|
Name |
Accession |
Description |
Interval |
E-value |
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
22-1170 |
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: 2037.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 22 KILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEEGQYTPVGAYLAMDEIIEIAKKHKVDFIHP 101
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 102 GYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIKAA 181
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 182 FGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVVE 261
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 262 VAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAGAT 341
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 342 L--TQLGL-LQDKITTRGFSIQCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDGGNAYAGATISPHYDSMLVKCSCSG 418
Cdd:TIGR01235 321 LptPQLGVpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 419 STYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFIDDTPQLFQMVSSQNRAQKLLHYLADLAVNGsS 498
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNG-H 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 499 IKGQIGLPKLKSNPSVPHLHDAQGNVinvtksapPSGWRQVLLEKGPSEFAKQVRQFNGTLLMDTTWRDAHQSLLATRVR 578
Cdd:TIGR01235 480 PEAKDKLKPLENAPRVVVLYADQNPV--------PRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVR 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 579 THDLATIAPTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLRGANGVAYSSLPDNAIDHFV 658
Cdd:TIGR01235 552 THDLAKIAPTTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFV 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 659 KQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSGDMLQPGK-KYNLDYYLEVVEKIVQMGTHILGIKDM 737
Cdd:TIGR01235 632 KQAAQGGIDIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARpKYDLKYYTNLAVELEKAGAHILGIKDM 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 738 AGTMKPAAAKLLIGSLRTRYpDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSGLTSQPSINALLASLEGN-ID 816
Cdd:TIGR01235 712 AGLLKPAAAKLLIKALREKT-DLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSeRD 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 817 TGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLGLGEQWAETKRAYREANYLLGDIV 896
Cdd:TIGR01235 791 PGLNVAWIRELSAYWEAVRNLYAAFESDLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIV 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 897 KVTPTSKVVGDLAQFMVSNKLTSDDIRRLANSLDFPDSVMDFFEGLIGQPYGGFPEPLRSDVLRNkRRKLTCRPGLELEP 976
Cdd:TIGR01235 871 KVTPSSKVVGDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKG-EKPITVRPGSLLEP 949
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 977 FDLEKIREDLQNRF-GDIDECDVASYNMYPRVYEDFQKIRETYGDLSVLPTKNFLAPAEPDEEIEVTIEQGKTLIIKLQA 1055
Cdd:TIGR01235 950 ADLDAIRKDLQEKHeREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQA 1029
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1056 VGDlNKKTGQREVYFELNGELRKIRVADKSQNIQSVAKPKADVHDTHQIGAPMAGVIIEVKVHKGSLVKKGESIAVLSAM 1135
Cdd:TIGR01235 1030 VGA-TDSQGEREVFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAM 1108
|
1130 1140 1150
....*....|....*....|....*....|....*
gi 1034701506 1136 KMEMVVSSPADGQVKDVFIRDGESVDASDLLVVLE 1170
Cdd:TIGR01235 1109 KMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
21-1169 |
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: 1868.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 21 NKILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEEGQytPVGAYLAMDEIIEIAKKHKVDFIH 100
Cdd:COG1038 5 KKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKG--PVDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 101 PGYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIKA 180
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 181 AFggggrgmrvvreG------------DDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFER 248
Cdd:COG1038 163 AA------------GgggrgmrvvrseEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFER 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 249 DCSVQRRHQKVVEVAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGID 328
Cdd:COG1038 231 DCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGID 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 329 IVSAQIQIAAGATLT--QLGLL-QDKITTRGFSIQCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDGGNAYAGATISP 405
Cdd:COG1038 311 IVQSQILIAEGYSLDdpEIGIPsQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 406 HYDSMLVKCSCSGSTYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFIDDTPQLFQMVSSQNRAQKL 485
Cdd:COG1038 391 YYDSLLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 486 LHYLADLAVNGSSIKGQIGLPKLKSnPSVPHLHdaqgnvinvTKSAPPSGWRQVLLEKGPSEFAKQVRQFNGTLLMDTTW 565
Cdd:COG1038 471 LTYLGDVTVNGPPGVKGRPKPDFPK-PKLPKVD---------LGAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTF 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 566 RDAHQSLLATRVRTHDLATIAPTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLRGANGVA 645
Cdd:COG1038 541 RDAHQSLLATRVRTRDMLKIAPATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVG 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 646 YSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSGDMLQPGK-KYNLDYYLEVVEKI 724
Cdd:COG1038 621 YTNYPDNVVRAFVKEAAEAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRtKYTLDYYVDLAKEL 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 725 VQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYpDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSGLTSQPSI 804
Cdd:COG1038 701 EKAGAHILAIKDMAGLLKPYAAYKLVKALKEEV-DLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSL 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 805 NALLASLEGNI-DTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLGLGEQWAETKR 883
Cdd:COG1038 780 NSLVAALEGTErDTGLDLDALQELSNYWEAVRKYYAPFESGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKE 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 884 AYREANYLLGDIVKVTPTSKVVGDLAQFMVSNKLTSDDIRRLANSLDFPDSVMDFFEGLIGQPYGGFPEPLRSDVLRNkR 963
Cdd:COG1038 860 MYAAVNRLFGDIVKVTPSSKVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKG-R 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 964 RKLTCRPGLELEPFDLEKIREDLQNRFG-DIDECDVASYNMYPRVYEDFQKIRETYGDLSVLPTKNFLAPAEPDEEIEVT 1042
Cdd:COG1038 939 KPITVRPGELLPPVDFDALRAELEEKLGrEPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVE 1018
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1043 IEQGKTLIIKLQAVGDLNKKtGQREVYFELNGELRKIRVADKSQNIQSVAKPKADVHDTHQIGAPMAGVIIEVKVHKGSL 1122
Cdd:COG1038 1019 IEEGKTLIIKLLAIGEPDED-GMRTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDE 1097
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*..
gi 1034701506 1123 VKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVL 1169
Cdd:COG1038 1098 VKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
21-1171 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 1750.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 21 NKILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEEGQytPVGAYLAMDEIIEIAKKHKVDFIH 100
Cdd:PRK12999 6 KKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKH--PVRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 101 PGYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIKA 180
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 181 AFggggrgmrvvreG------------DDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFER 248
Cdd:PRK12999 164 SA------------GgggrgmrivrseEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYER 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 249 DCSVQRRHQKVVEVAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGID 328
Cdd:PRK12999 232 DCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGID 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 329 IVSAQIQIAAGATLTQLGLL---QDKITTRGFSIQCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDGGNAYAGATISP 405
Cdd:PRK12999 312 IVQSQILIAEGATLHDLEIGipsQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 406 HYDSMLVKCSCSGSTYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFIDDTPQLFQMVSSQNRAQKL 485
Cdd:PRK12999 392 YYDSLLVKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 486 LHYLADLAVNGSsiKGQIGLPKLKSNPSVPHLHdaqgnvinvTKSAPPSGWRQVLLEKGPSEFAKQVRQFNGTLLMDTTW 565
Cdd:PRK12999 472 LTYIADVTVNGF--PGVKKKPPVFPDPRLPKVD---------LSAPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTF 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 566 RDAHQSLLATRVRTHDLATIAPTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLRGANGVA 645
Cdd:PRK12999 541 RDAHQSLLATRVRTKDLLRIAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVG 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 646 YSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSGDMLQPG-KKYNLDYYLEVVEKI 724
Cdd:PRK12999 621 YTNYPDNVVRAFVREAAAAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPArAKYDLDYYVDLAKEL 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 725 VQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYpDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSGLTSQPSI 804
Cdd:PRK12999 701 EKAGAHILAIKDMAGLLKPAAAYELVSALKEEV-DLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSL 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 805 NALLASLEGN-IDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLGLGEQWAETKR 883
Cdd:PRK12999 780 NSIVAALEGTeRDTGLDLDAIRKLSPYWEAVRPYYAPFESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKE 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 884 AYREANYLLGDIVKVTPTSKVVGDLAQFMVSNKLTSDDIRRLANSLDFPDSVMDFFEGLIGQPYGGFPEPLRSDVLRNKR 963
Cdd:PRK12999 860 MYAAVNRMFGDIVKVTPSSKVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEE 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 964 RkLTCRPGLELEPFDLEKIREDLQNRFG-DIDECDVASYNMYPRVYEDFQKIRETYGDLSVLPTKNFLAPAEPDEEIEVT 1042
Cdd:PRK12999 940 P-ITVRPGELLEPVDFEAERAELEEKLGrEVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVE 1018
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1043 IEQGKTLIIKLQAVGDLNKKtGQREVYFELNGELRKIRVADKSQNIQSVAKPKADVHDTHQIGAPMAGVIIEVKVHKGSL 1122
Cdd:PRK12999 1019 IEPGKTLIIKLEAIGEPDED-GMRTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDE 1097
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*....
gi 1034701506 1123 VKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVLEE 1171
Cdd:PRK12999 1098 VKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
21-468 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 658.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 21 NKILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEEgqyTPVGAYLAMDEIIEIAKKHKVDFIH 100
Cdd:COG4770 3 KKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPA---PAAESYLNIDAIIAAAKATGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 101 PGYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIKA 180
Cdd:COG4770 80 PGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 181 AFggggrgmrvvreG------------DDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFER 248
Cdd:COG4770 160 SA------------GgggkgmrvvrseEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGER 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 249 DCSVQRRHQKVVEVAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGID 328
Cdd:COG4770 228 DCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGID 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 329 IVSAQIQIAAGATltqLGLLQDKITTRGFSIQCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDGGnAYAGATISPHYD 408
Cdd:COG4770 308 LVEEQIRIAAGEP---LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYD 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 409 SMLVKCSCSGSTYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFIDD 468
Cdd:COG4770 384 SMIAKLIVWGPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIER 443
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
21-467 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 550.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 21 NKILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEegqyTP-VGAYLAMDEIIEIAKKHKVDFI 99
Cdd:PRK08591 3 DKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGP----APsKKSYLNIPAIISAAEITGADAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 100 HPGYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIK 179
Cdd:PRK08591 79 HPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 180 AAFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKV 259
Cdd:PRK08591 159 ATAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 260 VEVAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAG 339
Cdd:PRK08591 239 LEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 340 AtltQLGLLQDKITTRGFSIQCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDGGnAYAGATISPHYDSMLVKCSCSGS 419
Cdd:PRK08591 319 E---PLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMIGKLIVHGE 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1034701506 420 TYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFID 467
Cdd:PRK08591 395 TREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLE 442
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
21-485 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 549.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 21 NKILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEEgqyTPVGAYLAMDEIIEIAKKHKVDFIH 100
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPA---PPSKSYLNIERIIDVAKKAGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 101 PGYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIKA 180
Cdd:PRK08654 80 PGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 181 AFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVV 260
Cdd:PRK08654 160 SAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 261 EVAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNrHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAGA 340
Cdd:PRK08654 240 EEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGN-FYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 341 TLTqlgLLQDKITTRGFSIQCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDGGnAYAGATISPHYDSMLVKCSCSGST 420
Cdd:PRK08654 319 ELS---FKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSG-VHMGYEIPPYYDSMISKLIVWGRT 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 421 YEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFIDDTPQLFQ-----MVSSQNRAQKL 485
Cdd:PRK08654 395 REEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTILEemkryALEEEEREKTL 464
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
21-468 |
4.06e-172 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 514.96 E-value: 4.06e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 21 NKILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEegqyTPVG-AYLAMDEIIEIAKKHKVDFI 99
Cdd:PRK06111 3 QKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGG----PRVQeSYLNLEKIIEIAKKTGAEAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 100 HPGYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIK 179
Cdd:PRK06111 79 HPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 180 AAFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKV 259
Cdd:PRK06111 159 ASAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 260 VEVAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAG 339
Cdd:PRK06111 239 IEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 340 ATLTqlgLLQDKITTRGFSIQCRITTEDPsKNFQPDTGRLEVYRSAGGNGVRLDgGNAYAGATISPHYDSMLVKCSCSGS 419
Cdd:PRK06111 319 EKLS---FTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHD-HAVENGVTVTPFYDPMIAKLIAHGE 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1034701506 420 TYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFIDD 468
Cdd:PRK06111 394 TREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTK 442
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
22-495 |
7.48e-167 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 502.33 E-value: 7.48e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 22 KILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEEgqytPVGAYLAMDEIIEIAKKHKVDFIHP 101
Cdd:PRK07178 4 KILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD----PLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 102 GYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIKAA 181
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 182 FGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVVE 261
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 262 VAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAGAT 341
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 342 LTqlgLLQDKITTRGFSIQCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDGGnAYAGATISPHYDSMLVKCSCSGSTY 421
Cdd:PRK07178 320 LS---YKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTA-IYTGYTIPPYYDSMCAKLIVWALTW 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034701506 422 EIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFIDDTPQLFQMVSSQNRAQKLLHYLADLAVN 495
Cdd:PRK07178 396 EEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNYSIKRKPEELAAAIAAAIAAH 469
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
22-467 |
1.21e-159 |
|
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: 482.72 E-value: 1.21e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 22 KILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEEGQytpVGAYLAMDEIIEIAKKHKVDFIHP 101
Cdd:TIGR00514 4 KILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPS---AKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 102 GYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIKAA 181
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 182 FGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVVE 261
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 262 VAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAGat 341
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAG-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 342 lTQLGLLQDKITTRGFSIQCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDgGNAYAGATISPHYDSMLVKCSCSGSTY 421
Cdd:TIGR00514 319 -EPLSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWD-SHVYSGYTVPPYYDSMIGKLITYGKTR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1034701506 422 EIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFID 467
Cdd:TIGR00514 397 EVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLE 442
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
21-468 |
6.33e-158 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 478.05 E-value: 6.33e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 21 NKILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEEgqyTPVGAYLAMDEIIEIAKKHKVDFIH 100
Cdd:PRK05586 3 KKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPA---SSKDSYLNIQNIISATVLTGAQAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 101 PGYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIKA 180
Cdd:PRK05586 80 PGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 181 AFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVV 260
Cdd:PRK05586 160 SAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 261 EVAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAGa 340
Cdd:PRK05586 240 EEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYG- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 341 tlTQLGLLQDKITTRGFSIQCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDgGNAYAGATISPHYDSMLVKCSCSGST 420
Cdd:PRK05586 319 --EKLSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVD-SAVYSGYTIPPYYDSMIGKLIVYGKD 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1034701506 421 YEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFIDD 468
Cdd:PRK05586 396 REEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
560-841 |
1.84e-155 |
|
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: 464.60 E-value: 1.84e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 560 LMDTTWRDAHQSLLATRVRTHDLATIAPTTAHAlaGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLR 639
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEA--GFFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 640 GANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSGDmlqpgKKYNLDYYLE 719
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS-----PVHTLEYYVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 720 VVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYPdLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSGLT 799
Cdd:cd07937 154 LAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVG-LPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGGT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1034701506 800 SQPSINALLASLEGN-IDTGINVEHVRELDAYWAEMRLLYSCF 841
Cdd:cd07937 233 SQPSTESMVAALRGTgRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
562-1170 |
3.60e-149 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 460.85 E-value: 3.60e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 562 DTTWRDAHQSLLATRVRTHDLATIAPttahAL--AGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLR 639
Cdd:PRK09282 8 DTTLRDAHQSLLATRMRTEDMLPIAE----KLdkVGFWSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPLQMLLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 640 GANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSgdmlqPGKKYNLDYYLE 719
Cdd:PRK09282 84 GQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT-----TSPVHTIEKYVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 720 VVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYpDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSGLT 799
Cdd:PRK09282 159 LAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEV-DLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISPLAFGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 800 SQPSINALLASLEGN-IDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLG----L 874
Cdd:PRK09282 238 SQPPTESMVAALKGTpYDTGLDLELLFEIAEYFREVRKKYKQFESEFTIVDTRVLIHQVPGGMISNLVSQLKEQNaldkL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 875 GEQWAETKRAYREanylLGDIVKVTPTSKVVGDLAqfmVSNKLTSDDIRRLansldfPDSVMDFFEGLIGQPyggfPEPL 954
Cdd:PRK09282 318 DEVLEEIPRVRED----LGYPPLVTPTSQIVGTQA---VLNVLTGERYKVI------TKEVKDYVKGLYGRP----PAPI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 955 RSDVlrnkRRK-------LTCRPGLELEPfDLEKIREDLQnRFGDIDECDVASYNMYPRVYEDFQKIRETyGDLSVLPTK 1027
Cdd:PRK09282 381 NEEL----RKKiigdeepITCRPADLLEP-ELEKARKEAE-ELGKSEKEDVLTYALFPQIAKKFLEEREA-GELKPEPEP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1028 NFLAPAEPDE---EIEVTIEqGKTLIIKLQAVGDlnkkTGQREVYFELNGELRKIRVADKSQnIQSVAKPKADVHDThqI 1104
Cdd:PRK09282 454 KEAAAAGAEGiptEFKVEVD-GEKYEVKIEGVKA----EGKRPFYLRVDGMPEEVVVEPLKE-IVVGGRPRASAPGA--V 525
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034701506 1105 GAPMAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVLE 1170
Cdd:PRK09282 526 TSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
22-467 |
7.22e-147 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 450.42 E-value: 7.22e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 22 KILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEEgqytPVGAYLAMDEIIEIAKKHKVDFIHP 101
Cdd:PRK08463 4 KILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTD----PIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 102 GYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGT-PGPIETVQEALDFVNEYGYPVIIKA 180
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTeKLNSESMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 181 AFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVV 260
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 261 EVAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAGA 340
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 341 TLTqlgLLQDKITTRGFSIQCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDgGNAYAGATISPHYDSMLVKCSCSGST 420
Cdd:PRK08463 320 ILD---LEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVD-SHIYKDYTIPPYYDSMLAKLIVKATS 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1034701506 421 YEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFID 467
Cdd:PRK08463 396 YDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIE 442
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
21-467 |
7.85e-142 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 436.88 E-value: 7.85e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 21 NKILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGeegqytPVGA---YLAMDEIIEIAKKHKVD 97
Cdd:PRK12833 6 RKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIG------PSHAaksYLNPAAILAAARQCGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 98 FIHPGYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVI 177
Cdd:PRK12833 80 AIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 178 IKAAFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHgNVVHLFERDCSVQRRHQ 257
Cdd:PRK12833 160 IKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 258 KVVEVAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDN-QNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQI 336
Cdd:PRK12833 239 KILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDaRGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 337 AAGAtltQLGLLQDKITTRGFSIQCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDgGNAYAGATISPHYDSMLVKCSC 416
Cdd:PRK12833 319 ADGE---PLRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVD-SLLYPGYRVPPFYDSLLAKLIV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1034701506 417 SGSTYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFID 467
Cdd:PRK12833 395 HGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
562-1166 |
4.97e-136 |
|
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: 425.74 E-value: 4.97e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 562 DTTWRDAHQSLLATRVRTHDLATIAptTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLRGA 641
Cdd:TIGR01108 3 DVVLRDAHQSLFATRMRTEDMLPIA--EKLDDVGYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLRGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 642 NGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSgdmLQPgkKYNLDYYLEVV 721
Cdd:TIGR01108 81 NLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT---TSP--VHTLETYLDLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 722 EKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYpDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSGLTSQ 801
Cdd:TIGR01108 156 EELLEMGVDSICIKDMAGILTPKAAYELVSALKKRF-GLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGGTSH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 802 PSINALLASLEGN-IDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLG----LGE 876
Cdd:TIGR01108 235 PPTETMVAALRGTgYDTGLDIELLLEIAAYFREVRKKYSQFEGQLKGPDSRILVAQVPGGMLSNLESQLKEQNaldkLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 877 QWAETKRAYREanylLGDIVKVTPTSKVVGDLAqfmVSNKLTSDDIRRLANsldfpdSVMDFFEGLIGQPYGGFPEPLRS 956
Cdd:TIGR01108 315 VLEEIPRVRED----LGYPPLVTPTSQIVGTQA---VLNVLTGERYKTITK------ETKGYLKGEYGRTPAPINAELQR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 957 DVLRNKRRKLTCRPGLELEPfDLEKIREDLQnRFGDIDEC--DVASYNMYPRVYEDFQKIRETYGDLSVLP----TKNFL 1030
Cdd:TIGR01108 382 KILGDEKPIVDCRPADLLEP-ELDKLRAEVR-EAGAEKNSieDVLTYALFPQVGLKFLENRHNPAAFEPKPeekvIEQEH 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1031 APA-----EPDEEIEVTIEQ-GKTLIIKLQAVGDLNKKTGQrevyfelngelrkirvadkSQNIQSVAKPKADVHDTHQI 1104
Cdd:TIGR01108 460 AQVvgkyeETHASGSYTVEVeGKAFVVKVSPGGDVSQITAS-------------------APANTSGGTVAAKAGAGTPV 520
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034701506 1105 GAPMAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLL 1166
Cdd:TIGR01108 521 TAPIAGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREILVKVGDAVSVGQVL 582
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
560-1131 |
3.84e-134 |
|
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: 419.30 E-value: 3.84e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 560 LMDTTWRDAHQSLLATRVRTHDLATIAPttahAL--AGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQML 637
Cdd:COG5016 6 ITDTTLRDGHQSLFATRMRTEDMLPIAE----KLdeAGFWSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 638 LRGANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYsgdMLQPgkKYNLDYY 717
Cdd:COG5016 82 LRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISY---TISP--VHTVEYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 718 LEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYpDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSG 797
Cdd:COG5016 157 VELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEAL-DIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPLAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 798 LTSQPSINALLASLEG-NIDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLG--- 873
Cdd:COG5016 236 GTSQPPTESMVAALKGtGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGVDPRVLVHQVPGGMLSNLVSQLKEQGald 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 874 -LGEQWAETKRAYREanylLGDIVKVTPTSKVVGDLAqfmVSNKLTSDdirRLANsldFPDSVMDFFEGLIGQPYGGFPE 952
Cdd:COG5016 316 rLDEVLEEIPRVRED----LGYPPLVTPTSQIVGTQA---VLNVLTGE---RYKM---ITKEVKDYVLGYYGKTPAPIDP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 953 PLRSDVLRNKRRKlTCRPGLELEPfDLEKIREdlqnRFGDIDECDVASYNMYPRVYEDFQKIREtygdlsvlptKNFLAP 1032
Cdd:COG5016 383 EVRKKALGDEEPI-TCRPADLLEP-ELEKLRK----EGLAKSDEDVLTYALFPQVAIKFLKGRA----------AGEARP 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1033 AEPDEEIEVTIEQGKTLIIKLQAVGDLNKKTGQREVYFELNGELRKIRVADKSQNIQSVAKPKAdvhdthqIGAPMAGVI 1112
Cdd:COG5016 447 DAPLAELAAVEEVVVVAEGVVVVVVVGGGAEGVVVVVVGVPGAGAVAVVAAAAAVAAAAAAAAA-------AAAAAAGAA 519
|
570
....*....|....*....
gi 1034701506 1113 IEVKVHKGSLVKKGESIAV 1131
Cdd:COG5016 520 VKKVVAVGGAVVVGVEVVV 538
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
19-467 |
3.29e-132 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 410.68 E-value: 3.29e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 19 EKNKILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEEGQYTpvgAYLAMDEIIEIAKKHKVDF 98
Cdd:PRK08462 3 EIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSE---SYLNIPAIISAAEIFEADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 99 IHPGYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVII 178
Cdd:PRK08462 80 IFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 179 KAAFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQK 258
Cdd:PRK08462 160 KAAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 259 VVEVAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAA 338
Cdd:PRK08462 240 LIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 339 GATLTQlgllQDKITTRGFSIQCRITTEDPSKnFQPDTGRLEVYRSAGGNGVRLDgGNAYAGATISPHYDSMLVKCSCSG 418
Cdd:PRK08462 320 GEELPS----QESIKLKGHAIECRITAEDPKK-FYPSPGKITKWIAPGGRNVRMD-SHAYAGYVVPPYYDSMIGKLIVWG 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1034701506 419 STYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFID 467
Cdd:PRK08462 394 EDRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLE 442
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
560-1169 |
9.79e-118 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 377.73 E-value: 9.79e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 560 LMDTTWRDAHQSLLATRVRTHDLATIAPTTAHAlaGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLR 639
Cdd:PRK14040 7 ITDVVLRDAHQSLFATRLRLDDMLPIAAKLDKV--GYWSLESWGGATFDACIRFLGEDPWERLRELKKAMPNTPQQMLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 640 GANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSgdmLQPgkKYNLDYYLE 719
Cdd:PRK14040 85 GQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT---TSP--VHTLQTWVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 720 VVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYpDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSGLT 799
Cdd:PRK14040 160 LAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRV-DVPLHLHCHATTGLSTATLLKAIEAGIDGVDTAISSMSMTY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 800 SQPSINALLASLEG-NIDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLG----L 874
Cdd:PRK14040 239 GHSATETLVATLEGtERDTGLDILKLEEIAAYFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNMESQLKEQGaadkL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 875 GEQWAETKRAyREAnylLGDIVKVTPTSKVVGDLAqfmVSNKLTSDDIRRLANSLdfpdsvmdffEGLIGQPYGGFPEP- 953
Cdd:PRK14040 319 DEVLAEIPRV-RED---LGFIPLVTPTSQIVGTQA---VLNVLTGERYKTITKET----------AGVLKGEYGATPAPv 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 954 ---LRSDVLRNKrRKLTCRPGLELEPfDLEKIREDLQN-------RFGD--IDecDVASYNMYPRVYEDFQKIRETYGDL 1021
Cdd:PRK14040 382 naeLQARVLEGA-EPITCRPADLLAP-ELDKLEAELRRqaqekgiTLAEnaID--DVLTYALFPQIGLKFLENRHNPAAF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1022 SVLPTKNFLAPA--EPDEEIEV-TIE-QGKTLIIKlqaVGDlnkktgqrevyfelNGELRKIRVADKSQNIQSVAKPKAD 1097
Cdd:PRK14040 458 EPVPQAEAAQPAakAEPAGSETyTVEvEGKAYVVK---VSE--------------GGDISQITPAAPAAAPAAAAAAAPA 520
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034701506 1098 VHDTHQIGAPMAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVL 1169
Cdd:PRK14040 521 AAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
560-1016 |
1.02e-106 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 342.84 E-value: 1.02e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 560 LMDTTWRDAHQSLLATRVRTHDLATIAPTTAHAlaGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLR 639
Cdd:PRK12331 6 ITETVLRDGQQSLIATRMTTEEMLPILEKLDNA--GYHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQMLLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 640 GANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSgdmLQPgkKYNLDYYLE 719
Cdd:PRK12331 84 GQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT---TSP--VHTIDYFVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 720 VVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYpDLPIHVHSHDSAGtaVASMT--ACALAGADVVDVAINSMSG 797
Cdd:PRK12331 159 LAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAV-TVPLEVHTHATSG--IAEMTylKAIEAGADIIDTAISPFAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 798 LTSQPSINALLASLEG-NIDTGINVEHVRELDAYWAEMRLLY---SCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLG 873
Cdd:PRK12331 236 GTSQPATESMVAALQDlGYDTGLDLEELSEIAEYFNPIRDHYreeGILNPKVKDVEPKTLIYQVPGGMLSNLLSQLKEQG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 874 LGEQWAETKRAYREANYLLGDIVKVTPTSKVVGDLAqfmVSNKLTSDDIRRLansldfPDSVMDFFEGLIGQPyggfPEP 953
Cdd:PRK12331 316 AEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQA---LMNVISGERYKMV------PNEIKDYVRGLYGRP----PAP 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034701506 954 LRSDVLRN---KRRKLTCRPGLELEPfDLEKIREDLQNrFGDIDEcDVASYNMYPRVYEDFQKIRE 1016
Cdd:PRK12331 383 IAEEIKKKiigDEEVITCRPADLIEP-QLEKLREEIAE-YAESEE-DVLSYALFPQQAKDFLGRRE 445
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
852-1052 |
1.21e-99 |
|
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: 314.39 E-value: 1.21e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 852 VYQHEIPGGQLTNLLFQAQQLGLGEQWAETKRAYREANYLLGDIVKVTPTSKVVGDLAQFMVSNKLTSDDIRRLANSLDF 931
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 932 PDSVMDFFEGLIGQPYGGFPEPLRSDVLRNKRRkLTCRPGLELEPFDLEKIREDLQNRFG-DIDECDVASYNMYPRVYED 1010
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEP-ITCRPGDLLPPVDLEKLRKELEEKAGrETTEEDVLSYALYPKVAEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034701506 1011 FQKIRETYGDLSVLPTKNFLAPAEPDEEIEVTIEQGKTLIIK 1052
Cdd:pfam02436 160 FLKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
558-1170 |
1.00e-95 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 318.20 E-value: 1.00e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 558 TLLMDTTWRDAHQSLLATRVRTHDLATIAPTTAHAlaGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQML 637
Cdd:PRK14042 4 TFITDVTLRDAHQCLIATRMRTEDMLPICNKMDDV--GFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 638 LRGANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSGDMLqpgkkYNLDYY 717
Cdd:PRK14042 82 LRGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYTTSPV-----HTLDNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 718 LEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRtRYPDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSG 797
Cdd:PRK14042 157 LELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLK-QATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFSG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 798 LTSQPSINALLASL-EGNIDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLGLGE 876
Cdd:PRK14042 236 GASHPPTEALVAALtDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLYQVPGGMISNLYNQLKEQNALD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 877 QWAETKRAYREANYLLGDIVKVTPTSKVVGDLAqfmVSNKLTSDDIRRLANSLDFpdsvmdFFEGLIGQPYGGFPEPLRS 956
Cdd:PRK14042 316 KMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQA---VINVLTGERYKTITNEVKL------YCQGKYGTPPGKISSALRK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 957 DVLrNKRRKLTCRPGlELEPFDLEKiredLQNRFGDI---DEcDVASYNMYPRVYEDFQKIREtygDLSVLPTKNFLAPA 1033
Cdd:PRK14042 387 KAI-GRTEVIEVRPG-DLLPNELDQ----LQNEISDLalsDE-DVLLYAMFPEIGRQFLEQRK---NNQLIPEPLLTQSS 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1034 EPDEEIEVTIE---QGKTLIIKLQAVGDLnkKTGQREVYFELNGELRKIRVADKSQNIQSVAKPKADVHDTHQIGAPMAG 1110
Cdd:PRK14042 457 APDNSVMSEFDiilHGESYHVKVAGYGMI--EHGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIPG 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1111 VIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVLE 1170
Cdd:PRK14042 535 SIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
136-342 |
6.64e-93 |
|
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: 296.14 E-value: 6.64e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 136 DKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIKAAFGGGGRGMRVVREGDDVADAFQRATSEARTAFGN 215
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 216 GTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVVEVAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTA 295
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034701506 296 EFLVDNQN-RHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAGATL 342
Cdd:pfam02786 161 EFALDPFSgEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
559-1013 |
7.16e-89 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 295.15 E-value: 7.16e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 559 LLMDTTWRDAHQSLLATRVRTHDLATIapTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLL 638
Cdd:PRK14041 4 MFVDTTLRDGHQSLIATRMRTEDMLPA--LEAFDRMGFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQMLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 639 RGANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSgdmLQPgkKYNLDYYL 718
Cdd:PRK14041 82 RGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT---VSP--VHTLEYYL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 719 EVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYpDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSGL 798
Cdd:PRK14041 157 EFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKF-GVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPFSMG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 799 TSQPSINALLASLEGN-IDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQaqqlgLGEQ 877
Cdd:PRK14041 236 TSQPPFESMYYAFRENgKETDFDRKALKFLVEYFTKVREKYSEYDVGMKSPDSRILVSQIPGGMYSNLVKQ-----LKEQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 878 WAETK--RAYREANYL---LGDIVKVTPTSKVVGDLAqfmVSNKLTSDDIRRLANsldfpdSVMDFFEGLIGQPYGGFPE 952
Cdd:PRK14041 311 KMLHKldKVLEEVPRVrkdLGYPPLVTPTSQIVGVQA---VLNVLTGERYKRVTN------ETKNYVKGLYGRPPAPIDE 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034701506 953 PLRSDVLRNKrRKLTCRPGLELEPfDLEKIREDLqNRFGDIDEcDVASYNMYPRVYEDFQK 1013
Cdd:PRK14041 382 ELMKKILGDE-KPIDCRPADLLEP-ELEKARKEL-GILAETDE-DLLIYVILGEVGKKFLK 438
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
566-1015 |
7.75e-86 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 287.81 E-value: 7.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 566 RDAHQSLLATRVRTHDLATIAPTTAHAlaGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLRGANGVA 645
Cdd:PRK12330 13 RDAHQSLMATRMAMEDMVGACEDIDNA--GYWSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQMLLRGQNLLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 646 YSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSGDMLqpgkkYNLDYYLEVVEKIV 725
Cdd:PRK12330 91 YRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYTVSPI-----HTVEGFVEQAKRLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 726 QMGTHILGIKDMAGTMKPAAAKLLIGSLRTRY-PDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMS-GLTSQPS 803
Cdd:PRK12330 166 DMGADSICIKDMAALLKPQPAYDIVKGIKEACgEDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAISSMSlGPGHNPT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 804 iNALLASLEGN-IDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLGLG----EQW 878
Cdd:PRK12330 246 -ESLVEMLEGTgYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTTGVETEIFKSQIPGGMLSNMESQLKQQGAGdrmdEVL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 879 AETKRAYREANYllgdIVKVTPTSKVVGDLAQFmvsnkltsddirrlaNSLDFPDSVM--DFFEGLIGQpYGGFPEPLRS 956
Cdd:PRK12330 325 EEVPRVRKDAGY----PPLVTPSSQIVGTQAVF---------------NVLMGRYKVLtgEFADLMLGY-YGETPGERNP 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034701506 957 DVL-----RNKRRKLTCRPGLELEPfDLEKIREDLQ--NRFGDIDEcDVASYNMYPRVYEDFQKIR 1015
Cdd:PRK12330 385 EVVeqakkQAKKEPITCRPADLLEP-EWDKLRAEALalEGCDGSDE-DVLTYALFPQVAPKFFATR 448
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
561-833 |
2.32e-76 |
|
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: 253.15 E-value: 2.32e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 561 MDTTWRDAHQSLLATRvRTHDLATIAPTTAHAlaGAFALECWGGATFDVAmrFLHEDPWERLRKLRSLVPNIPFQMLLRG 640
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDEA--GVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 641 AngvaysslpdnaiDHFVKQAKDNGVDIFRVFDALND--------------LEQLKVGVNAVKKAGGVVEATVCYSGDMl 706
Cdd:cd03174 76 R-------------EKGIERALEAGVDEVRIFDSASEthsrknlnksreedLENAEEAIEAAKEAGLEVEGSLEDAFGC- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 707 qpgkKYNLDYYLEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYPDLPIHVHSHDSAGTAVASMTACALAGAD 786
Cdd:cd03174 142 ----KTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEAGAD 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034701506 787 VVDVAINSMSGLTSQPSINALLASLEGN-IDTGINVEHVRELDAYWAE 833
Cdd:cd03174 218 RVDGSVNGLGERAGNAATEDLVAALEGLgIDTGIDLEKLLEISRYVEE 265
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
560-1011 |
3.25e-74 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 254.27 E-value: 3.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 560 LMDTTWRDAHQSLLATRVRTHDLATIapTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLR 639
Cdd:PRK12581 15 ITETVLRDGHQSLMATRLSIEDMLPV--LTILDKIGYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRLQMLLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 640 GANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSGDMLqpgkkYNLDYYLE 719
Cdd:PRK12581 93 GQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYTTSPV-----HTLNYYLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 720 VVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTrYPDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSGLT 799
Cdd:PRK12581 168 LVKELVEMGADSICIKDMAGILTPKAAKELVSGIKA-MTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALSPFSEGT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 800 SQPSINAL-LASLEGNIDTGINVEHVRELDAYWAEMRLLY---SCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLG-- 873
Cdd:PRK12581 247 SQPATESMyLALKEAGYDITLDETLLEQAANHLRQARQKYladGILDPSLLFPDPRTLQYQVPGGMLSNMLSQLKQANae 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 874 --LGEQWAETKRAYREanylLGDIVKVTPTSKVVGDLAQFMV----SNKLTSDDIRRLansldfpdsvmdffegLIGQpY 947
Cdd:PRK12581 327 skLEEVLAEVPRVRKD----LGYPPLVTPLSQMVGTQAAMNVilgkPYQMVSKEIKQY----------------LAGD-Y 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034701506 948 GGFPEPLRSDVLRNKRRKLTC---RPGLELEPfDLEKIREDLQNrFGDIDEcDVASYNMYPRVYEDF 1011
Cdd:PRK12581 386 GKTPAPVNEDLKRSQIGSAPVttnRPADQLSP-EFEVLKAEVAD-LAQTDE-DVLTYALFPSVAKPF 449
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
21-130 |
1.65e-52 |
|
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: 179.22 E-value: 1.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 21 NKILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEEgqyTPVGAYLAMDEIIEIAKKHKVDFIH 100
Cdd:pfam00289 2 KKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPG---PASESYLNIDAIIDAAKETGADAIH 78
|
90 100 110
....*....|....*....|....*....|
gi 1034701506 101 PGYGFLSENSEFADKVVKAGITWIGPPAEV 130
Cdd:pfam00289 79 PGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
360-467 |
5.66e-50 |
|
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: 171.83 E-value: 5.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 360 QCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDGGnAYAGATISPHYDSMLVKCSCSGSTYEIVRRKMIRALIEFRIRG 439
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSG-VYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 1034701506 440 VKTNIPFLLTLLTNPVFIEGTYWTTFID 467
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
84-339 |
1.85e-48 |
|
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: 173.52 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 84 MDEII----EIAKKHKVDFIhpgygfLSEN---SEFADKVVKA-GITwiGPPAEVIDSVGDKVSARHLAARANVPtVPGT 155
Cdd:COG0439 2 IDAIIaaaaELARETGIDAV------LSESefaVETAAELAEElGLP--GPSPEAIRAMRDKVLMREALAAAGVP-VPGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 156 pGPIETVQEALDFVNEYGYPVIIKAAfggggrgmrvvrEG------------DDVADAFQRATSEARTAFGNGTCFVERF 223
Cdd:COG0439 73 -ALVDSPEEALAFAEEIGYPVVVKPA------------DGagsrgvrvvrdeEELEAALAEARAEAKAGSPNGEVLVEEF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 224 LDKPkHIEVQLLADnHGNVVHlferdCSVQRRHQK---VVE---VAPAKtLPREVRDAILTDAVKLAKVCGYRN-AGTAE 296
Cdd:COG0439 140 LEGR-EYSVEGLVR-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTE 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034701506 297 FLVDNQNRHYFIEINPRIQVEH--TITEEITGIDIVSAQIQIAAG 339
Cdd:COG0439 212 FLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALG 256
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
360-468 |
1.45e-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: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 360 QCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDGGnAYAGATISPHYDSMLVKCSCSGSTYEIVRRKMIRALIEFRIRG 439
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSG-VYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 1034701506 440 VKTNIPFLLTLLTNPVFIEGTYWTTFIDD 468
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
560-830 |
1.10e-30 |
|
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: 122.45 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 560 LMDTTWRDAHQSLLAtrvrthdlatiAPTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLR 639
Cdd:pfam00682 4 ICDTTLRDGEQALGV-----------AFSIDEKLAIARALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVLCR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 640 GAngvaysslpDNAIDHFVKQAKDNGVDIFRVFDALNDLE-QLKVG-------------VNAVKKAGGVVEATVCYSGdm 705
Cdd:pfam00682 73 AR---------EHDIKAAVEALKGAGAVRVHVFIATSDLHrKYKLGkdreevakravaaVKAARSRGIDVEFSPEDAS-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 706 lqpgkKYNLDYYLEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYPD-LPIHVHSHDSAGTAVASMTACALAG 784
Cdd:pfam00682 142 -----RTDPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAG 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034701506 785 ADVVDVAINSMSGLTSQPSINALLASLEG-NIDTGINVEHVRELDAY 830
Cdd:pfam00682 217 ADRVDGTVNGIGERAGNAALEEVAAALEGlGVDTGLDLQRLRSIANL 263
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1103-1169 |
1.88e-23 |
|
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: 94.79 E-value: 1.88e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034701506 1103 QIGAPMAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVL 1169
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1102-1169 |
8.75e-21 |
|
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: 87.27 E-value: 8.75e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034701506 1102 HQIGAPMAGV-----IIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVL 1169
Cdd:pfam00364 1 TEIKSPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1089-1170 |
3.51e-13 |
|
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: 67.61 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1089 QSVAKPKADVHDTHQIGAPMAGVI-------IEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVD 1161
Cdd:COG0511 48 PAAAAAAAAASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVE 127
|
....*....
gi 1034701506 1162 ASDLLVVLE 1170
Cdd:COG0511 128 YGQPLFVIE 136
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
87-347 |
3.73e-13 |
|
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: 73.37 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 87 IIEIAKKHKVDFIHPGYG-----FLSEnsEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGtpGPIET 161
Cdd:COG0458 62 VLDIIEKEKPDGVIVQFGgqtalNLAV--ELEEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKS--GTATS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 162 VQEALDFVNEYGYPVIIKAAFggggrgmrvvregddV-----------ADAFQRATSEARTAFGNGTCFVERFLDKPKHI 230
Cdd:COG0458 138 VEEALAIAEEIGYPVIVRPSY---------------VlggrgmgivynEEELEEYLERALKVSPDHPVLIDESLLGAKEI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 231 EVQLLADNHGNVV------HlFER------DCSVqrrhqkvveVAPAKTLPREVRDAILTDAVKLAK---VCGYRNagtA 295
Cdd:COG0458 203 EVDVVRDGEDNVIivgimeH-IEPagvhsgDSIC---------VAPPQTLSDKEYQRLRDATLKIARalgVVGLCN---I 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034701506 296 EFLVDNqNRHYFIEINPRiqVEHTIT--EEITGIDIvsAQI--QIAAGATLTQLGL 347
Cdd:COG0458 270 QFAVDD-GRVYVIEVNPR--ASRSSPfaSKATGYPI--AKIaaKLALGYTLDELGN 320
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1104-1169 |
1.40e-12 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 66.42 E-value: 1.40e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034701506 1104 IGAPMAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVL 1169
Cdd:PRK05641 87 VTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
37-314 |
1.86e-12 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 70.34 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 37 RSAHELSMRTIAIYSHEDRLSMH-RLkADEAYVIGEEGQYTPVgaylAMDEIIEIAKKHKVDFIHPGY----GFLSEN-S 110
Cdd:COG3919 22 RSLGEAGVRVIVVDRDPLGPAARsRY-VDEVVVVPDPGDDPEA----FVDALLELAERHGPDVLIPTGdeyvELLSRHrD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 111 EFADKVVkagITWigPPAEVIDSVGDKVSARHLAARANVPtVPGTpGPIETVQEALDFVNEYGYPVIIKAAfGGGGRGMR 190
Cdd:COG3919 97 ELEEHYR---LPY--PDADLLDRLLDKERFYELAEELGVP-VPKT-VVLDSADDLDALAEDLGFPVVVKPA-DSVGYDEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 191 VVREGDDV-----ADAFQRATSEARTAFGNgtCFVERFLDKPKHIE--VQLLADNHGNVVHLFerdcSVQRRHQKVVEVA 263
Cdd:COG3919 169 SFPGKKKVfyvddREELLALLRRIAAAGYE--LIVQEYIPGDDGEMrgLTAYVDRDGEVVATF----TGRKLRHYPPAGG 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1034701506 264 PAkTLPREVRDAILTDAVK--LAKVcGYRNAGTAEFLVDNQ-NRHYFIEINPRI 314
Cdd:COG3919 243 NS-AARESVDDPELEEAARrlLEAL-GYHGFANVEFKRDPRdGEYKLIEINPRF 294
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
113-351 |
7.82e-12 |
|
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: 70.03 E-value: 7.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 113 ADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGtpGPIETVQEALDFVNEYGYPVIIKAAFGGGGRGMRVV 192
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 193 REGDDVADAFQRATSEArtafGNGTCFVERFLDKPKHIEVQLLADnHGNVV--HLFErdcsvqrrHqkvVEVA------- 263
Cdd:TIGR01369 724 YNEEELRRYLEEAVAVS----PEHPVLIDKYLEDAVEVDVDAVSD-GEEVLipGIME--------H---IEEAgvhsgds 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 264 ----PAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNqNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAG 339
Cdd:TIGR01369 788 tcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLG 866
|
250
....*....|..
gi 1034701506 340 ATLTQLGLLQDK 351
Cdd:TIGR01369 867 KKLEELGVGKEK 878
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
63-313 |
2.13e-11 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 66.45 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 63 ADEAYVI---GEEGqytpvgaYLamDEIIEIAKKHKVDFIHPGY----GFLSENsefADKVVKAGITWIGPPAEVIDSVG 135
Cdd:PRK12767 43 ADKFYVVpkvTDPN-------YI--DRLLDICKKEKIDLLIPLIdpelPLLAQN---RDRFEEIGVKVLVSSKEVIEICN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 136 DKVSARHLAARANVPTVPG-TPGPIETVQEAlDFVNEYGYPVIIKAAFGGGGRGMRVVREGDDVADAFQRatseartafg 214
Cdd:PRK12767 111 DKWLTYEFLKENGIPTPKSyLPESLEDFKAA-LAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEY---------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 215 NGTCFVERFLDKPKhIEVQLLADNHGNVVHlferdcSVQRRHQKVV--EVAPAKTlpreVRDAILTDAV-KLAKVCGYRN 291
Cdd:PRK12767 180 VPNLIIQEFIEGQE-YTVDVLCDLNGEVIS------IVPRKRIEVRagETSKGVT----VKDPELFKLAeRLAEALGARG 248
|
250 260
....*....|....*....|..
gi 1034701506 292 AGTAEFLVDNqNRHYFIEINPR 313
Cdd:PRK12767 249 PLNIQCFVTD-GEPYLFEINPR 269
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
82-347 |
3.20e-11 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 68.07 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 82 LAMDEIIEIAKKHKVDFIHPGYGFLSENSeFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGtpGPIET 161
Cdd:PRK12815 617 LTLEDVLNVAEAENIKGVIVQFGGQTAIN-LAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATD 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 162 VQEALDFVNEYGYPVIIKAAFGGGGRGMRVVREGDDVADAFQRATSEARTAfgngtcFVERFLDKpKHIEVQLLADnhGN 241
Cdd:PRK12815 694 EEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENASQLYPI------LIDQFIDG-KEYEVDAISD--GE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 242 VVHL---FErdcsvqrrHqkvVE-----------VAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNqNRHYF 307
Cdd:PRK12815 765 DVTIpgiIE--------H---IEqagvhsgdsiaVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAN-DEIYV 832
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034701506 308 IEINPRiqVEHT--ITEEITGIDIVSAQIQIAAGATLTQLGL 347
Cdd:PRK12815 833 LEVNPR--ASRTvpFVSKATGVPLAKLATKVLLGKSLAELGY 872
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1102-1170 |
3.98e-11 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 59.80 E-value: 3.98e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034701506 1102 HQIGAPMAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVLE 1170
Cdd:PRK08225 2 TKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
44-332 |
8.76e-10 |
|
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: 61.11 E-value: 8.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 44 MRTIAIYSHEDRLSMHRLKADEA-------YVIGEEGQYTPVGAYLAMDEIIEIAKkhkVDFI-----HPGYGFlsensE 111
Cdd:COG0189 1 MMKIAILTDPPDKDSTKALIEAAqrrghevEVIDPDDLTLDLGRAPELYRGEDLSE---FDAVlpridPPFYGL-----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 112 FADKVVKAGITWIGPPAEVIDSvGDKVSARHLAARANVPTvpgtpgP----IETVQEALDFVNEYGYPVIIKAAFggggr 187
Cdd:COG0189 73 LLRQLEAAGVPVVNDPEAIRRA-RDKLFTLQLLARAGIPV------PptlvTRDPDDLRAFLEELGGPVVLKPLD----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 188 gmrvVREGDDVA-----DAFqRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNhGNVVHLFERDcsVQRRHQKVVEV 262
Cdd:COG0189 141 ----GSGGRGVFlvedeDAL-ESILEALTELGSEPVLVQEFIPEEDGRDIRVLVVG-GEPVAAIRRI--PAEGEFRTNLA 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 263 APAKTLPREVRDAILTDAVKLAKVCGYRNAGTaEFLVDNqNRHYFIEINPRIQVEHtiTEEITGIDIVSA 332
Cdd:COG0189 213 RGGRAEPVELTDEERELALRAAPALGLDFAGV-DLIEDD-DGPLVLEVNVTPGFRG--LERATGVDIAEA 278
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
63-353 |
4.46e-09 |
|
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: 60.78 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 63 ADEAYvigeegqYTPVGAYlAMDEIIEiakKHKVDFIHPGYG---FLSENSEFADKVV--KAGITWIGPPAEVIDSVGDK 137
Cdd:TIGR01369 60 ADKVY-------IEPLTPE-AVEKIIE---KERPDAILPTFGgqtALNLAVELEESGVleKYGVEVLGTPVEAIKKAEDR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 138 VSARHLAARANVPTVPGtpGPIETVQEALDFVNEYGYPVIIKAAFGGGGRgmrvvreGDDVA---DAFQRATSEARTAFG 214
Cdd:TIGR01369 129 ELFREAMKEIGEPVPES--EIAHSVEEALAAAKEIGYPVIVRPAFTLGGT-------GGGIAynrEELKEIAERALSASP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 215 NGTCFVERFLDKPKHIEVQLLADNHGNVVHLferdCSVQR-----RH--QKVVeVAPAKTLPRE----VRDAiltdAVKL 283
Cdd:TIGR01369 200 INQVLVEKSLAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHtgDSIV-VAPSQTLTDKeyqmLRDA----SIKI 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034701506 284 AKVCGYRNAGTAEFLVDNQN-RHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAGATLTQlglLQDKIT 353
Cdd:TIGR01369 271 IRELGIEGGCNVQFALNPDSgRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAVGYTLDE---LKNPVT 338
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
714-827 |
5.68e-09 |
|
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate synthase (IPMS) catalyzes an aldol-type condensation of acetyl-CoA and 2-oxoisovalerate yielding 2-isopropylmalate and CoA, the first committed step in leucine biosynthesis. This family includes the Arabidopsis thaliana IPMS1 and IPMS2 proteins, the Glycine max GmN56 protein, and the Brassica insularis BatIMS protein. This family also includes a group of archeal IPMS-like proteins represented by the Methanocaldococcus jannaschii AksA protein. AksA catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form trans-homoaconitate, one of 13 steps in the conversion of alpha-ketoglutarate and acetylCoA to alpha-ketosuberate, a precursor to coenzyme B and biotin. AksA also catalyzes the condensation of alpha-ketoadipate or alpha-ketopimelate with acetylCoA to form, respectively, the (R)-homocitrate homologs (R)-2-hydroxy-1,2,5-pentanetricarboxylic acid and (R)-2-hydroxy-1,2,6- hexanetricarboxylic acid. 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: 163678 Cd Length: 268 Bit Score: 58.61 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 714 LDYYLEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYP--DLPIHVHSHDSAGTAVASMTACALAGADVVDVA 791
Cdd:cd07940 142 LDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVPniKVPISVHCHNDLGLAVANSLAAVEAGARQVECT 221
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034701506 792 INSM---SGltsqpsiNallASLE------------GNIDTGINVEHVREL 827
Cdd:cd07940 222 INGIgerAG-------N---AALEevvmalktrydyYGVETGIDTEELYET 262
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
664-827 |
4.26e-08 |
|
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; Isopropylmalate/homocitrate/citramalate synthases is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439889 [Multi-domain] Cd Length: 452 Bit Score: 57.10 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 664 NGVDIFRVFDALN-DLEQ-LKVGVNAVK--KAGGvveATVCYSG-DmlqpGKKYNLDYYLEVVEKIVQMGTHILGIKDMA 738
Cdd:COG0119 99 IKTSDLHVEYKLRkTREEvLEMAVEAVKyaKEHG---LEVEFSAeD----ATRTDPDFLLEVLEAAIEAGADRINLPDTV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 739 GTMKPAAAKLLIGSLRTRYPDLPIHVHSHDSAGTAVA-SMTAcALAGADVVDVAINsmsGL---TSQPSINALLASLE-- 812
Cdd:COG0119 172 GGATPNEVADLIEELRERVPDVILSVHCHNDLGLAVAnSLAA-VEAGADQVEGTIN---GIgerAGNAALEEVVMNLKlk 247
|
170
....*....|....*
gi 1034701506 813 GNIDTGINVEHVREL 827
Cdd:COG0119 248 YGVDTGIDLSKLTEL 262
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
628-822 |
4.63e-08 |
|
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: 55.86 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 628 LVPNipfqmlLRGAngvaysslpDNAIDHfvkqakdnGVDIFRVF----DALN----------DLEQLKVGVNAVKKAGG 693
Cdd:cd07938 72 LVPN------LRGA---------ERALAA--------GVDEVAVFvsasETFSqknincsiaeSLERFEPVAELAKAAGL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 694 VVEATV-----C-YSGDMlqpgkkyNLDYYLEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYPDLPIHVHSH 767
Cdd:cd07938 129 RVRGYVstafgCpYEGEV-------PPERVAEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERFPDEKLALHFH 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034701506 768 DSAGTAVASMTACALAGADVVDVainSMSGLTSQP-----SIN----ALLASLEG-NIDTGINVE 822
Cdd:cd07938 202 DTRGQALANILAALEAGVRRFDS---SVGGLGGCPfapgaTGNvateDLVYMLEGmGIETGIDLD 263
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1082-1167 |
6.26e-08 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 52.51 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1082 ADKSQNIQSVAKPKADVhdthqIGAPMAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVD 1161
Cdd:PRK06549 47 QVEAQAPQPAAAAGADA-----MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVN 121
|
....*.
gi 1034701506 1162 ASDLLV 1167
Cdd:PRK06549 122 PGDGLI 127
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
713-833 |
1.23e-07 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 55.18 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 713 NLDYYLEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYpDLPIHVHSHDSAGTAVASMTACALAGADVVDVAI 792
Cdd:PRK11858 143 DLDFLIEFAKAAEEAGADRVRFCDTVGILDPFTMYELVKELVEAV-DIPIEVHCHNDFGMATANALAGIEAGAKQVHTTV 221
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1034701506 793 NsmsGLTSQPSINAL---LASL--EGNIDTGINVEHVRELDAYWAE 833
Cdd:PRK11858 222 N---GLGERAGNAALeevVMALkyLYGIDLGIDTERLYELSRLVSK 264
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1103-1169 |
1.70e-07 |
|
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: 49.36 E-value: 1.70e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034701506 1103 QIGAPM------AGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVL 1169
Cdd:cd06663 1 TILIPDlaqhlgDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| DRE_TIM_CMS |
cd07945 |
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ... |
709-824 |
7.11e-07 |
|
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic TIM barrel domain; Citramalate synthase (CMS) catalyzes the conversion of pyruvate and acetyl-CoA to (R)-citramalate in the first dedicated step of the citramalate pathway. Citramalate is only found in Leptospira interrogans and a few other microorganisms. 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: 163683 [Multi-domain] Cd Length: 280 Bit Score: 52.38 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 709 GKKYNLDYYLEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYPDLPIHVHSHDSAGTAVASMTACALAGADVV 788
Cdd:cd07945 141 GMRDSPDYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFHAHNDYDLAVANVLAAVKAGIKGL 220
|
90 100 110
....*....|....*....|....*....|....*...
gi 1034701506 789 DVAINSMSGLTSQPSINALLASLEG--NIDTGINVEHV 824
Cdd:cd07945 221 HTTVNGLGERAGNAPLASVIAVLKDklKVKTNIDEKRL 258
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1103-1169 |
1.34e-06 |
|
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: 46.98 E-value: 1.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034701506 1103 QIGAPMA-GVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVL 1169
Cdd:COG0508 9 DLGESMTeGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
136-312 |
2.26e-06 |
|
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: 50.88 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 136 DKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIKAAFggggrgmrvvrEG-----------DDVADAFQR 204
Cdd:COG1181 95 DKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAR-----------EGssvgvskvknaEELAAALEE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 205 ATSEARTAfgngtcFVERFLDkPKHIEVQLLADNHGNVVHLFERDcsVQRR----HQK-----VVEVAPAKtLPREVRDA 275
Cdd:COG1181 164 AFKYDDKV------LVEEFID-GREVTVGVLGNGGPRALPPIEIV--PENGfydyEAKytdggTEYICPAR-LPEELEER 233
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034701506 276 ILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINP 312
Cdd:COG1181 234 IQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
85-180 |
3.38e-06 |
|
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: 50.78 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 85 DEIIEIAKKHKVDFIHPGygflsenSE------FADKVVKAGITWIGPPA-----EvidsvGDKVSARHLAARANVPTVP 153
Cdd:COG0151 52 EALVAFAKEENIDLVVVG-------PEaplvagIVDAFRAAGIPVFGPSKaaaqlE-----GSKAFAKEFMARYGIPTAA 119
|
90 100
....*....|....*....|....*..
gi 1034701506 154 GtpGPIETVQEALDFVNEYGYPVIIKA 180
Cdd:COG0151 120 Y--RVFTDLEEALAYLEEQGAPIVVKA 144
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
86-182 |
4.16e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 51.25 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 86 EIIE-IAKKHKVDFIHPGYG---FLSENSEFADKVV--KAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGtpGPI 159
Cdd:PRK05294 72 EFVEkIIEKERPDAILPTMGgqtALNLAVELAESGVleKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIA 149
|
90 100
....*....|....*....|...
gi 1034701506 160 ETVQEALDFVNEYGYPVIIKAAF 182
Cdd:PRK05294 150 HSMEEALEVAEEIGYPVIIRPSF 172
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1106-1169 |
5.75e-06 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 45.18 E-value: 5.75e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034701506 1106 APMAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVL 1169
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
118-345 |
6.10e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 50.74 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 118 KAGITWIGPPAEVIDSVGDKVSARHLAARANVPtVPGTpGPIETVQEALDFVNEYGYPVIIKAAFGGGGRGMRVVREGDD 197
Cdd:PRK12815 110 QYGVELLGTNIEAIQKGEDRERFRALMKELGEP-VPES-EIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 198 VADAFQRATSEARTAfgngTCFVERFLDKPKHIEVQLLADNHGNVVHLferdCSVQRrhqkvVE-----------VAPAK 266
Cdd:PRK12815 188 LEQLFKQGLQASPIH----QCLLEESIAGWKEIEYEVMRDRNGNCITV----CNMEN-----IDpvgihtgdsivVAPSQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 267 TLP----REVRDAiltdAVKLAKVCGYRNAGTAEFLVD-NQNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAGAT 341
Cdd:PRK12815 255 TLTddeyQMLRSA----SLKIISALGVVGGCNIQFALDpKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAVGYT 330
|
....
gi 1034701506 342 LTQL 345
Cdd:PRK12815 331 LNEL 334
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1104-1177 |
3.09e-05 |
|
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: 47.95 E-value: 3.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034701506 1104 IGAPMAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVLE-EETLPPS 1177
Cdd:TIGR01348 124 IGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSvAGSTPAT 198
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
126-313 |
4.05e-05 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 47.38 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 126 PPAEVIDSVGDKVSARHLAARANVPTVPGTPgpIETVQEALDFVNEYGYPVIIKAAFggggrgmrvvrEG---------- 195
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAPFAA--VDSLEDLEAAIAELGLPAVLKTRR-----------GGydgkgqvvik 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 196 --DDVADAFQratseartAFGNGTCFVERFLD--KpkhiEVQLLA--DNHGNVVH--LFErdcSVQRRHQKVVEVAPAKt 267
Cdd:COG0026 146 saADLEAAWA--------ALGGGPCILEEFVPfeR----ELSVIVarSPDGEVATypVVE---NVHRNGILDESIAPAR- 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034701506 268 LPREVRDAILTDAVKLAKVCGYRnaGT--AEFLVDNQNRHYFIEINPR 313
Cdd:COG0026 210 ISEALAAEAEEIAKRIAEALDYV--GVlaVEFFVTKDGELLVNEIAPR 255
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
125-352 |
6.69e-05 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 47.47 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 125 GPPAEVIDSVGDKVSARHLAARANVPTVPGtpGPIETVQEALDFVNEYGYPVIIKAAFGGGGRGMRVVREGDDVadafQR 204
Cdd:PLN02735 691 GTSPDSIDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKL----KT 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 205 ATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVV-------------HLFERDCSVqrrhqkvvevaPAKTLPRE 271
Cdd:PLN02735 765 YLETAVEVDPERPVLVDKYLSDATEIDVDALADSEGNVViggimehieqagvHSGDSACSL-----------PTQTIPSS 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 272 VRDAILTDAVKLAK---VCGYRNagtAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAGATLTQLGLL 348
Cdd:PLN02735 834 CLATIRDWTTKLAKrlnVCGLMN---CQYAITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSGKSLKDLGFT 910
|
....
gi 1034701506 349 QDKI 352
Cdd:PLN02735 911 EEVI 914
|
|
| PRK00915 |
PRK00915 |
2-isopropylmalate synthase; Validated |
714-793 |
1.39e-04 |
|
2-isopropylmalate synthase; Validated
Pssm-ID: 234864 [Multi-domain] Cd Length: 513 Bit Score: 45.87 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 714 LDYYLEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYP---DLPIHVHSHDSAGTAVASMTACALAGADVVDV 790
Cdd:PRK00915 148 LDFLCRVVEAAIDAGATTINIPDTVGYTTPEEFGELIKTLRERVPnidKAIISVHCHNDLGLAVANSLAAVEAGARQVEC 227
|
...
gi 1034701506 791 AIN 793
Cdd:PRK00915 228 TIN 230
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
63-345 |
1.56e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 45.92 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 63 ADEAYVigeeGQYTPvgaylamdEIIE-IAKKHKVDFIHPGYG---------FLSENSEFAdkvvKAGITWIGPPAEVID 132
Cdd:PLN02735 77 ADRTYI----APMTP--------ELVEqVIAKERPDALLPTMGgqtalnlavALAESGILE----KYGVELIGAKLDAIK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 133 SVGDKVSARHLAARANVPTVPGtpGPIETVQEALDFVNEYG-YPVIIKAAFGGGGRgmrvvreGDDVA---DAFQRATSE 208
Cdd:PLN02735 141 KAEDRELFKQAMEKIGLKTPPS--GIATTLDECFEIAEDIGeFPLIIRPAFTLGGT-------GGGIAynkEEFETICKA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 209 ARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLferdCSVQRRHQKVVE------VAPAKTLP----REVRDAILT 278
Cdd:PLN02735 212 GLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVII----CSIENIDPMGVHtgdsitVAPAQTLTdkeyQRLRDYSVA 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034701506 279 DAVKLAKVCGYRNAGTAEFLVDNQnrHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAGATLTQL 345
Cdd:PLN02735 288 IIREIGVECGGSNVQFAVNPVDGE--VMIIEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTLDQI 352
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
714-827 |
2.61e-04 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 44.93 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 714 LDYYLEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLrTRYPDLPIHVHSHDSAGTAVASMTACALAGADVVDVAIN 793
Cdd:PRK09389 142 LDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRL-SELVKGPVSIHCHNDFGLAVANTLAALAAGADQVHVTIN 220
|
90 100 110
....*....|....*....|....*....|....*.
gi 1034701506 794 SMSGLTSQPSINALLASLEG--NIDTGINVEHVREL 827
Cdd:PRK09389 221 GIGERAGNASLEEVVMALKHlyDVETGIKLEELYEL 256
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
728-829 |
2.69e-04 |
|
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: 44.03 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 728 GTHILGIKDMAGTMKPAAAKLLIGSLRTRYPDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSM---SGLTsqpSI 804
Cdd:cd07943 154 GADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATRIDGSLAGLgagAGNT---PL 230
|
90 100
....*....|....*....|....*.
gi 1034701506 805 NALLASLE-GNIDTGINVEHVreLDA 829
Cdd:cd07943 231 EVLVAVLErMGIETGIDLYKL--MDA 254
|
|
| PRK05692 |
PRK05692 |
hydroxymethylglutaryl-CoA lyase; Provisional |
718-835 |
3.09e-04 |
|
hydroxymethylglutaryl-CoA lyase; Provisional
Pssm-ID: 180206 Cd Length: 287 Bit Score: 44.11 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 718 LEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYPDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSG 797
Cdd:PRK05692 158 ADVAERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAEFPAERLAGHFHDTYGQALANIYASLEEGITVFDASVGGLGG 237
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1034701506 798 LTSQP------SINALLASLEG-NIDTGINVEHVRELDAYWAEMR 835
Cdd:PRK05692 238 CPYAPgasgnvATEDVLYMLHGlGIETGIDLDKLVRAGQFIQSKL 282
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1112-1176 |
4.84e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 44.04 E-value: 4.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034701506 1112 IIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVLEEETLPP 1176
Cdd:PRK11855 135 VIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAP 199
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1082-1177 |
8.17e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 43.45 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1082 ADKSQNIQSVAKPKADVHDTH--QIGAPmAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGES 1159
Cdd:PRK11854 89 EEKKEAAPAAAPAAAAAKDVHvpDIGSD-EVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDK 167
|
90
....*....|....*...
gi 1034701506 1160 VDASDLLVVLEEETLPPS 1177
Cdd:PRK11854 168 VSTGSLIMVFEVAGEAPA 185
|
|
| MfnD |
COG1821 |
Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme ... |
111-314 |
1.00e-03 |
|
Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme transport and metabolism];
Pssm-ID: 441426 [Multi-domain] Cd Length: 323 Bit Score: 42.61 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 111 EFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPietvqealDFVNEYGYPVIIKAafggggrgmr 190
Cdd:COG1821 99 RLTRIVEAAGKRNLGSSPEAIALAADKLLTAELLAAAGIPTPPTFPAD--------DAPPLLAGPWVVKP---------- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 191 vvregDDVADA-----FQRATSEARTAFGNGTCFVERFLDKpKHIEVQLLAdNHGNVVHLferdcSVQRRHqkvVEVAPA 265
Cdd:COG1821 161 -----DDGAGSegtrlFDDPAALRAREARGAGLIVQPYIEG-EAASLSLLC-GRGGALLL-----SINRQR---IEVDGG 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034701506 266 K------TLP-REVRDAILTD-AVKLAKV----CGYrnAGtaeflVD---NQNRHYFIEINPRI 314
Cdd:COG1821 226 RfsylggTVPaEHPRKEELQAlAQKVAEAlpglRGY--VG-----VDlilTADGPVVVEVNPRL 282
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
714-833 |
1.12e-03 |
|
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: 42.11 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 714 LDYYLEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRtRYPDLPIHVHSHDSAGTAVASMTACALAGADVVDVAIN 793
Cdd:cd07939 138 PDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLR-AATDLPLEFHAHNDLGLATANTLAAVRAGATHVSVTVN 216
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1034701506 794 smsGLTSQpsinALLASLE---------GNIDTGINVEHVRELDAYWAE 833
Cdd:cd07939 217 ---GLGER----AGNAALEevvmalkhlYGRDTGIDTTRLPELSQLVAR 258
|
|
| PLN03228 |
PLN03228 |
methylthioalkylmalate synthase; Provisional |
715-795 |
1.18e-03 |
|
methylthioalkylmalate synthase; Provisional
Pssm-ID: 178767 [Multi-domain] Cd Length: 503 Bit Score: 42.99 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 715 DYYLEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYP---DLPIHVHSHDSAGTAVASMTACALAGADVVDVA 791
Cdd:PLN03228 239 EFLCKILGEAIKAGATSVGIADTVGINMPHEFGELVTYVKANTPgidDIVFSVHCHNDLGLATANTIAGICAGARQVEVT 318
|
....
gi 1034701506 792 INSM 795
Cdd:PLN03228 319 INGI 322
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
118-329 |
1.79e-03 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 41.56 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 118 KAGITWIGPPaEVIDSVGDKVSARHLAARANVPTvPGTpGPIETVQEALDFVNEYGYPVIIKAAFGGGgrgmrvvreGDD 197
Cdd:TIGR00768 71 SLGVPVINSS-DAILNAGDKFLSHQLLAKAGIPL-PRT-GLAGSPEEALKLIEEIGFPVVLKPVFGSW---------GRG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 198 VADAFQR----ATSEARTAFGN--GTCFVERFLDKPKHIEVQLLADNhGNVVHLFERdcsVQRRHQKVVEVAPAKTLPRE 271
Cdd:TIGR00768 139 VSLARDRqaaeSLLEHFEQLNGpqNLFLVQEYIKKPGGRDIRVFVVG-DEVVAAIYR---ITSGHWRSNLARGGKAEPCS 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034701506 272 VRDAILTDAVKLAKVCGYRNAGTAefLVDNQNRHYFIEINPriQVEHTITEEITGIDI 329
Cdd:TIGR00768 215 LTEEIEELAIKAAKALGLDVAGVD--LLESEDGLLVNEVNA--NPEFKNSVKTTGVNI 268
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1101-1177 |
1.82e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 42.30 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1101 THQIGAPMAGV----IIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVLEEETLPP 1176
Cdd:PRK11854 2 AIEIKVPDIGAdeveVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGAA 81
|
.
gi 1034701506 1177 S 1177
Cdd:PRK11854 82 D 82
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1104-1178 |
1.86e-03 |
|
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: 42.17 E-value: 1.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034701506 1104 IGAPMAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVLEEETLPPSQ 1178
Cdd:TIGR01348 8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGAGAQAQ 82
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
267-339 |
1.95e-03 |
|
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: 41.83 E-value: 1.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034701506 267 TLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDnQNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAG 339
Cdd:COG2232 217 ALPPALAEEMRAIAEALVAALGLVGLNGVDFILD-GDGPYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRG 288
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
1118-1178 |
2.27e-03 |
|
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: 41.64 E-value: 2.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034701506 1118 HK--GSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVLEEETLPPSQ 1178
Cdd:TIGR01347 21 HKkvGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATAA 83
|
|
| PRK06524 |
PRK06524 |
biotin carboxylase-like protein; Validated |
105-326 |
2.36e-03 |
|
biotin carboxylase-like protein; Validated
Pssm-ID: 180605 [Multi-domain] Cd Length: 493 Bit Score: 42.03 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 105 FLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYpviikaafgg 184
Cdd:PRK06524 111 FVMFDEETEALARQAGLEVMHPPAELRHRLDSKIVTTRLANEAGVPSVPHVLGRVDSYDELSALAHGAGL---------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 185 ggrgmrvvreGDDVAdafqratseARTAFGN---GTCFVERFLDKPKHIEvQLLADNHGNVV-HLFERDCSVQ---RRHQ 257
Cdd:PRK06524 181 ----------GDDLV---------VQTPYGDsgsTTFFVRGQRDWDKYAG-GIVGQPEIKVMkRIRNVEVCIEacvTRHG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 258 KVV-----------EVAPAK-----------TLPREVRDAILTDAVKLAKVC---GYRNAGTAEFLVD-NQNRHYFIEIN 311
Cdd:PRK06524 241 TVIgpamtslvgypELTPYRggwcgndiwpgALPPAQTRKAREMVRKLGDVLsreGYRGYFEVDLLHDlDADELYLGEVN 320
|
250
....*....|....*
gi 1034701506 312 PRIQVEHTITEEITG 326
Cdd:PRK06524 321 PRLSGASPMTNLTTE 335
|
|
| DRE_TIM_HCS |
cd07948 |
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ... |
718-833 |
2.84e-03 |
|
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: 40.78 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 718 LEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYpDLPIHVHSHDSAGTAVASMTACALAGADVVDVA---INS 794
Cdd:cd07948 144 LRVYRAVDKLGVNRVGIADTVGIATPRQVYELVRTLRGVV-SCDIEFHGHNDTGCAIANAYAALEAGATHIDTTvlgIGE 222
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1034701506 795 MSGLTSQPSINALLASLE-GNIDTGINVEHVRELDAYWAE 833
Cdd:cd07948 223 RNGITPLGGLIARMYTADpEYVVSKYKLELLPELERLVAD 262
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
126-313 |
2.87e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 41.29 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 126 PPAEVIDSVGDKVSARHLAARANVPTVPGTPgpIETVQEALDFVNEYGYPVIIKAAFggggrgmrvvrEG---------D 196
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPVAPFAV--VDSAEDLEAALADLGLPAVLKTRR-----------GGydgkgqwviR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 197 DVADAfqratSEARTAFGNGTCFVERF--LDKpkhiEVQLLA--DNHGNVVH--LFErdcSVQRRHQKVVEVAPAKtLPR 270
Cdd:PRK06019 157 SAEDL-----EAAWALLGSVPCILEEFvpFER----EVSVIVarGRDGEVVFypLVE---NVHRNGILRTSIAPAR-ISA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034701506 271 EVRDAILTDAVKLAKVCGYRnaGTA--EFLVDNQNRHYFIEINPR 313
Cdd:PRK06019 224 ELQAQAEEIASRIAEELDYV--GVLavEFFVTGDGELLVNEIAPR 266
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1104-1172 |
3.49e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 41.35 E-value: 3.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034701506 1104 IGAPMAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVLEEE 1172
Cdd:PRK11855 10 IGEVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAA 78
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
113-352 |
3.52e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 41.62 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 113 ADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGtpGPIETVQEALDFVNEYGYPVIIKAAFggggrgmrvv 192
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVRPSY---------- 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 193 regddV-----------ADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADnHGNVV------HLfER------D 249
Cdd:PRK05294 714 -----VlggrameivydEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD-GEDVLiggimeHI-EEagvhsgD 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 250 --CSVqrrhqkvvevaPAKTLPREVRDAILTDAVKLAK---VCGYRNagtAEFLVDNqNRHYFIEINPRiqVEHTI--TE 322
Cdd:PRK05294 787 saCSL-----------PPQTLSEEIIEEIREYTKKLALelnVVGLMN---VQFAVKD-DEVYVIEVNPR--ASRTVpfVS 849
|
250 260 270
....*....|....*....|....*....|
gi 1034701506 323 EITGIDIVSAQIQIAAGATLTQLGLLQDKI 352
Cdd:PRK05294 850 KATGVPLAKIAARVMLGKKLAELGYTKGLI 879
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1110-1179 |
5.61e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 40.76 E-value: 5.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034701506 1110 GVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIRDGESVDASDLLVVLEEETLPPSQK 1179
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPAAA 288
|
|
| |
