFGLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 774 LTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGLGE 853
Cdd:TIGR01108 231 GTSHPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFEGQLKGPDSRILVAQVPGGMLSNLESQLKEQNALD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 854 RFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMALYMVqndldeqsVITDGYKLDFPEsVVSFFKGEIGQPVNGFNKDLQA 933
Cdd:TIGR01108 311 KLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNV--------LTGERYKTITKE-TKGYLKGEYGRTPAPINAELQR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 934 VILKGQEA-LTARPGEYLEPvDFEKVRELLEEEQQGPVTEQDIISYVLYPKVYEQYIQTRNQygnlslldtPTFFFGMrn 1012
Cdd:TIGR01108 382 KILGDEKPiVDCRPADLLEP-ELDKLRAEVREAGAEKNSIEDVLTYALFPQVGLKFLENRHN---------PAAFEPK-- 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1013 GETVEIEIDKGKRLIIKLETIsepdenGNRTIYYAMNGQARRIYIKDENVHTNAN-----------VKPKADKSNPshIG 1081
Cdd:TIGR01108 450 PEEKVIEQEHAQVVGKYEETH------ASGSYTVEVEGKAFVVKVSPGGDVSQITasapantsggtVAAKAGAGTP--VT 521
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586172456 1082 AQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLL 1142
Cdd:TIGR01108 522 APIAGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREILVKVGDAVSVGQVL 582
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
3-452 |
5.82e-151 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 460.43 E-value: 5.82e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 3 QIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDlgPAESYLNIERIIDVAKQANVDAIH 82
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTD--PIKGYLDVKRIVEIAKACGADAIH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 83 PGYGFLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDgPIKSYELA--KEFAEEAGFPLMI 160
Cdd:PRK08463 79 PGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTE-KLNSESMEeiKIFARKIGYPVIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 161 KATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQK 240
Cdd:PRK08463 158 KASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 241 VVEVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSG-DEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAA 319
Cdd:PRK08463 238 VIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDyNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 320 GadlfgeEINMPQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAgDGFQGAEISPYYDSLLVKLS 399
Cdd:PRK08463 318 G------EILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDS-HIYKDYTIPPYYDSMLAKLI 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 586172456 400 THAISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEE 452
Cdd:PRK08463 391 VKATSYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIET 443
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
535-1145 |
1.31e-142 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 442.83 E-value: 1.31e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 535 LTDTTFRDAHQSLLATRVRTKDMINIASKTADVfkdGF-SLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQMLL 613
Cdd:PRK14040 7 ITDVVLRDAHQSLFATRLRLDDMLPIAAKLDKV---GYwSLESWGGATFDACIRFLGEDPWERLRELKKAMPNTPQQMLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 614 RASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTgdilnpeRSNIYTLEY 693
Cdd:PRK14040 84 RGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT-------TSPVHTLQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 694 YVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASMSG 773
Cdd:PRK14040 157 WVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRVDVPLHLHCHATTGLSTATLLKAIEAGIDGVDTAISSMSM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 774 LTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGLGE 853
Cdd:PRK14040 237 TYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNMESQLKEQGAAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 854 RFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMAlymVQNdldeqsVIT-DGYKLDFPESvVSFFKGEIGQPVNGFNKDLQ 932
Cdd:PRK14040 317 KLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQA---VLN------VLTgERYKTITKET-AGVLKGEYGATPAPVNAELQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 933 AVILKGQEALTARPGEYLEPvDFEKVR-ELLEEEQQGPVT-----EQDIISYVLYPKVYEQYIQTRNQygnlslldtPTF 1006
Cdd:PRK14040 387 ARVLEGAEPITCRPADLLAP-ELDKLEaELRRQAQEKGITlaenaIDDVLTYALFPQIGLKFLENRHN---------PAA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1007 F--------------FGMRNGETVEIEIDkGKRLIIKletISEpdengnrtiyyamNGQARRIYIKDENVHTNANVKPKA 1072
Cdd:PRK14040 457 FepvpqaeaaqpaakAEPAGSETYTVEVE-GKAYVVK---VSE-------------GGDISQITPAAPAAAPAAAAAAAP 519
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586172456 1073 DKSNPSHIGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEI 1145
Cdd:PRK14040 520 AAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
533-992 |
9.95e-127 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 395.61 E-value: 9.95e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 533 VLLTDTTFRDAHQSLLATRVRTKDMINIASKTADVfkdGF-SLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQM 611
Cdd:PRK12331 4 IKITETVLRDGQQSLIATRMTTEEMLPILEKLDNA---GYhSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 612 LLRASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTgdilnpeRSNIYTL 691
Cdd:PRK12331 81 LLRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT-------TSPVHTI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 692 EYYVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASM 771
Cdd:PRK12331 154 DYFVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAVTVPLEVHTHATSGIAEMTYLKAIEAGADIIDTAISPF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 772 SGLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYYSDfESDIK------SPNTEIYQheMPGGQYSNLSQQ 845
Cdd:PRK12331 234 AGGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYRE-EGILNpkvkdvEPKTLIYQ--VPGGMLSNLLSQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 846 AKSLGLGERFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMALYmvqndldeqSVIT-DGYKLdFPESVVSFFKGEIGQPV 924
Cdd:PRK12331 311 LKEQGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQALM---------NVISgERYKM-VPNEIKDYVRGLYGRPP 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586172456 925 NGFNKDLQAVILKGQEALTARPGEYLEPvDFEKVRellEEEQQGPVTEQDIISYVLYPKVYEQYIQTR 992
Cdd:PRK12331 381 APIAEEIKKKIIGDEEVITCRPADLIEP-QLEKLR---EEIAEYAESEEDVLSYALFPQQAKDFLGRR 444
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
534-1146 |
1.02e-116 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 374.44 E-value: 1.02e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 534 LLTDTTFRDAHQSLLATRVRTKDMINIASKTADVfkdGF-SLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQML 612
Cdd:PRK14042 5 FITDVTLRDAHQCLIATRMRTEDMLPICNKMDDV---GFwAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 613 LRASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTgdilnpeRSNIYTLE 692
Cdd:PRK14042 82 LRGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYT-------TSPVHTLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 693 YYVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASMS 772
Cdd:PRK14042 155 NFLELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLKQATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 773 GLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGLG 852
Cdd:PRK14042 235 GGASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLYQVPGGMISNLYNQLKEQNAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 853 ERFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMALYMVQNDlDEQSVITDGYKLdfpesvvsFFKGEIGQPVNGFNKDLQ 932
Cdd:PRK14042 315 DKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQAVINVLTG-ERYKTITNEVKL--------YCQGKYGTPPGKISSALR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 933 AVILKGQEALTARPGEYLEpvdfEKVRELLEEEQQGPVTEQDIISYVLYPKVYEQYIQTRNqygNLSLLDTPTFFFGMRN 1012
Cdd:PRK14042 386 KKAIGRTEVIEVRPGDLLP----NELDQLQNEISDLALSDEDVLLYAMFPEIGRQFLEQRK---NNQLIPEPLLTQSSAP 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1013 GETVEIEID---KGKRLIIKLETISEPdENGNRTIYYAMNGQARRIYIKDENVHTNANVKPKADKSNPSHIGAQMPGSVT 1089
Cdd:PRK14042 459 DNSVMSEFDiilHGESYHVKVAGYGMI-EHGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIPGSII 537
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 586172456 1090 EVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIE 1146
Cdd:PRK14042 538 AIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
533-995 |
6.30e-109 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 349.08 E-value: 6.30e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 533 VLLTDTTFRDAHQSLLATRVRTKDMINIASKTADVfkdGF-SLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQM 611
Cdd:PRK14041 3 VMFVDTTLRDGHQSLIATRMRTEDMLPALEAFDRM---GFySMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 612 LLRASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTgdilnpeRSNIYTL 691
Cdd:PRK14041 80 LLRGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT-------VSPVHTL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 692 EYYVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASM 771
Cdd:PRK14041 153 EYYLEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKFGVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 772 SGLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGL 851
Cdd:PRK14041 233 SMGTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYDVGMKSPDSRILVSQIPGGMYSNLVKQLKEQKM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 852 GERFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMALYMVqndldeqsVITDGYKLDFPEsVVSFFKGEIGQPVNGFNKDL 931
Cdd:PRK14041 313 LHKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQAVLNV--------LTGERYKRVTNE-TKNYVKGLYGRPPAPIDEEL 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586172456 932 QAVILKGQEALTARPGEYLEPvDFEKVRELLEEEQQgpvTEQDIISYVLYPKVYEQYIqtRNQY 995
Cdd:PRK14041 384 MKKILGDEKPIDCRPADLLEP-ELEKARKELGILAE---TDEDLLIYVILGEVGKKFL--KKKY 441
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
535-994 |
4.74e-105 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 339.81 E-value: 4.74e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 535 LTDTTFRDAHQSLLATRVRTKDMINIAsktADVFKDGF-SLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQMLL 613
Cdd:PRK12330 7 VTELALRDAHQSLMATRMAMEDMVGAC---EDIDNAGYwSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQMLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 614 RASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTgdilnpeRSNIYTLEY 693
Cdd:PRK12330 84 RGQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYT-------VSPIHTVEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 694 YVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAV--DLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASM 771
Cdd:PRK12330 157 FVEQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgeDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAISSM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 772 S-GLTSQPSaNSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLG 850
Cdd:PRK12330 237 SlGPGHNPT-ESLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTTGVETEIFKSQIPGGMLSNMESQLKQQG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 851 LGERFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMALYmvqndldeqSVITDGYKL---DFPESVVSFFkgeiGQPVNGF 927
Cdd:PRK12330 316 AGDRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQAVF---------NVLMGRYKVltgEFADLMLGYY----GETPGER 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586172456 928 NKDL--QAVILKGQEALTARPGEYLEPvDFEKVRELLEEEQQGPVTEQDIISYVLYPKVYEQYIQTRNQ 994
Cdd:PRK12330 383 NPEVveQAKKQAKKEPITCRPADLLEP-EWDKLRAEALALEGCDGSDEDVLTYALFPQVAPKFFATRAE 450
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
829-1029 |
8.21e-103 |
|
Conserved carboxylase domain; This domain represents a conserved region in pyruvate carboxylase (PYC), oxaloacetate decarboxylase alpha chain (OADA), and transcarboxylase 5s subunit. The domain is found adjacent to the HMGL-like domain (pfam00682) and often close to the biotin_lipoyl domain (pfam00364) of biotin requiring enzymes.
Pssm-ID: 460557 [Multi-domain] Cd Length: 201 Bit Score: 322.10 E-value: 8.21e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 829 IYQHEMPGGQYSNLSQQAKSLGLGERFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMALYMVQNDLDEQSVITDGYKLDF 908
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 909 PESVVSFFKGEIGQPVNGFNKDLQAVILKGQEALTARPGEYLEPVDFEKVRELLEEEQQGPVTEQDIISYVLYPKVYEQY 988
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 586172456 989 IQTRNQYGNLSLLDTPTFFFGMRNGETVEIEIDKGKRLIIK 1029
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
530-994 |
1.13e-88 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 294.33 E-value: 1.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 530 QDDVLLTDTTFRDAHQSLLATRVRTKDMINIASKTADVfkDGFSLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLF 609
Cdd:PRK12581 10 QQQVAITETVLRDGHQSLMATRLSIEDMLPVLTILDKI--GYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 610 QMLLRASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEGTICYTgdilnpeRSNIY 689
Cdd:PRK12581 88 QMLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYT-------TSPVH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 690 TLEYYVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVA 769
Cdd:PRK12581 161 TLNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIKAMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 770 SMSGLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYY---SDFESDIKSPNTEIYQHEMPGGQYSNLSQQA 846
Cdd:PRK12581 241 PFSEGTSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYladGILDPSLLFPDPRTLQYQVPGGMLSNMLSQL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 847 KSLGLGERFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMALYMVqndldeqsVITDGYKLdFPESVVSFFKGEIGQPVNG 926
Cdd:PRK12581 321 KQANAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNV--------ILGKPYQM-VSKEIKQYLAGDYGKTPAP 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586172456 927 FNKDLQAVILKGQEALTARPGEYLEPvDFEKVRELLEEEQQgpvTEQDIISYVLYPKVYEQYIQTRNQ 994
Cdd:PRK12581 392 VNEDLKRSQIGSAPVTTNRPADQLSP-EFEVLKAEVADLAQ---TDEDVLTYALFPSVAKPFLTTKYQ 455
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
118-323 |
6.42e-88 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 282.27 E-value: 6.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 118 DKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGN 197
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 198 SEVYIERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVEVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTV 277
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 586172456 278 EFLVS--GDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAGADL 323
Cdd:pfam02786 161 EFALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
536-809 |
4.48e-71 |
|
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163674 [Multi-domain] Cd Length: 265 Bit Score: 238.12 E-value: 4.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 536 TDTTFRDAHQSLLATRvRTKDMINIASKTADVfkdGF-SLEMWGGATFDVAynFLKENPWERLERLRKAIPNVLFQMLLR 614
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDEA---GVdSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 615 ASnavgyknypdnviHKFVQESAKAGIDVFRIFDSLN--------------WVDQMKVANEAVQEAGKISEGTICYTGDi 680
Cdd:cd03174 75 NR-------------EKGIERALEAGVDEVRIFDSASethsrknlnksreeDLENAEEAIEAAKEAGLEVEGSLEDAFG- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 681 lnpersNIYTLEYYVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAV-DLPIHLHTHDTSGNGLLTYKQAIDA 759
Cdd:cd03174 141 ------CKTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALpDVPLGLHTHNTLGLAVANSLAALEA 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 586172456 760 GVDIIDTAVASMSGLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWS 809
Cdd:cd03174 215 GADRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVE 264
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
65-320 |
2.58e-67 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 227.45 E-value: 2.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 65 NIERIID----VAKQANVDAIhpgygfLSENE----QFARRCAEEGIKFIGPhlEHLDMFGDKVKARTTAIKADLPViPG 136
Cdd:COG0439 1 DIDAIIAaaaeLARETGIDAV------LSESEfaveTAAELAEELGLPGPSP--EAIRAMRDKVLMREALAAAGVPV-PG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 137 TDgPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNPkHIEVQV 216
Cdd:COG0439 72 FA-LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGR-EYSVEG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 217 IGDeHGNIVHlferdCSVQRRHQK---VVE---VAPSVgLSPTLRQRICDAAIQLMENIKYVN-AGTVEFLVSGD-EFFF 288
Cdd:COG0439 150 LVR-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDgEPYL 222
|
250 260 270
....*....|....*....|....*....|....
gi 586172456 289 IEVNPRVQVEH--TITEMVTGIDIVKTQILVAAG 320
Cdd:COG0439 223 IEINARLGGEHipPLTELATGVDLVREQIRLALG 256
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
4-108 |
5.47e-58 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 194.63 E-value: 5.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 4 IKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYLVGSDlGPAESYLNIERIIDVAKQANVDAIHP 83
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPG-PASESYLNIDAIIDAAKETGADAIHP 79
|
90 100
....*....|....*....|....*
gi 586172456 84 GYGFLSENEQFARRCAEEGIKFIGP 108
Cdd:pfam00289 80 GYGFLSENAEFARACEEAGIIFIGP 104
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
344-451 |
1.68e-49 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 170.29 E-value: 1.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 344 QCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAGdGFQGAEISPYYDSLLVKLSTHAISFKQAEEKMVRSLREMRIRG 423
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSG-VYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 586172456 424 VKTNIPFLINVMKNKKFTSGDYTTKFIE 451
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
344-452 |
1.75e-43 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 153.42 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 344 QCRITTEDPLNDFMPDTGTIIAYRSSGGFGVRLDAGdGFQGAEISPYYDSLLVKLSTHAISFKQAEEKMVRSLREMRIRG 423
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSG-VYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 586172456 424 VKTNIPFLINVMKNKKFTSGDYTTKFIEE 452
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1079-1145 |
9.51e-28 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 106.73 E-value: 9.51e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586172456 1079 HIGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEI 1145
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
533-807 |
1.12e-26 |
|
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase.
Pssm-ID: 459902 [Multi-domain] Cd Length: 264 Bit Score: 110.51 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 533 VLLTDTTFRDAHQSLlATRVRTKDMINIASKtadvfkdgfsLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQML 612
Cdd:pfam00682 2 VAICDTTLRDGEQAL-GVAFSIDEKLAIARA----------LDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 613 LRASnavgyknypDNVIHKFVQESAKAGIDVFRIFD-------------SLNWVdqMKVANEAVQEAGKisegticYTGD 679
Cdd:pfam00682 71 CRAR---------EHDIKAAVEALKGAGAVRVHVFIatsdlhrkyklgkDREEV--AKRAVAAVKAARS-------RGID 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 680 I-LNPERSNIYTLEYYVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVD--LPIHLHTHDTSGNGLLTYKQA 756
Cdd:pfam00682 133 VeFSPEDASRTDPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPnkAIISVHCHNDLGMAVANSLAA 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 586172456 757 IDAGVDIIDTAVASMSGLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHY 807
Cdd:pfam00682 213 VEAGADRVDGTVNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANL 263
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
64-295 |
6.49e-24 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 107.27 E-value: 6.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 64 LNIERIIDVAKQANVDAIHPGYGflsenEQFARRCAEE--------GIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIP 135
Cdd:COG0458 57 LTVEDVLDIIEKEKPDGVIVQFG-----GQTALNLAVEleeagileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 136 GtdGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEAeksfGNSEVYIERYIDNPKHIEVQ 215
Cdd:COG0458 132 S--GTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLERALKVS----PDHPVLIDESLLGAKEIEVD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 216 VIGDEHGNIV------HlFER------DCSVqrrhqkvveVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSG 283
Cdd:COG0458 206 VVRDGEDNVIivgimeH-IEPagvhsgDSIC---------VAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDD 275
|
250
....*....|..
gi 586172456 284 DEFFFIEVNPRV 295
Cdd:COG0458 276 GRVYVIEVNPRA 287
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1066-1146 |
4.32e-21 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 90.34 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1066 ANVKPKADKSNPSHIGAQMPGSV-------TEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIAT 1138
Cdd:COG0511 49 AAAAAAAAASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEY 128
|
....*...
gi 586172456 1139 GDLLIEIE 1146
Cdd:COG0511 129 GQPLFVIE 136
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
21-295 |
2.65e-19 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 91.53 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 21 RAAAELDISTVAIYSNEDKSSLH-RYkADESYLVGSDLGPAESYlnIERIIDVAKQANVDAIHPGY----GFLSEN-EQF 94
Cdd:COG3919 22 RSLGEAGVRVIVVDRDPLGPAARsRY-VDEVVVVPDPGDDPEAF--VDALLELAERHGPDVLIPTGdeyvELLSRHrDEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 95 arrcaEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPViPGTDgPIKSYELAKEFAEEAGFPLMIKATSG--------G 166
Cdd:COG3919 99 -----EEHYRLPYPDADLLDRLLDKERFYELAEELGVPV-PKTV-VLDSADDLDALAEDLGFPVVVKPADSvgydelsfP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 167 GGKGMRIVREESELEDAFHRAKSEAEksfgnsEVYIERYIDNPKHIEVQVIG--DEHGNIVHLFerdcSVQRRHQKVVEV 244
Cdd:COG3919 172 GKKKVFYVDDREELLALLRRIAAAGY------ELIVQEYIPGDDGEMRGLTAyvDRDGEVVATF----TGRKLRHYPPAG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 586172456 245 APSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLV--SGDEFFFIEVNPRV 295
Cdd:COG3919 242 GNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRdpRDGEYKLIEINPRF 294
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1070-1145 |
7.01e-19 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 84.53 E-value: 7.01e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586172456 1070 PKADKSNPSHIGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEI 1145
Cdd:PRK05641 77 PAPASAGENVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
25-323 |
2.92e-18 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 90.80 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 25 ELDISTVAIySNEDKSSLHRYK-ADESYLvgsdlgpaESyLNIERIIDVAKQANVDAIHPGYGFLSENeQFARRCAEEGI 103
Cdd:PRK12815 587 KEGYETIMI-NNNPETVSTDYDtADRLYF--------EP-LTLEDVLNVAEAENIKGVIVQFGGQTAI-NLAKGLEEAGL 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 104 KFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGtdGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDA 183
Cdd:PRK12815 656 TILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAY 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 184 FhrakseAEKSFGNSEVYIERYIDNpKHIEVQVIGDEH----GNIVHLFERDCSvqrrHQ-KVVEVAPSVGLSPTLRQRI 258
Cdd:PRK12815 734 L------AENASQLYPILIDQFIDG-KEYEVDAISDGEdvtiPGIIEHIEQAGV----HSgDSIAVLPPQSLSEEQQEKI 802
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586172456 259 CDAAIQLMENIKYVNAGTVEFLVSGDEFFFIEVNPRVQveHT--ITEMVTGIDIVKTQILVAAGADL 323
Cdd:PRK12815 803 RDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRAS--RTvpFVSKATGVPLAKLATKVLLGKSL 867
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1079-1145 |
3.79e-18 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 79.57 E-value: 3.79e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586172456 1079 HIGAQMPG-----SVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEI 1145
Cdd:pfam00364 2 EIKSPMIGesvreGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
45-294 |
5.79e-17 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 83.39 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 45 YKADESYLVgsdlgP---AESYlnIERIIDVAKQANVDAIHPGY----GFLSENEQfarRCAEEGIKFIGPHLEHLDMFG 117
Cdd:PRK12767 41 YFADKFYVV-----PkvtDPNY--IDRLLDICKKEKIDLLIPLIdpelPLLAQNRD---RFEEIGVKVLVSSKEVIEICN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 118 DKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRakseaeksfgN 197
Cdd:PRK12767 111 DKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEY----------V 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 198 SEVYIERYIDNPKhIEVQVIGDEHGNIVHlferdcSVQRRHQKV----VEVAPSVGlsptlRQRICDAAIQLMENIKYVN 273
Cdd:PRK12767 181 PNLIIQEFIEGQE-YTVDVLCDLNGEVIS------IVPRKRIEVrageTSKGVTVK-----DPELFKLAERLAEALGARG 248
|
250 260
....*....|....*....|.
gi 586172456 274 AGTVEFLVSGDEFFFIEVNPR 294
Cdd:PRK12767 249 PLNIQCFVTDGEPYLFEINPR 269
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
64-324 |
1.24e-16 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 85.44 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 64 LNIERIIDVAKQANVD--AIHPGyGFLSENeqFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGtdGPI 141
Cdd:TIGR01369 616 LTFEDVMNIIELEKPEgvIVQFG-GQTPLN--LAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTA 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 142 KSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEdafHRAKSEAEKSfGNSEVYIERYIDNPKHIEVQVIGDeH 221
Cdd:TIGR01369 691 TSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELR---RYLEEAVAVS-PEHPVLIDKYLEDAVEVDVDAVSD-G 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 222 GNIV--HLFErdcsvqrrHqkvVEVA-----------PSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGDEFFF 288
Cdd:TIGR01369 766 EEVLipGIME--------H---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYV 834
|
250 260 270
....*....|....*....|....*....|....*.
gi 586172456 289 IEVNPRVQVEHTITEMVTGIDIVKTQILVAAGADLF 324
Cdd:TIGR01369 835 IEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLE 870
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1080-1145 |
1.11e-15 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 74.85 E-value: 1.11e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586172456 1080 IGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEI 1145
Cdd:PRK06549 64 MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITI 129
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1078-1146 |
7.27e-15 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 70.20 E-value: 7.27e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586172456 1078 SHIGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIE 1146
Cdd:PRK08225 2 TKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
66-295 |
5.36e-14 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 77.06 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 66 IERIIdvaKQANVDAIHPGYGflsenEQFARRCA----------EEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIP 135
Cdd:PRK05294 74 VEKII---EKERPDAILPTMG-----GQTALNLAvelaesgvleKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 136 GtdGPIKSYELAKEFAEEAGFPLMIKA--TSGGGGKGmrIVREESELEDafhRAKSEAEKSfGNSEVYIERYIDNPKHIE 213
Cdd:PRK05294 146 S--GIAHSMEEALEVAEEIGYPVIIRPsfTLGGTGGG--IAYNEEELEE---IVERGLDLS-PVTEVLIEESLLGWKEYE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 214 VQVIGDEHGN--IVhlferdCSVqrrhqkvvE--------------VAPSVGLSPTLRQRICDAAIQLMENIKYVNAGT- 276
Cdd:PRK05294 218 YEVMRDKNDNciIV------CSI--------EnidpmgvhtgdsitVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCn 283
|
250 260
....*....|....*....|.
gi 586172456 277 VEFLVS--GDEFFFIEVNPRV 295
Cdd:PRK05294 284 VQFALNpkDGRYIVIEMNPRV 304
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
4-342 |
7.32e-14 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 76.58 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 4 IKKLLVANRGEIAIRifrAAAELDIS--------------TVAIYSNEDKSSLHRYKADESYLVgsDLGPAesylNIERI 69
Cdd:TIGR01369 6 IKKILVIGSGPIVIG---QAAEFDYSgsqackalkeegyrVILVNSNPATIMTDPEMADKVYIE--PLTPE----AVEKI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 70 IDVAKqanVDAIHPGYGflsenEQFARRCAEE----------GIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGtdG 139
Cdd:TIGR01369 77 IEKER---PDAILPTFG-----GQTALNLAVEleesgvlekyGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--E 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 140 PIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELedafhraKSEAEKSFGNS---EVYIERYIDNPKHIEVQV 216
Cdd:TIGR01369 147 IAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREEL-------KEIAERALSASpinQVLVEKSLAGWKEIEYEV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 217 IGDEHGNIVHLferdCSVQR-----RH--QKVVeVAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGD--EFF 287
Cdd:TIGR01369 220 MRDSNDNCITV----CNMENfdpmgVHtgDSIV-VAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDsgRYY 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 586172456 288 FIEVNPRVQVEHTITEMVTGIDIVKTQILVAAGADLFgEEINmpqqkDITTLGYA 342
Cdd:TIGR01369 295 VIEVNPRVSRSSALASKATGYPIAKVAAKLAVGYTLD-ELKN-----PVTGTTPA 343
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
94-312 |
1.96e-13 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 72.28 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 94 FARRCAEEGIKFIGPHlEHLDMFGDKVKARTTAIKADLPVipgtdgP----IKSYELAKEFAEEAGFPLMIKATSGGGGK 169
Cdd:COG0189 73 LLRQLEAAGVPVVNDP-EAIRRARDKLFTLQLLARAGIPV------PptlvTRDPDDLRAFLEELGGPVVLKPLDGSGGR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 170 GMRIVREESELEDAFhraksEAEKSFGNSEVYIERYIDNPKHIE--VQVIGDEhgnIVHLFER-----DCSVQRRHQKVV 242
Cdd:COG0189 146 GVFLVEDEDALESIL-----EALTELGSEPVLVQEFIPEEDGRDirVLVVGGE---PVAAIRRipaegEFRTNLARGGRA 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 243 EVAPsvglsptLRQRICDAAIQLMENIKYVNAGtVEFLVSGDEFFFIEVNPRVQVEHtiTEMVTGIDIVK 312
Cdd:COG0189 218 EPVE-------LTDEERELALRAAPALGLDFAG-VDLIEDDDGPLVLEVNVTPGFRG--LERATGVDIAE 277
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1086-1148 |
5.53e-12 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 70.03 E-value: 5.53e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586172456 1086 GSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIEKA 1148
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVA 180
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1080-1148 |
1.79e-11 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 68.49 E-value: 1.79e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586172456 1080 IGAQmPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIEKA 1148
Cdd:PRK11854 10 IGAD-EVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESA 77
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
71-295 |
1.95e-11 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 67.10 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 71 DVAKQANVDAIHPGYGFLSENEQFARRC------------------AEEGIKFIGPH-LEHLdmfGDKVKARTTAIKADL 131
Cdd:PRK06019 37 SPAAQVADEVIVADYDDVAALRELAEQCdvityefenvpaealdalAARVPVPPGPDaLAIA---QDRLTEKQFLDKLGI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 132 PVIPGTdgPIKSYELAKEFAEEAGFPLMIKATSGG-GGKGMRIVREESELEDAFhrakseaeKSFGNSEVYIERYIDNPK 210
Cdd:PRK06019 114 PVAPFA--VVDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEAAW--------ALLGSVPCILEEFVPFER 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 211 hiEVQVIG--DEHGNIVH--LFErdcSVQRRHQKVVEVAPSvGLSPTLRQRICDAAIQLMENIKYVnaGT--VEFLVSGD 284
Cdd:PRK06019 184 --EVSVIVarGRDGEVVFypLVE---NVHRNGILRTSIAPA-RISAELQAQAEEIASRIAEELDYV--GVlaVEFFVTGD 255
|
250
....*....|..
gi 586172456 285 EFFFI-EVNPRV 295
Cdd:PRK06019 256 GELLVnEIAPRP 267
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1080-1148 |
3.09e-11 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 67.21 E-value: 3.09e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586172456 1080 IGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIEKA 1148
Cdd:TIGR01348 124 IGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVA 192
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1086-1148 |
6.11e-11 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 66.56 E-value: 6.11e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586172456 1086 GSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIEKA 1148
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVE 281
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
140-295 |
1.22e-10 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 61.50 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 140 PIKSYELAKEFAEEAGFPLMIKATSGG-GGKGMRIVREESELEDAFhrakseaeKSFGNSEVYIERYIDNPKHIEVQVIG 218
Cdd:pfam02222 12 AAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLPQAW--------EELGDGPVIVEEFVPFDRELSVLVVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 219 DEHGNiVHLFErdcSVQRRHQK---VVEVAPSvGLSPTLRQRICDAAIQLMENIKYVNAGTVE-FLVSGDEFFFIEVNPR 294
Cdd:pfam02222 84 SVDGE-TAFYP---VVETIQEDgicRLSVAPA-RVPQAIQAEAQDIAKRLVDELGGVGVFGVElFVTEDGDLLINELAPR 158
|
.
gi 586172456 295 V 295
Cdd:pfam02222 159 P 159
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
3-342 |
3.14e-10 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 64.61 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 3 QIKKLLVANRGEIAIRifrAAAELDIS-TVAIysnedksslhryKA--DESY---LVGS-------DLGPA-ESYLN--- 65
Cdd:PRK12815 6 DIQKILVIGSGPIVIG---QAAEFDYSgTQAC------------LAlkEEGYqvvLVNPnpatimtDPAPAdTVYFEplt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 66 ---IERIIDVAKQanvDAIHPGYGflsenEQFARRCAEE----------GIKFIGPHLEHLDMFGDKVKARTTAIKADLP 132
Cdd:PRK12815 71 vefVKRIIAREKP---DALLATLG-----GQTALNLAVKlhedgileqyGVELLGTNIEAIQKGEDRERFRALMKELGEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 133 VipGTDGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAksEAEKSFgnSEVYIERYIDNPKHI 212
Cdd:PRK12815 143 V--PESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQG--LQASPI--HQCLLEESIAGWKEI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 213 EVQVIGDEHGNIVHLferdCSVQRrhqkvVE-----------VAPSVGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLV 281
Cdd:PRK12815 217 EYEVMRDRNGNCITV----CNMEN-----IDpvgihtgdsivVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFAL 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586172456 282 --SGDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAGADLfGEEINmpqqkDITTLGYA 342
Cdd:PRK12815 288 dpKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAVGYTL-NELKN-----PVTGLTYA 344
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
95-294 |
3.30e-10 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 64.73 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 95 ARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGtdGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIV 174
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 175 REESELEDAFhrakSEAEKSFGNSEVYIERYIDNPKHIEVQVIGD----------EHgnI----VHLFERDCSVqrrhqk 240
Cdd:PRK05294 724 YDEEELERYM----REAVKVSPDHPVLIDKFLEGAIEVDVDAICDgedvliggimEH--IeeagVHSGDSACSL------ 791
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 586172456 241 vvevaPSVGLSPTLRQRICDAAIQLMENIKYV---NagtVEFLVSGDEFFFIEVNPR 294
Cdd:PRK05294 792 -----PPQTLSEEIIEEIREYTKKLALELNVVglmN---VQFAVKDDEVYVIEVNPR 840
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1080-1146 |
4.52e-10 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 63.69 E-value: 4.52e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586172456 1080 IGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIE 1146
Cdd:PRK11855 10 IGEVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1086-1145 |
1.44e-09 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 55.46 E-value: 1.44e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1086 GSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEI 1145
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1086-1145 |
1.85e-09 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 55.10 E-value: 1.85e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1086 GSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEI 1145
Cdd:cd06849 15 GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
118-293 |
3.00e-09 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 59.73 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 118 DKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEAEKsfgn 197
Cdd:COG1181 95 DKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKYDDK---- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 198 seVYIERYIDnPKHIEVQVIGDEH------GNIV--HLFeRDCSVQRRHQKVVEVAPSvGLSPTLRQRICDAAIQLMENI 269
Cdd:COG1181 171 --VLVEEFID-GREVTVGVLGNGGpralppIEIVpeNGF-YDYEAKYTDGGTEYICPA-RLPEELEERIQELALKAFRAL 245
|
170 180
....*....|....*....|....*...
gi 586172456 270 K---YvnaGTVEFLVSGD-EFFFIEVNP 293
Cdd:COG1181 246 GcrgY---ARVDFRLDEDgEPYLLEVNT 270
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1086-1150 |
4.06e-09 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 60.61 E-value: 4.06e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586172456 1086 GSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIEKATD 1150
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAA 197
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1080-1146 |
4.26e-09 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 60.66 E-value: 4.26e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586172456 1080 IGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIE 1146
Cdd:TIGR01348 8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
118-324 |
7.50e-09 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 60.25 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 118 DKVKARTTAIKADLPViPGTDGPIKSYELAkEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEaeksfGN 197
Cdd:PRK02186 107 DKKRLARTLRDHGIDV-PRTHALALRAVAL-DALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRA-----GT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 198 SEVYIERYIDNPKHiEVQVIGDEHGNIV------HLFERDCSVQRRHqkvveVAPSVGLSPTlRQRICDAAIQLMENIKY 271
Cdd:PRK02186 180 RAALVQAYVEGDEY-SVETLTVARGHQVlgitrkHLGPPPHFVEIGH-----DFPAPLSAPQ-RERIVRTVLRALDAVGY 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586172456 272 -VNAGTVEFLVSGDEFFFIEVNPR-------VQVEHtitemVTGIDIVKTQILVAAGADLF 324
Cdd:PRK02186 253 aFGPAHTELRVRGDTVVIIEINPRlaggmipVLLEE-----AFGVDLLDHVIDLHLGVAAF 308
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1077-1145 |
4.64e-08 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 51.29 E-value: 4.64e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586172456 1077 PSHIGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEI 1145
Cdd:cd06663 5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
1-365 |
1.47e-07 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 54.93 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 1 MKQIKKLLVA---NRGeIAirifRAAAELDISTVAI--YSNEDkssLHRYKADESYLVGSDLGPAESYLnIERIIDVAKQ 75
Cdd:COG2232 1 MSSPPDLLIAgfsARA-LA----QSARRAGYRVYAVdlFADLD---TRALAERWVRLDAESCGFDLEDL-PAALLELAAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 76 ANVDAIHPGYGFLSENEQFARrcAEEGIKFIGPHLEHLDMFGDKVK-ARTTAiKADLPVipgtdgPiksyELAKEfAEEA 154
Cdd:COG2232 72 DDPDGLVYGSGFENFPELLER--LARRLPLLGNPPEVVRRVKDPLRfFALLD-ELGIPH------P----ETRFE-PPPD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 155 GFPLMIKATSGGGGKGMRIVREESeledafhrakseaeksFGNSEVYIERYIDNPkHIEVQVIGDEHGNIVHLFERdcsv 234
Cdd:COG2232 138 PGPWLVKPIGGAGGWHIRPADSEA----------------PPAPGRYFQRYVEGT-PASVLFLADGSDARVLGFNR---- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 235 qrrhQKVVEVAPS----------VGLSPTLRQRICDAAIQLMENIKYVNAGTVEFLVSGDEFFFIEVNPRVQVEHTITEM 304
Cdd:COG2232 197 ----QLIGPAGERpfryggnigpLALPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYED 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586172456 305 VTGIDIVKTQILvAAGADLFGEEINMPQQkditTLGYAI-----QCRITTEDPLNDF---MPDTGTIIA 365
Cdd:COG2232 273 ATGGNLFDAHLR-ACRGELPEVPRPKPRR----VAAKAIlyaprDLTIPDDLSWPPWvadIPAPGTRIE 336
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
143-306 |
1.56e-07 |
|
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439798 [Multi-domain] Cd Length: 393 Bit Score: 55.13 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 143 SYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEAEksFGNSEVYIE--------------RYIDN 208
Cdd:COG0027 137 SLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSPADIEAAWEYAQEGGR--GGAGRVIVEgfvdfdyeitlltvRAVDG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 209 PKH----IE-VQVIGDEHgnivhlferdCSVQrrhqkvvevaPsvglsptlrQRICDAAIQLMENI--KYVNA------- 274
Cdd:COG0027 215 PTHfcepIGhRQEDGDYR----------ESWQ----------P---------QPMSEAALAKAQEIakKVTDAlggrgif 265
|
170 180 190
....*....|....*....|....*....|..
gi 586172456 275 GtVEFLVSGDEFFFIEVNPRvqvEHTiTEMVT 306
Cdd:COG0027 266 G-VELFVKGDEVYFSEVSPR---PHD-TGMVT 292
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1082-1145 |
4.01e-07 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 48.27 E-value: 4.01e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586172456 1082 AQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEI 1145
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
143-306 |
4.25e-07 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 53.60 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 143 SYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEAEKsfGNSEVYIE--------------RYIDN 208
Cdd:PRK09288 137 SLEELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSPEDIEKAWEYAQEGGRG--GAGRVIVEefidfdyeitlltvRAVDG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 209 PKH----IE-VQVIGDEHgnivhlferdCSVQrrhqkvvevaPsvglsptlrQRICDAAIQLMENI--KYVNA------- 274
Cdd:PRK09288 215 GTHfcapIGhRQEDGDYR----------ESWQ----------P---------QPMSPAALEEAQEIakKVTDAlggrglf 265
|
170 180 190
....*....|....*....|....*....|..
gi 586172456 275 GtVEFLVSGDEFFFIEVNPRvqvEHTiTEMVT 306
Cdd:PRK09288 266 G-VELFVKGDEVYFSEVSPR---PHD-TGMVT 292
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
123-328 |
6.75e-07 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 53.63 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 123 RTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRA-KSEAEKSfgnseVY 201
Cdd:PLN02735 705 RFNAILNELKIEQPKGGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAvEVDPERP-----VL 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 202 IERYIDNPKHIEVQVIGDEHGNIV-------------HLFERDCSVqrrhqkvvevaPSVGLSPTLRQRICDAAIQLMEN 268
Cdd:PLN02735 780 VDKYLSDATEIDVDALADSEGNVViggimehieqagvHSGDSACSL-----------PTQTIPSSCLATIRDWTTKLAKR 848
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586172456 269 IKYVNAGTVEFLVS-GDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAGADL----FGEEI 328
Cdd:PLN02735 849 LNVCGLMNCQYAITpSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSGKSLkdlgFTEEV 913
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
129-293 |
1.03e-06 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 50.78 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 129 ADLPVIP-----GTDGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEAEKsfgnseVYIE 203
Cdd:pfam07478 5 AGLPVVPfvtftRADWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEK------VLVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 204 RYIDNPKhIEVQVIGDEHGNIVHLFER--DCSVQRRHQK-VVEVAPSV---GLSPTLRQRICDAAIQLMENIKYVNAGTV 277
Cdd:pfam07478 79 EGIEGRE-IECAVLGNEDPEVSPVGEIvpSGGFYDYEAKyIDDSAQIVvpaDLEEEQEEQIQELALKAYKALGCRGLARV 157
|
170
....*....|....*..
gi 586172456 278 EFLVSGD-EFFFIEVNP 293
Cdd:pfam07478 158 DFFLTEDgEIVLNEVNT 174
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
131-229 |
4.23e-06 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 50.93 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 131 LPVIPGTdgPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRI-VREESELEDAFHRAKSEaeksfgNSEVYIERYIDNP 209
Cdd:PRK14016 227 VPVPEGR--VVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKE------SSDVIVERYIPGK 298
|
90 100 110
....*....|....*....|....*....|....*
gi 586172456 210 KH---------------IEVQVIGDEHGNIVHLFE 229
Cdd:PRK14016 299 DHrllvvggklvaaarrEPPHVIGDGKHTIRELIE 333
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
118-220 |
5.13e-06 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 49.72 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 118 DKVKARTTAIKADLPVIPGtdGPIKSYELAKEFAEEAGFPLMIKATSGGGGKGMRIVREESELEDAFhrakSEAEKsFGN 197
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPW--IVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAAL----ELAFK-YDD 170
|
90 100
....*....|....*....|...
gi 586172456 198 sEVYIERYIDNPKhIEVQVIGDE 220
Cdd:PRK01372 171 -EVLVEKYIKGRE-LTVAVLGGK 191
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
695-774 |
7.48e-06 |
|
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163676 Cd Length: 274 Bit Score: 48.93 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 695 VKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAV-DLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVAsmsG 773
Cdd:cd07938 152 AEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERFpDEKLALHFHDTRGQALANILAALEAGVRRFDSSVG---G 228
|
.
gi 586172456 774 L 774
Cdd:cd07938 229 L 229
|
|
| DRE_TIM_HCS |
cd07948 |
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ... |
705-768 |
1.15e-05 |
|
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel domain; Homocitrate synthase (HCS) catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate, the first step in the lysine biosynthesis pathway. This family includes the Yarrowia lipolytica LYS1 protein as well as the Saccharomyces cerevisiae LYS20 and LYS21 proteins. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163685 Cd Length: 262 Bit Score: 48.48 E-value: 1.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586172456 705 GFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAV 768
Cdd:cd07948 154 GVNRVGIADTVGIATPRQVYELVRTLRGVVSCDIEFHGHNDTGCAIANAYAALEAGATHIDTTV 217
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
149-296 |
1.23e-05 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 46.61 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 149 EFAEEAGFPLMIKATSGGGGKGMRIVREESELEdafhrakseaeksFGNSEVYIERYIDNpKHIEVQVIGDEHGNIVHLF 228
Cdd:pfam02655 25 EELLREEKKYVVKPRDGCGGEGVRKVENGREDE-------------AFIENVLVQEFIEG-EPLSVSLLSDGEKALPLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586172456 229 ERdcsvQRRHQKVVEVAPSVGLSP---TLRQRICDAAIQLMENIKYVN--AGtVEFLVSGDEFFFIEVNPRVQ 296
Cdd:pfam02655 91 NR----QYIDNGGSGFVYAGNVTPsrtELKEEIIELAEEVVECLPGLRgyVG-VDLVLKDNEPYVIEVNPRIT 158
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
102-323 |
1.69e-05 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 49.39 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 102 GIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPgtDGPIKSYELAKEFAEEAG-FPLMIKA--TSGGGGKGMRIVREES 178
Cdd:PLN02735 128 GVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP--SGIATTLDECFEIAEDIGeFPLIIRPafTLGGTGGGIAYNKEEF 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 179 EledAFHRAKSEAEKsfgNSEVYIERYIDNPKHIEVQVIGDEHGNIVHLferdCSVQRRHQKVVE------VAPSVGLSP 252
Cdd:PLN02735 206 E---TICKAGLAASI---TSQVLVEKSLLGWKEYELEVMRDLADNVVII----CSIENIDPMGVHtgdsitVAPAQTLTD 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586172456 253 TLRQRICDAAIQLMENIKYVNAGT-VEFLVS--GDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAGADL 323
Cdd:PLN02735 276 KEYQRLRDYSVAIIREIGVECGGSnVQFAVNpvDGEVMIIEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTL 349
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
1083-1148 |
1.85e-05 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 48.29 E-value: 1.85e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586172456 1083 QMPGSVTEVKVS-----VGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIEKA 1148
Cdd:PRK05704 9 TLPESVTEATIAtwhkkPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEG 79
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
1086-1148 |
4.80e-05 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 47.37 E-value: 4.80e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586172456 1086 GSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIEKA 1148
Cdd:PTZ00144 59 GTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTG 121
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
682-768 |
8.17e-05 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 46.32 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 682 NPE---RSNIYTLEYYVKLAKELEREGFHILaikDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSG----NGLLtyk 754
Cdd:PRK11858 135 SAEdasRTDLDFLIEFAKAAEEAGADRVRFC---DTVGILDPFTMYELVKELVEAVDIPIEVHCHNDFGmataNALA--- 208
|
90
....*....|....
gi 586172456 755 qAIDAGVDIIDTAV 768
Cdd:PRK11858 209 -GIEAGAKQVHTTV 221
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
695-768 |
8.56e-05 |
|
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) of Streptomyces rubellomurinus catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate and CoA, a reaction similar to one catalyzed by homocitrate synthase. The gene encoding FrbC is one of several genes required for the biosynthesis of FR900098, a potent antimalarial antibiotic. This protein is also required for assembly of the nitrogenase MoFe complex but its exact role is unknown. This family also includes the NifV proteins of Heliobacterium chlorum and Gluconacetobacter diazotrophicus, which appear to be orthologous to FrbC. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163677 [Multi-domain] Cd Length: 259 Bit Score: 45.57 E-value: 8.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586172456 695 VKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSG----NGLltykQAIDAGVDIIDTAV 768
Cdd:cd07939 142 IEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAATDLPLEFHAHNDLGlataNTL----AAVRAGATHVSVTV 215
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
1084-1150 |
2.65e-04 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 44.72 E-value: 2.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586172456 1084 MPGSVTEVKVS-----VGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIEKATD 1150
Cdd:TIGR01347 8 LAESITEGTVAewhkkVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGND 79
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
1093-1146 |
4.08e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 40.00 E-value: 4.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 586172456 1093 VSVGETVKANQPLLITEAMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIE 1146
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| PRK06524 |
PRK06524 |
biotin carboxylase-like protein; Validated |
87-307 |
5.37e-04 |
|
biotin carboxylase-like protein; Validated
Pssm-ID: 180605 [Multi-domain] Cd Length: 493 Bit Score: 43.96 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 87 FLSENEQFARRCAEEGIKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAEEAGF--PLMIKATS 164
Cdd:PRK06524 111 FVMFDEETEALARQAGLEVMHPPAELRHRLDSKIVTTRLANEAGVPSVPHVLGRVDSYDELSALAHGAGLgdDLVVQTPY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 165 GGGGKGMRIVREESELedafhraKSEAEKSFGNSEVYIERYIDN-PKHIEVQVIgdEHGNIVHLFERDcsvqrrhqkVV- 242
Cdd:PRK06524 191 GDSGSTTFFVRGQRDW-------DKYAGGIVGQPEIKVMKRIRNvEVCIEACVT--RHGTVIGPAMTS---------LVg 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 243 --EVAPSVG-----------LSPTLRQricdAAIQLMENI-------KYVNAGTVEFLVSGD--EFFFIEVNPRVQVEHT 300
Cdd:PRK06524 253 ypELTPYRGgwcgndiwpgaLPPAQTR----KAREMVRKLgdvlsreGYRGYFEVDLLHDLDadELYLGEVNPRLSGASP 328
|
....*..
gi 586172456 301 ITEMVTG 307
Cdd:PRK06524 329 MTNLTTE 335
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
1116-1147 |
6.66e-04 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 38.58 E-value: 6.66e-04
10 20 30
....*....|....*....|....*....|..
gi 586172456 1116 TIQAPFDGVIKQVTVNNGDTIATGDLLIEIEK 1147
Cdd:pfam13533 4 KIASPVSGKVVAVNVKEGQQVKKGDVLATLDS 35
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
65-207 |
7.11e-04 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 43.46 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 65 NIERIIDVAKQANVDAIHPGygflSENEQFA---RRCAEEGIKFIGP-----HLEhldmfGDKVKARTTAIKADLPVIPG 136
Cdd:COG0151 50 DIEALVAFAKEENIDLVVVG----PEAPLVAgivDAFRAAGIPVFGPskaaaQLE-----GSKAFAKEFMARYGIPTAAY 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586172456 137 ---TDgpiksYELAKEFAEEAGFPLMIKAtSG-GGGKGMRIVREESELEDAFHRAKseAEKSFGN--SEVYIERYID 207
Cdd:COG0151 121 rvfTD-----LEEALAYLEEQGAPIVVKA-DGlAAGKGVVVAETLEEALAAVDDML--ADGKFGDagARVVIEEFLE 189
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
92-225 |
1.40e-03 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 42.74 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 92 EQFARRCA----EegIKFIGPH-LEHLDMFGDKV--KARTTAI------------KADLPVIPGTDgpIKSYELAKEFAE 152
Cdd:PLN02948 78 REFAKRCDvltvE--IEHVDVDtLEALEKQGVDVqpKSSTIRIiqdkyaqkvhfsKHGIPLPEFME--IDDLESAEKAGD 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586172456 153 EAGFPLMIKATSGG-GGKGMRIVREESELEDAFhrakseaeKSFGNSE--VYIERYIDNPKHIEVQVIGDEHGNIV 225
Cdd:PLN02948 154 LFGYPLMLKSRRLAyDGRGNAVAKTEEDLSSAV--------AALGGFErgLYAEKWAPFVKELAVMVARSRDGSTR 221
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
1085-1146 |
3.78e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 40.70 E-value: 3.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586172456 1085 PGSVTEVKVSVGeTVKANQplliteamkmETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIE 1146
Cdd:COG0845 5 RGDVPETVEATG-TVEARR----------EVEVRARVSGRVEEVLVDEGDRVKKGQVLARLD 55
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
1116-1145 |
4.34e-03 |
|
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.
Pssm-ID: 433206 [Multi-domain] Cd Length: 104 Bit Score: 38.11 E-value: 4.34e-03
10 20 30
....*....|....*....|....*....|
gi 586172456 1116 TIQAPFDGVIKQVTVNNGDTIATGDLLIEI 1145
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATI 30
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
686-771 |
5.03e-03 |
|
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy 2-ketovalerate aldolase (Also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. This family includes the Escherichia coli MhpE aldolase, the Pseudomonas DmpG aldolase, and the Burkholderia xenovorans BphI pyruvate aldolase. In Pseudomonas, the DmpG aldolase tightly associates with a dehydrogenase (DmpF ) and is inactive without it. HOA has a canonical TIM-barrel fold with a C-terminal extension that forms a funnel leading to the active site. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163681 Cd Length: 263 Bit Score: 40.17 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 686 SNIYTLEYYVKLAKELEREGFHILAIKDMAGLLKPKAAYELIGELKSAVDL-PIHLHTHDTSGNGLLTYKQAIDAGVDII 764
Cdd:cd07943 135 SHMASPEELAEQAKLMESYGADCVYVTDSAGAMLPDDVRERVRALREALDPtPVGFHGHNNLGLAVANSLAAVEAGATRI 214
|
....*..
gi 586172456 765 DTAVASM 771
Cdd:cd07943 215 DGSLAGL 221
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1114-1145 |
5.50e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.42 E-value: 5.50e-03
10 20 30
....*....|....*....|....*....|..
gi 586172456 1114 ETTIQAPFDGVIKQVTVNNGDTIATGDLLIEI 1145
Cdd:COG1566 207 RTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTI 238
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
102-218 |
5.86e-03 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 40.10 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586172456 102 GIKFIGPHLEH--LDMfgDKVKARTTAIKADLPVIPG---TDGPIKSYELAkEFAEEAGFPLMIKATSGGGGKGMRIVRE 176
Cdd:PRK01966 107 GIPYVGCGVLAsaLSM--DKILTKRLLAAAGIPVAPYvvlTRGDWEEASLA-EIEAKLGLPVFVKPANLGSSVGISKVKN 183
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 586172456 177 ESELEDAFHRAKSEAEKsfgnseVYIERYIdNPKHIEVQVIG 218
Cdd:PRK01966 184 EEELAAALDLAFEYDRK------VLVEQGI-KGREIECAVLG 218
|
|
| |
