|
Name |
Accession |
Description |
Interval |
E-value |
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
21-1169 |
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: 2094.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 21 KILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEVGQYTPVGAYLAIDEIISIAQKHQVDFIHP 100
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 101 GYGFLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVIIKAA 180
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 181 FGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVVE 260
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 261 VAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVAAQIQIAAGAS 340
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 341 LP--QLGLF-QDKITTRGFAIQCRITTEDPAKNFQPDTGRIEVYRSAGGNGVRLDGGNAYAGTIISPHYDSMLVKCSCSG 417
Cdd:TIGR01235 321 LPtpQLGVPnQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 418 STYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTHPVFIEGTYWTTFIDDTPQLFQMVSSQNRAQKLLHYLADVAVNGsS 497
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNG-H 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 498 IKGQIGLPKLKSNPSVPHLHDAQGNVinvtksapPSGWRQVLLEKGPAEFARQVRQFNGTLLMDTTWRDAHQSLLATRVR 577
Cdd:TIGR01235 480 PEAKDKLKPLENAPRVVVLYADQNPV--------PRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVR 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 578 THDLATIAPTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLRGANGVAYSSLPDNAIDHFV 657
Cdd:TIGR01235 552 THDLAKIAPTTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFV 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 658 KQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGGVVEATVCFSGDMLQPGK-KYNLDYYLEIAEKIVQMGTHILGIKDM 736
Cdd:TIGR01235 632 KQAAQGGIDIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARpKYDLKYYTNLAVELEKAGAHILGIKDM 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 737 AGTMKPAAAKLLIGSLRAKYpDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMSGLTSQPSINALLASLEGN-ID 815
Cdd:TIGR01235 712 AGLLKPAAAKLLIKALREKT-DLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSeRD 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 816 TGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLGLGEQWAETKRAYREANYLLGDIV 895
Cdd:TIGR01235 791 PGLNVAWIRELSAYWEAVRNLYAAFESDLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIV 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 896 KVTPTSKVVGDLAQFMVSNKLTSDDVRRLANSLDFPDSVMDFFEGLIGQPYGGFPEPFRSDVLRNkRRKLTCRPGLELEP 975
Cdd:TIGR01235 871 KVTPSSKVVGDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKG-EKPITVRPGSLLEP 949
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 976 FDLEKIREDLQNRF-GDVDECDVASYNMYPRVYEDFQKMRETYGDLSVLPTRSFLSPLETDEEIEVVIEQGKTLIIKLQA 1054
Cdd:TIGR01235 950 ADLDAIRKDLQEKHeREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQA 1029
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 1055 VGDlNKKTGEREVYFDLNGEMRKIRVADRSQKVETVTKSKADMHDPLHIGAPMAGVIVEVKVHKGSLIKKGQPVAVLSAM 1134
Cdd:TIGR01235 1030 VGA-TDSQGEREVFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAM 1108
|
1130 1140 1150
....*....|....*....|....*....|....*
gi 1028056092 1135 KMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLLE 1169
Cdd:TIGR01235 1109 KMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
20-1168 |
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: 1859.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 20 NKILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEVGQytPVGAYLAIDEIISIAQKHQVDFIH 99
Cdd:COG1038 5 KKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKG--PVDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 100 PGYGFLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVIIKA 179
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 180 AFggggrgmrvvreG------------DDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFER 247
Cdd:COG1038 163 AA------------GgggrgmrvvrseEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFER 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 248 DCSVQRRHQKVVEVAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGID 327
Cdd:COG1038 231 DCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGID 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 328 IVAAQIQIAAGASL--PQLGLF-QDKITTRGFAIQCRITTEDPAKNFQPDTGRIEVYRSAGGNGVRLDGGNAYAGTIISP 404
Cdd:COG1038 311 IVQSQILIAEGYSLddPEIGIPsQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 405 HYDSMLVKCSCSGSTYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTHPVFIEGTYWTTFIDDTPQLFQMVSSQNRAQKL 484
Cdd:COG1038 391 YYDSLLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 485 LHYLADVAVNGSSIKGQIGLPKLKSnPSVPHLHdaqgnvinvTKSAPPSGWRQVLLEKGPAEFARQVRQFNGTLLMDTTW 564
Cdd:COG1038 471 LTYLGDVTVNGPPGVKGRPKPDFPK-PKLPKVD---------LGAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTF 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 565 RDAHQSLLATRVRTHDLATIAPTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLRGANGVA 644
Cdd:COG1038 541 RDAHQSLLATRVRTRDMLKIAPATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVG 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 645 YSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGGVVEATVCFSGDMLQPGK-KYNLDYYLEIAEKI 723
Cdd:COG1038 621 YTNYPDNVVRAFVKEAAEAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRtKYTLDYYVDLAKEL 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 724 VQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYpDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMSGLTSQPSI 803
Cdd:COG1038 701 EKAGAHILAIKDMAGLLKPYAAYKLVKALKEEV-DLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSL 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 804 NALLASLEGNI-DTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLGLGEQWAETKR 882
Cdd:COG1038 780 NSLVAALEGTErDTGLDLDALQELSNYWEAVRKYYAPFESGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKE 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 883 AYREANYLLGDIVKVTPTSKVVGDLAQFMVSNKLTSDDVRRLANSLDFPDSVMDFFEGLIGQPYGGFPEPFRSDVLRNkR 962
Cdd:COG1038 860 MYAAVNRLFGDIVKVTPSSKVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKG-R 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 963 RKLTCRPGLELEPFDLEKIREDLQNRFG-DVDECDVASYNMYPRVYEDFQKMRETYGDLSVLPTRSFLSPLETDEEIEVV 1041
Cdd:COG1038 939 KPITVRPGELLPPVDFDALRAELEEKLGrEPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVE 1018
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 1042 IEQGKTLIIKLQAVGDLNKKtGEREVYFDLNGEMRKIRVADRSQKVETVTKSKADMHDPLHIGAPMAGVIVEVKVHKGSL 1121
Cdd:COG1038 1019 IEEGKTLIIKLLAIGEPDED-GMRTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDE 1097
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*..
gi 1028056092 1122 IKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLL 1168
Cdd:COG1038 1098 VKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
20-1170 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 1741.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 20 NKILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEVGQytPVGAYLAIDEIISIAQKHQVDFIH 99
Cdd:PRK12999 6 KKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKH--PVRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 100 PGYGFLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVIIKA 179
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 180 AFggggrgmrvvreG------------DDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFER 247
Cdd:PRK12999 164 SA------------GgggrgmrivrseEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYER 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 248 DCSVQRRHQKVVEVAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGID 327
Cdd:PRK12999 232 DCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGID 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 328 IVAAQIQIAAGASLPQLGLF---QDKITTRGFAIQCRITTEDPAKNFQPDTGRIEVYRSAGGNGVRLDGGNAYAGTIISP 404
Cdd:PRK12999 312 IVQSQILIAEGATLHDLEIGipsQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 405 HYDSMLVKCSCSGSTYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTHPVFIEGTYWTTFIDDTPQLFQMVSSQNRAQKL 484
Cdd:PRK12999 392 YYDSLLVKLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 485 LHYLADVAVNGSsiKGQIGLPKLKSNPSVPHLHdaqgnvinvTKSAPPSGWRQVLLEKGPAEFARQVRQFNGTLLMDTTW 564
Cdd:PRK12999 472 LTYIADVTVNGF--PGVKKKPPVFPDPRLPKVD---------LSAPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTF 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 565 RDAHQSLLATRVRTHDLATIAPTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLRGANGVA 644
Cdd:PRK12999 541 RDAHQSLLATRVRTKDLLRIAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVG 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 645 YSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGGVVEATVCFSGDMLQPG-KKYNLDYYLEIAEKI 723
Cdd:PRK12999 621 YTNYPDNVVRAFVREAAAAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPArAKYDLDYYVDLAKEL 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 724 VQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYpDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMSGLTSQPSI 803
Cdd:PRK12999 701 EKAGAHILAIKDMAGLLKPAAAYELVSALKEEV-DLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSL 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 804 NALLASLEGN-IDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLGLGEQWAETKR 882
Cdd:PRK12999 780 NSIVAALEGTeRDTGLDLDAIRKLSPYWEAVRPYYAPFESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKE 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 883 AYREANYLLGDIVKVTPTSKVVGDLAQFMVSNKLTSDDVRRLANSLDFPDSVMDFFEGLIGQPYGGFPEPFRSDVLRNKR 962
Cdd:PRK12999 860 MYAAVNRMFGDIVKVTPSSKVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEE 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 963 RkLTCRPGLELEPFDLEKIREDLQNRFG-DVDECDVASYNMYPRVYEDFQKMRETYGDLSVLPTRSFLSPLETDEEIEVV 1041
Cdd:PRK12999 940 P-ITVRPGELLEPVDFEAERAELEEKLGrEVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVE 1018
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 1042 IEQGKTLIIKLQAVGDLNKKtGEREVYFDLNGEMRKIRVADRSQKVETVTKSKADMHDPLHIGAPMAGVIVEVKVHKGSL 1121
Cdd:PRK12999 1019 IEPGKTLIIKLEAIGEPDED-GMRTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDE 1097
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*....
gi 1028056092 1122 IKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLLED 1170
Cdd:PRK12999 1098 VKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
20-467 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 642.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 20 NKILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEVgqyTPVGAYLAIDEIISIAQKHQVDFIH 99
Cdd:COG4770 3 KKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPA---PAAESYLNIDAIIAAAKATGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 100 PGYGFLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVIIKA 179
Cdd:COG4770 80 PGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 180 AFggggrgmrvvreG------------DDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFER 247
Cdd:COG4770 160 SA------------GgggkgmrvvrseEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGER 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 248 DCSVQRRHQKVVEVAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGID 327
Cdd:COG4770 228 DCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGID 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 328 IVAAqiqiaagaslpQ--------LGLFQDKITTRGFAIQCRITTEDPAKNFQPDTGRIEVYRSAGGNGVRLDGGnAYAG 399
Cdd:COG4770 308 LVEE-----------QiriaagepLPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEG 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028056092 400 TIISPHYDSMLVKCSCSGSTYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTHPVFIEGTYWTTFIDD 467
Cdd:COG4770 376 YEIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIER 443
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
20-466 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 540.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 20 NKILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEVgqyTPVGAYLAIDEIISIAQKHQVDFIH 99
Cdd:PRK08591 3 DKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPA---PSKKSYLNIPAIISAAEITGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 100 PGYGFLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVIIKA 179
Cdd:PRK08591 80 PGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 180 AFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVV 259
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 260 EVAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVAAQIQIAAGA 339
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 340 SLPqlgLFQDKITTRGFAIQCRITTEDPAKNFQPDTGRIEVYRSAGGNGVRLDGGnAYAGTIISPHYDSMLVKCSCSGST 419
Cdd:PRK08591 320 PLS---IKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMIGKLIVHGET 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1028056092 420 YEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTHPVFIEGTYWTTFID 466
Cdd:PRK08591 396 REEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLE 442
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
20-484 |
4.18e-176 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 527.24 E-value: 4.18e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 20 NKILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEVgqyTPVGAYLAIDEIISIAQKHQVDFIH 99
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPA---PPSKSYLNIERIIDVAKKAGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 100 PGYGFLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVIIKA 179
Cdd:PRK08654 80 PGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 180 AFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVV 259
Cdd:PRK08654 160 SAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 260 EVAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNrHYFIEINPRIQVEHTITEEITGIDIVAAQIQIAAGA 339
Cdd:PRK08654 240 EEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGN-FYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 340 SLPqlgLFQDKITTRGFAIQCRITTEDPAKNFQPDTGRIEVYRSAGGNGVRLDGGnAYAGTIISPHYDSMLVKCSCSGST 419
Cdd:PRK08654 319 ELS---FKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSG-VHMGYEIPPYYDSMISKLIVWGRT 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 420 YEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTHPVFIEGTYWTTFIDDTPQLFQ-----MVSSQNRAQKL 484
Cdd:PRK08654 395 REEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTILEemkryALEEEEREKTL 464
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
20-467 |
2.79e-168 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 504.95 E-value: 2.79e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 20 NKILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEvgqyTPVG-AYLAIDEIISIAQKHQVDFI 98
Cdd:PRK06111 3 QKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGG----PRVQeSYLNLEKIIEIAKKTGAEAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 99 HPGYGFLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVIIK 178
Cdd:PRK06111 79 HPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 179 AAFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKV 258
Cdd:PRK06111 159 ASAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 259 VEVAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVAAQIQIAAG 338
Cdd:PRK06111 239 IEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 339 ASLPqlgLFQDKITTRGFAIQCRITTEDPaKNFQPDTGRIEVYRSAGGNGVRLDgGNAYAGTIISPHYDSMLVKCSCSGS 418
Cdd:PRK06111 319 EKLS---FTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHD-HAVENGVTVTPFYDPMIAKLIAHGE 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1028056092 419 TYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTHPVFIEGTYWTTFIDD 467
Cdd:PRK06111 394 TREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTK 442
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
21-494 |
1.39e-163 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 493.85 E-value: 1.39e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 21 KILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEvgqyTPVGAYLAIDEIISIAQKHQVDFIHP 100
Cdd:PRK07178 4 KILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGA----DPLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 101 GYGFLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVIIKAA 180
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 181 FGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVVE 260
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 261 VAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVAAQIQIAAGAS 340
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 341 LPQLglfQDKITTRGFAIQCRITTEDPAKNFQPDTGRIEVYRSAGGNGVRLDGGnAYAGTIISPHYDSMLVKCSCSGSTY 420
Cdd:PRK07178 320 LSYK---QEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTA-IYTGYTIPPYYDSMCAKLIVWALTW 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028056092 421 EIVRRKMIRALIEFRIRGVKTNIPFLLTLLTHPVFIEGTYWTTFIDDTPQLFQMVSSQNRAQKLLHYLADVAVN 494
Cdd:PRK07178 396 EEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNYSIKRKPEELAAAIAAAIAAH 469
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
21-466 |
3.15e-157 |
|
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: 476.18 E-value: 3.15e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 21 KILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEVGQytpVGAYLAIDEIISIAQKHQVDFIHP 100
Cdd:TIGR00514 4 KILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPS---AKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 101 GYGFLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVIIKAA 180
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 181 FGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVVE 260
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 261 VAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVAAQIQIAAGAS 340
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 341 LPqlgLFQDKITTRGFAIQCRITTEDPAKNFQPDTGRIEVYRSAGGNGVRLDgGNAYAGTIISPHYDSMLVKCSCSGSTY 420
Cdd:TIGR00514 321 LS---LKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWD-SHVYSGYTVPPYYDSMIGKLITYGKTR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1028056092 421 EIVRRKMIRALIEFRIRGVKTNIPFLLTLLTHPVFIEGTYWTTFID 466
Cdd:TIGR00514 397 EVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLE 442
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
559-840 |
1.88e-156 |
|
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: 467.29 E-value: 1.88e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 559 LMDTTWRDAHQSLLATRVRTHDLATIAPTTAHAlaGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLR 638
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEA--GFFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 639 GANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGGVVEATVCFSGDmlqpgKKYNLDYYLE 718
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS-----PVHTLEYYVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 719 IAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYPdLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMSGLT 798
Cdd:cd07937 154 LAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVG-LPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGGT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1028056092 799 SQPSINALLASLEGN-IDTGINVEHVRELDAYWAEMRLLYSCF 840
Cdd:cd07937 233 SQPSTESMVAALRGTgRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
20-467 |
3.35e-154 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 468.42 E-value: 3.35e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 20 NKILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEVgqyTPVGAYLAIDEIISIAQKHQVDFIH 99
Cdd:PRK05586 3 KKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPA---SSKDSYLNIQNIISATVLTGAQAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 100 PGYGFLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVIIKA 179
Cdd:PRK05586 80 PGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 180 AFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVV 259
Cdd:PRK05586 160 SAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 260 EVAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVaaqIQIAAGA 339
Cdd:PRK05586 240 EEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLV---KEQIKIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 340 SLPQLGLFQDKITTRGFAIQCRITTEDPAKNFQPDTGRIEVYRSAGGNGVRLDgGNAYAGTIISPHYDSMLVKCSCSGST 419
Cdd:PRK05586 317 YGEKLSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVD-SAVYSGYTIPPYYDSMIGKLIVYGKD 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1028056092 420 YEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTHPVFIEGTYWTTFIDD 467
Cdd:PRK05586 396 REEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
561-1169 |
2.75e-150 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 463.55 E-value: 2.75e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 561 DTTWRDAHQSLLATRVRTHDLATIAPttahAL--AGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLR 638
Cdd:PRK09282 8 DTTLRDAHQSLLATRMRTEDMLPIAE----KLdkVGFWSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPLQMLLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 639 GANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGGVVEATVCFSgdmlqPGKKYNLDYYLE 718
Cdd:PRK09282 84 GQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT-----TSPVHTIEKYVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 719 IAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYpDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMSGLT 798
Cdd:PRK09282 159 LAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEV-DLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISPLAFGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 799 SQPSINALLASLEGN-IDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLG----L 873
Cdd:PRK09282 238 SQPPTESMVAALKGTpYDTGLDLELLFEIAEYFREVRKKYKQFESEFTIVDTRVLIHQVPGGMISNLVSQLKEQNaldkL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 874 GEQWAETKRAYREanylLGDIVKVTPTSKVVGDLAqfmVSNKLTSDDVRRLansldfPDSVMDFFEGLIGQPyggfPEPF 953
Cdd:PRK09282 318 DEVLEEIPRVRED----LGYPPLVTPTSQIVGTQA---VLNVLTGERYKVI------TKEVKDYVKGLYGRP----PAPI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 954 RSDVlrnkRRK-------LTCRPGLELEPfDLEKIREDLQnRFGDVDECDVASYNMYPRVYEDFQKMRE--TYGDLSVLP 1024
Cdd:PRK09282 381 NEEL----RKKiigdeepITCRPADLLEP-ELEKARKEAE-ELGKSEKEDVLTYALFPQIAKKFLEEREagELKPEPEPK 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 1025 TRSFLSPLETDEEIEVVIEqGKTLIIKLQAVGDlnkkTGEREVYFDLNGEMRKIRVAdRSQKVETVTKSKADmhDPLHIG 1104
Cdd:PRK09282 455 EAAAAGAEGIPTEFKVEVD-GEKYEVKIEGVKA----EGKRPFYLRVDGMPEEVVVE-PLKEIVVGGRPRAS--APGAVT 526
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028056092 1105 APMAGVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLLE 1169
Cdd:PRK09282 527 SPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
21-466 |
1.08e-139 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 431.54 E-value: 1.08e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 21 KILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEvgqyTPVGAYLAIDEIISIAQKHQVDFIHP 100
Cdd:PRK08463 4 KILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGT----DPIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 101 GYGFLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGT-PGPIETVEEALDFVNEYGYPVIIKA 179
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTeKLNSESMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 180 AFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVV 259
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 260 EVAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVAAQIQIAAGA 339
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 340 SLPqlgLFQDKITTRGFAIQCRITTEDPAKNFQPDTGRIEVYRSAGGNGVRLDgGNAYAGTIISPHYDSMLVKCSCSGST 419
Cdd:PRK08463 320 ILD---LEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVD-SHIYKDYTIPPYYDSMLAKLIVKATS 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1028056092 420 YEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTHPVFIEGTYWTTFID 466
Cdd:PRK08463 396 YDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIE 442
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
20-466 |
3.01e-138 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 427.25 E-value: 3.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 20 NKILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGevgqytPVGA---YLAIDEIISIAQKHQVD 96
Cdd:PRK12833 6 RKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIG------PSHAaksYLNPAAILAAARQCGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 97 FIHPGYGFLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVI 176
Cdd:PRK12833 80 AIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 177 IKAAFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHgNVVHLFERDCSVQRRHQ 256
Cdd:PRK12833 160 IKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 257 KVVEVAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDN-QNRHYFIEINPRIQVEHTITEEITGIDIVAAQIQI 335
Cdd:PRK12833 239 KILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDaRGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 336 AAGASlpqLGLFQDKITTRGFAIQCRITTEDPAKNFQPDTGRIEVYRSAGGNGVRLDgGNAYAGTIISPHYDSMLVKCSC 415
Cdd:PRK12833 319 ADGEP---LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVD-SLLYPGYRVPPFYDSLLAKLIV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1028056092 416 SGSTYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTHPVFIEGTYWTTFID 466
Cdd:PRK12833 395 HGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
559-1130 |
2.18e-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: 419.68 E-value: 2.18e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 559 LMDTTWRDAHQSLLATRVRTHDLATIAPttahAL--AGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQML 636
Cdd:COG5016 6 ITDTTLRDGHQSLFATRMRTEDMLPIAE----KLdeAGFWSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 637 LRGANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGGVVEATVCFsgdMLQPgkKYNLDYY 716
Cdd:COG5016 82 LRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISY---TISP--VHTVEYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 717 LEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYpDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMSG 796
Cdd:COG5016 157 VELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEAL-DIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPLAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 797 LTSQPSINALLASLEG-NIDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLG--- 872
Cdd:COG5016 236 GTSQPPTESMVAALKGtGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGVDPRVLVHQVPGGMLSNLVSQLKEQGald 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 873 -LGEQWAETKRAYREanylLGDIVKVTPTSKVVGDLAqfmVSNKLTSDdvrRLANsldFPDSVMDFFEGLIGQPYGGFPE 951
Cdd:COG5016 316 rLDEVLEEIPRVRED----LGYPPLVTPTSQIVGTQA---VLNVLTGE---RYKM---ITKEVKDYVLGYYGKTPAPIDP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 952 PFRSDVLRNKRRKlTCRPGLELEPfDLEKIREdlqnRFGDVDECDVASYNMYPRVYEDFQKMRETYGDLSVLPTRsflsP 1031
Cdd:COG5016 383 EVRKKALGDEEPI-TCRPADLLEP-ELEKLRK----EGLAKSDEDVLTYALFPQVAIKFLKGRAAGEARPDAPLA----E 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 1032 LETDEEIEVVIEQGKTliiklqAVGDLNKKTGEREVYFDLNGEMRKIRVADRSQKVETVTKSKAdmhdplhIGAPMAGVI 1111
Cdd:COG5016 453 LAAVEEVVVVAEGVVV------VVVVGGGAEGVVVVVVGVPGAGAVAVVAAAAAVAAAAAAAAA-------AAAAAAGAA 519
|
570
....*....|....*....
gi 1028056092 1112 VEVKVHKGSLIKKGQPVAV 1130
Cdd:COG5016 520 VKKVVAVGGAVVVGVEVVV 538
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
561-1165 |
2.38e-133 |
|
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: 418.81 E-value: 2.38e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 561 DTTWRDAHQSLLATRVRTHDLATIAptTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLRGA 640
Cdd:TIGR01108 3 DVVLRDAHQSLFATRMRTEDMLPIA--EKLDDVGYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLRGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 641 NGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGGVVEATVCFSgdmLQPgkKYNLDYYLEIA 720
Cdd:TIGR01108 81 NLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT---TSP--VHTLETYLDLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 721 EKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYpDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMSGLTSQ 800
Cdd:TIGR01108 156 EELLEMGVDSICIKDMAGILTPKAAYELVSALKKRF-GLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGGTSH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 801 PSINALLASLEGN-IDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLG----LGE 875
Cdd:TIGR01108 235 PPTETMVAALRGTgYDTGLDIELLLEIAAYFREVRKKYSQFEGQLKGPDSRILVAQVPGGMLSNLESQLKEQNaldkLDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 876 QWAETKRAYREanylLGDIVKVTPTSKVVGDLAqfmVSNKLTSDDVRRLANsldfpdSVMDFFEGLIGQPYGGFPEPFRS 955
Cdd:TIGR01108 315 VLEEIPRVRED----LGYPPLVTPTSQIVGTQA---VLNVLTGERYKTITK------ETKGYLKGEYGRTPAPINAELQR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 956 DVLRNKRRKLTCRPGLELEPfDLEKIREDL--QNRFGDVDEcDVASYNMYPRVYEDFQKMRETygdlsvlPTRSFLSPLE 1033
Cdd:TIGR01108 382 KILGDEKPIVDCRPADLLEP-ELDKLRAEVreAGAEKNSIE-DVLTYALFPQVGLKFLENRHN-------PAAFEPKPEE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 1034 TDEEIEVVIEQGKtliiklqavgdlNKKTGEREVYF-DLNGEMRKIRVA---DRSQKVETVTKSK------ADMHDPLHI 1103
Cdd:TIGR01108 453 KVIEQEHAQVVGK------------YEETHASGSYTvEVEGKAFVVKVSpggDVSQITASAPANTsggtvaAKAGAGTPV 520
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028056092 1104 GAPMAGVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLL 1165
Cdd:TIGR01108 521 TAPIAGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREILVKVGDAVSVGQVL 582
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
18-466 |
6.01e-133 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 412.60 E-value: 6.01e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 18 EKNKILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEVGQYTpvgAYLAIDEIISIAQKHQVDF 97
Cdd:PRK08462 3 EIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSE---SYLNIPAIISAAEIFEADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 98 IHPGYGFLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVII 177
Cdd:PRK08462 80 IFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 178 KAAFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQK 257
Cdd:PRK08462 160 KAAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 258 VVEVAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVAAQIQIAA 337
Cdd:PRK08462 240 LIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 338 GASLPQlglfQDKITTRGFAIQCRITTEDPaKNFQPDTGRIEVYRSAGGNGVRLDgGNAYAGTIISPHYDSMLVKCSCSG 417
Cdd:PRK08462 320 GEELPS----QESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMD-SHAYAGYVVPPYYDSMIGKLIVWG 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1028056092 418 STYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTHPVFIEGTYWTTFID 466
Cdd:PRK08462 394 EDRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLE 442
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
559-1168 |
1.23e-113 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 366.56 E-value: 1.23e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 559 LMDTTWRDAHQSLLATRVRTHDLATIAPTTAHAlaGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLR 638
Cdd:PRK14040 7 ITDVVLRDAHQSLFATRLRLDDMLPIAAKLDKV--GYWSLESWGGATFDACIRFLGEDPWERLRELKKAMPNTPQQMLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 639 GANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGGVVEATVCFSgdmLQPgkKYNLDYYLE 718
Cdd:PRK14040 85 GQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT---TSP--VHTLQTWVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 719 IAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYpDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMSGLT 798
Cdd:PRK14040 160 LAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRV-DVPLHLHCHATTGLSTATLLKAIEAGIDGVDTAISSMSMTY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 799 SQPSINALLASLEG-NIDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLG----L 873
Cdd:PRK14040 239 GHSATETLVATLEGtERDTGLDILKLEEIAAYFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNMESQLKEQGaadkL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 874 GEQWAETKRAyREAnylLGDIVKVTPTSKVVGDLAqfmVSNKLTSDDVRRLANSLdfpdsvmdffEGLIGQPYGGFPEPF 953
Cdd:PRK14040 319 DEVLAEIPRV-RED---LGFIPLVTPTSQIVGTQA---VLNVLTGERYKTITKET----------AGVLKGEYGATPAPV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 954 RSD----VLRNKrRKLTCRPGLELEPfDLEKIREDLQN-------RFGD--VDecDVASYNMYPRVYEDFQKMRETYGDL 1020
Cdd:PRK14040 382 NAElqarVLEGA-EPITCRPADLLAP-ELDKLEAELRRqaqekgiTLAEnaID--DVLTYALFPQIGLKFLENRHNPAAF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 1021 SVLPTRSFLSP----LETDEEIEVVIEQGKTLIIKLQAVGDLNkktgerevyfdlngemrKIRVADRSQKVETVTKSKAD 1096
Cdd:PRK14040 458 EPVPQAEAAQPaakaEPAGSETYTVEVEGKAYVVKVSEGGDIS-----------------QITPAAPAAAPAAAAAAAPA 520
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028056092 1097 MHDPLHIGAPMAGVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLL 1168
Cdd:PRK14040 521 AAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
559-1015 |
7.64e-108 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 345.92 E-value: 7.64e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 559 LMDTTWRDAHQSLLATRVRTHDLATIAPTTAHAlaGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLR 638
Cdd:PRK12331 6 ITETVLRDGQQSLIATRMTTEEMLPILEKLDNA--GYHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQMLLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 639 GANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGGVVEATVCFSgdmLQPgkKYNLDYYLE 718
Cdd:PRK12331 84 GQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT---TSP--VHTIDYFVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 719 IAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYpDLPIHVHTHDSAGtaVASMT--ACALAGADVVDVAINSMSG 796
Cdd:PRK12331 159 LAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAV-TVPLEVHTHATSG--IAEMTylKAIEAGADIIDTAISPFAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 797 LTSQPSINALLASLEG-NIDTGINVEHVRELDAYWAEMRLLY---SCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLG 872
Cdd:PRK12331 236 GTSQPATESMVAALQDlGYDTGLDLEELSEIAEYFNPIRDHYreeGILNPKVKDVEPKTLIYQVPGGMLSNLLSQLKEQG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 873 LGEQWAETKRAYREANYLLGDIVKVTPTSKVVGDLAqfmVSNKLTSDDVRRLansldfPDSVMDFFEGLIGQPyggfPEP 952
Cdd:PRK12331 316 AEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQA---LMNVISGERYKMV------PNEIKDYVRGLYGRP----PAP 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028056092 953 FRSDVLRN---KRRKLTCRPGLELEPfDLEKIREDLQNrFGDVDEcDVASYNMYPRVYEDFQKMRE 1015
Cdd:PRK12331 383 IAEEIKKKiigDEEVITCRPADLIEP-QLEKLREEIAE-YAESEE-DVLSYALFPQQAKDFLGRRE 445
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
851-1051 |
2.93e-98 |
|
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: 310.54 E-value: 2.93e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 851 VYQHEIPGGQLTNLLFQAQQLGLGEQWAETKRAYREANYLLGDIVKVTPTSKVVGDLAQFMVSNKLTSDDVRRLANSLDF 930
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 931 PDSVMDFFEGLIGQPYGGFPEPFRSDVLRNKRRkLTCRPGLELEPFDLEKIREDLQNRFG-DVDECDVASYNMYPRVYED 1009
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEP-ITCRPGDLLPPVDLEKLRKELEEKAGrETTEEDVLSYALYPKVAEK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1028056092 1010 FQKMRETYGDLSVLPTRSFLSPLETDEEIEVVIEQGKTLIIK 1051
Cdd:pfam02436 160 FLKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
557-1169 |
8.15e-97 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 321.29 E-value: 8.15e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 557 TLLMDTTWRDAHQSLLATRVRTHDLATIAPTTAHAlaGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQML 636
Cdd:PRK14042 4 TFITDVTLRDAHQCLIATRMRTEDMLPICNKMDDV--GFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 637 LRGANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGGVVEATVCFSGDMLqpgkkYNLDYY 716
Cdd:PRK14042 82 LRGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYTTSPV-----HTLDNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 717 LEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRaKYPDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMSG 796
Cdd:PRK14042 157 LELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLK-QATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFSG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 797 LTSQPSINALLASL-EGNIDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLGLGE 875
Cdd:PRK14042 236 GASHPPTEALVAALtDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLYQVPGGMISNLYNQLKEQNALD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 876 QWAETKRAYREANYLLGDIVKVTPTSKVVGDLAqfmVSNKLTSDDVRRLANSLDFpdsvmdFFEGLIGQPYGGFPEPFRS 955
Cdd:PRK14042 316 KMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQA---VINVLTGERYKTITNEVKL------YCQGKYGTPPGKISSALRK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 956 DVLrNKRRKLTCRPGlELEPFDLEKiredLQNRFGDV---DEcDVASYNMYPRVYEDFQKMR-------ETYGDLSVLPT 1025
Cdd:PRK14042 387 KAI-GRTEVIEVRPG-DLLPNELDQ----LQNEISDLalsDE-DVLLYAMFPEIGRQFLEQRknnqlipEPLLTQSSAPD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 1026 RSFLSPLEtdeeievVIEQGKTLIIKLQAVGDLnkKTGEREVYFDLNGEMRKIrVADRSQKVETVTKSKADMH-DPLHIG 1104
Cdd:PRK14042 460 NSVMSEFD-------IILHGESYHVKVAGYGMI--EHGQQSCFLWVDGVPEEV-VVQHSELHDKIERSSVNNKiGPGDIT 529
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028056092 1105 APMAGVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLLE 1169
Cdd:PRK14042 530 VAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
135-329 |
3.13e-89 |
|
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: 286.12 E-value: 3.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 135 DKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYPVIIKAAFGGGGRGMRVVREGDDVADAFQRATSEARTAFGN 214
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 215 GTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVVEVAPAKTLPREVRDAILTDAVKLAKECGYRNAGTA 294
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1028056092 295 EFLVDNQN-RHYFIEINPRIQVEHTITEEITGIDIV 329
Cdd:pfam02786 161 EFALDPFSgEYYFIEMNTRLQVEHALAEKATGYDLA 196
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
558-1012 |
6.03e-89 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 295.15 E-value: 6.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 558 LLMDTTWRDAHQSLLATRVRTHDLATIapTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLL 637
Cdd:PRK14041 4 MFVDTTLRDGHQSLIATRMRTEDMLPA--LEAFDRMGFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQMLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 638 RGANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGGVVEATVCFSgdmLQPgkKYNLDYYL 717
Cdd:PRK14041 82 RGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT---VSP--VHTLEYYL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 718 EIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYpDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMSGL 797
Cdd:PRK14041 157 EFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKF-GVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPFSMG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 798 TSQPSINALLASLEGN-IDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQaqqlgLGEQ 876
Cdd:PRK14041 236 TSQPPFESMYYAFRENgKETDFDRKALKFLVEYFTKVREKYSEYDVGMKSPDSRILVSQIPGGMYSNLVKQ-----LKEQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 877 WAETK--RAYREANYL---LGDIVKVTPTSKVVGDLAqfmVSNKLTSDDVRRLANsldfpdSVMDFFEGLIGQPYGGFPE 951
Cdd:PRK14041 311 KMLHKldKVLEEVPRVrkdLGYPPLVTPTSQIVGVQA---VLNVLTGERYKRVTN------ETKNYVKGLYGRPPAPIDE 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1028056092 952 PFRSDVLRNKrRKLTCRPGLELEPfDLEKIREDLqNRFGDVDEcDVASYNMYPRVYEDFQK 1012
Cdd:PRK14041 382 ELMKKILGDE-KPIDCRPADLLEP-ELEKARKEL-GILAETDE-DLLIYVILGEVGKKFLK 438
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
565-1014 |
1.36e-85 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 287.04 E-value: 1.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 565 RDAHQSLLATRVRTHDLATIAPTTAHAlaGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLRGANGVA 644
Cdd:PRK12330 13 RDAHQSLMATRMAMEDMVGACEDIDNA--GYWSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQMLLRGQNLLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 645 YSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGGVVEATVCFSGDMLqpgkkYNLDYYLEIAEKIV 724
Cdd:PRK12330 91 YRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYTVSPI-----HTVEGFVEQAKRLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 725 QMGTHILGIKDMAGTMKPAAAKLLIGSLRAKY-PDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMS-GLTSQPS 802
Cdd:PRK12330 166 DMGADSICIKDMAALLKPQPAYDIVKGIKEACgEDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAISSMSlGPGHNPT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 803 iNALLASLEGN-IDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLGLG----EQW 877
Cdd:PRK12330 246 -ESLVEMLEGTgYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTTGVETEIFKSQIPGGMLSNMESQLKQQGAGdrmdEVL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 878 AETKRAYREANYllgdIVKVTPTSKVVGDLAQFmvsnkltsddvrrlaNSLDFPDSVM--DFFEGLIGQpYGGFPEPFRS 955
Cdd:PRK12330 325 EEVPRVRKDAGY----PPLVTPSSQIVGTQAVF---------------NVLMGRYKVLtgEFADLMLGY-YGETPGERNP 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028056092 956 DVL-----RNKRRKLTCRPGLELEPfDLEKIREDLQ--NRFGDVDEcDVASYNMYPRVYEDFQKMR 1014
Cdd:PRK12330 385 EVVeqakkQAKKEPITCRPADLLEP-EWDKLRAEALalEGCDGSDE-DVLTYALFPQVAPKFFATR 448
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
560-832 |
5.28e-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: 251.99 E-value: 5.28e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 560 MDTTWRDAHQSLLATRvRTHDLATIAPTTAHAlaGAFALECWGGATFDVAmrFLHEDPWERLRKLRSLVPNIPFQMLLRG 639
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDEA--GVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 640 AngvaysslpdnaiDHFVKQAKDNGVDIFRVFDALND--------------LEQLKVGVDAVKKAGGVVEATVCFSGDMl 705
Cdd:cd03174 76 R-------------EKGIERALEAGVDEVRIFDSASEthsrknlnksreedLENAEEAIEAAKEAGLEVEGSLEDAFGC- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 706 qpgkKYNLDYYLEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYPDLPIHVHTHDSAGTAVASMTACALAGAD 785
Cdd:cd03174 142 ----KTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEAGAD 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1028056092 786 VVDVAINSMSGLTSQPSINALLASLEGN-IDTGINVEHVRELDAYWAE 832
Cdd:cd03174 218 RVDGSVNGLGERAGNAATEDLVAALEGLgIDTGIDLEKLLEISRYVEE 265
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
559-1010 |
4.14e-74 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 254.27 E-value: 4.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 559 LMDTTWRDAHQSLLATRVRTHDLATIapTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLR 638
Cdd:PRK12581 15 ITETVLRDGHQSLMATRLSIEDMLPV--LTILDKIGYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRLQMLLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 639 GANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGGvvEATVCFSgdmLQPGKKYNLDYYLE 718
Cdd:PRK12581 93 GQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGK--EAQLCIA---YTTSPVHTLNYYLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 719 IAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAkYPDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMSGLT 798
Cdd:PRK12581 168 LVKELVEMGADSICIKDMAGILTPKAAKELVSGIKA-MTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALSPFSEGT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 799 SQPSINAL-LASLEGNIDTGINVEHVRELDAYWAEMRLLY---SCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLG-- 872
Cdd:PRK12581 247 SQPATESMyLALKEAGYDITLDETLLEQAANHLRQARQKYladGILDPSLLFPDPRTLQYQVPGGMLSNMLSQLKQANae 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 873 --LGEQWAETKRAYREanylLGDIVKVTPTSKVVGDLAQFMV----SNKLTSDDVRRLansldfpdsvmdffegLIGQpY 946
Cdd:PRK12581 327 skLEEVLAEVPRVRKD----LGYPPLVTPLSQMVGTQAAMNVilgkPYQMVSKEIKQY----------------LAGD-Y 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028056092 947 GGFPEPFRSDVLRNKRRKLTC---RPGLELEPfDLEKIREDLQNrFGDVDEcDVASYNMYPRVYEDF 1010
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 ... |
20-129 |
3.82e-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: 178.06 E-value: 3.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 20 NKILVANRGEIPIRIFRTAHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEVgqyTPVGAYLAIDEIISIAQKHQVDFIH 99
Cdd:pfam00289 2 KKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPG---PASESYLNIDAIIDAAKETGADAIH 78
|
90 100 110
....*....|....*....|....*....|
gi 1028056092 100 PGYGFLSENSEFADKVAKAGITWIGPPAEV 129
Cdd:pfam00289 79 PGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
359-466 |
1.91e-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: 172.98 E-value: 1.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 359 QCRITTEDPAKNFQPDTGRIEVYRSAGGNGVRLDGGnAYAGTIISPHYDSMLVKCSCSGSTYEIVRRKMIRALIEFRIRG 438
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSG-VYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 1028056092 439 VKTNIPFLLTLLTHPVFIEGTYWTTFID 466
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
83-329 |
1.63e-45 |
|
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: 165.05 E-value: 1.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 83 IDEIIS----IAQKHQVDFIhpgygfLSEN---SEFADKVAKA-GITwiGPPAEVIDSVGDKVSARNLAAKANVPtVPGT 154
Cdd:COG0439 2 IDAIIAaaaeLARETGIDAV------LSESefaVETAAELAEElGLP--GPSPEAIRAMRDKVLMREALAAAGVP-VPGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 155 pGPIETVEEALDFVNEYGYPVIIKAAfggggrgmrvvrEG------------DDVADAFQRATSEARTAFGNGTCFVERF 222
Cdd:COG0439 73 -ALVDSPEEALAFAEEIGYPVVVKPA------------DGagsrgvrvvrdeEELEAALAEARAEAKAGSPNGEVLVEEF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 223 LDKPkHIEVQLLADnHGNVVHlferdCSVQRRHQK---VVE---VAPAKtLPREVRDAILTDAVKLAKECGYRN-AGTAE 295
Cdd:COG0439 140 LEGR-EYSVEGLVR-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTE 211
|
250 260 270
....*....|....*....|....*....|....*.
gi 1028056092 296 FLVDNQNRHYFIEINPRIQVEH--TITEEITGIDIV 329
Cdd:COG0439 212 FLLTPDGEPYLIEINARLGGEHipPLTELATGVDLV 247
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
359-467 |
2.36e-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: 153.03 E-value: 2.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 359 QCRITTEDPAKNFQPDTGRIEVYRSAGGNGVRLDGGnAYAGTIISPHYDSMLVKCSCSGSTYEIVRRKMIRALIEFRIRG 438
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSG-VYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 1028056092 439 VKTNIPFLLTLLTHPVFIEGTYWTTFIDD 467
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
559-829 |
1.82e-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: 121.68 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 559 LMDTTWRDAHQSLLAtrvrthdlatiAPTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLR 638
Cdd:pfam00682 4 ICDTTLRDGEQALGV-----------AFSIDEKLAIARALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVLCR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 639 GAngvaysslpDNAIDHFVKQAKDNGVDIFRVFDALNDLE-QLKVGVDAVKKAGGVVEAT---------VCFSGDMlqpG 708
Cdd:pfam00682 73 AR---------EHDIKAAVEALKGAGAVRVHVFIATSDLHrKYKLGKDREEVAKRAVAAVkaarsrgidVEFSPED---A 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 709 KKYNLDYYLEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYPD-LPIHVHTHDSAGTAVASMTACALAGADVV 787
Cdd:pfam00682 141 SRTDPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1028056092 788 DVAINSMSGLTSQPSINALLASLEG-NIDTGINVEHVRELDAY 829
Cdd:pfam00682 221 DGTVNGIGERAGNAALEEVAAALEGlGVDTGLDLQRLRSIANL 263
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1102-1168 |
3.99e-24 |
|
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: 96.72 E-value: 3.99e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028056092 1102 HIGAPMAGVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLL 1168
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1102-1168 |
4.44e-20 |
|
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: 85.34 E-value: 4.44e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1028056092 1102 HIGAPMAGV-----IVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLL 1168
Cdd:pfam00364 2 EIKSPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1088-1169 |
1.89e-14 |
|
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: 71.46 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 1088 ETVTKSKADMHDPLHIGAPMAGVI-------VEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVD 1160
Cdd:COG0511 48 PAAAAAAAAASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVE 127
|
....*....
gi 1028056092 1161 SSDLLVLLE 1169
Cdd:COG0511 128 YGQPLFVIE 136
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
53-312 |
1.43e-13 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 73.38 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 53 DRLSTHKQKADEAYVIgevgqyTPVGAYLAIDEIISIAQKHQVDFIHPGY----GFLSENsefADKVAKAGITWIGPPAE 128
Cdd:PRK12767 34 SELAPALYFADKFYVV------PKVTDPNYIDRLLDICKKEKIDLLIPLIdpelPLLAQN---RDRFEEIGVKVLVSSKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 129 VIDSVGDKVSARNLAAKANVPTVPG-TPGPIETVEEAlDFVNEYGYPVIIKAAFGGGGRGMRVVREGDDVADAFQRatse 207
Cdd:PRK12767 105 VIEICNDKWLTYEFLKENGIPTPKSyLPESLEDFKAA-LAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEY---- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 208 artafgNGTCFVERFLDKPKhIEVQLLADNHGNVVHlferdcSVQRRHQKVV--EVAPAKTlpreVRDAILTDAV-KLAK 284
Cdd:PRK12767 180 ------VPNLIIQEFIEGQE-YTVDVLCDLNGEVIS------IVPRKRIEVRagETSKGVT----VKDPELFKLAeRLAE 242
|
250 260
....*....|....*....|....*...
gi 1028056092 285 ECGYRNAGTAEFLVDNqNRHYFIEINPR 312
Cdd:PRK12767 243 ALGARGPLNIQCFVTD-GEPYLFEINPR 269
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
112-312 |
4.16e-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: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 112 ADKVAKAGITW----IGPPAEVIDSVGDKVSARNLAAKANVPTVPGtpGPIETVEEALDFVNEYGYPVIIKAAFggggrg 187
Cdd:COG0458 87 AVELEEAGILEgvkiLGTSPDAIDLAEDRELFKELLDKLGIPQPKS--GTATSVEEALAIAEEIGYPVIVRPSY------ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 188 mrvvregddV-----------ADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVV------HlFER--- 247
Cdd:COG0458 159 ---------VlggrgmgivynEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIivgimeH-IEPagv 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028056092 248 ---DCSVqrrhqkvveVAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNqNRHYFIEINPR 312
Cdd:COG0458 229 hsgDSIC---------VAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDD-GRVYVIEVNPR 286
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1102-1169 |
4.36e-13 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 65.19 E-value: 4.36e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028056092 1102 HIGAPMAGVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLLE 1169
Cdd:PRK08225 3 KVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1103-1168 |
6.09e-13 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 67.58 E-value: 6.09e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1028056092 1103 IGAPMAGVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLL 1168
Cdd:PRK05641 87 VTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
32-313 |
1.26e-11 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 68.03 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 32 IRIFrtaHELSMQTVAIYSHEDRLSTHKQKADEAYVIGEVGQYTPVgaylAIDEIISIAQKHQVDFIHPGY----GFLSE 107
Cdd:COG3919 21 ARSL---GEAGVRVIVVDRDPLGPAARSRYVDEVVVVPDPGDDPEA----FVDALLELAERHGPDVLIPTGdeyvELLSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 108 N-SEFADKVAkagITWigPPAEVIDSVGDKVSARNLAAKANVPtVPGTpGPIETVEEALDFVNEYGYPVIIKAAfGGGGR 186
Cdd:COG3919 94 HrDELEEHYR---LPY--PDADLLDRLLDKERFYELAEELGVP-VPKT-VVLDSADDLDALAEDLGFPVVVKPA-DSVGY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 187 GMRVVREGDDV-----ADAFQRATSEARTAFGNgtCFVERFLDKPKHIE--VQLLADNHGNVVHLFerdcSVQRRHQKVV 259
Cdd:COG3919 166 DELSFPGKKKVfyvddREELLALLRRIAAAGYE--LIVQEYIPGDDGEMrgLTAYVDRDGEVVATF----TGRKLRHYPP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1028056092 260 EVAPAkTLpREVRD--AILTDAVKLAKECGYRNAGTAEFLVDNQ-NRHYFIEINPRI 313
Cdd:COG3919 240 AGGNS-AA-RESVDdpELEEAARRLLEALGYHGFANVEFKRDPRdGEYKLIEINPRF 294
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
18-329 |
1.44e-11 |
|
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: 69.26 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 18 EKNKILVANRGeiPIRI-----F--------RTAHELSMQTVAIYSHEDRLSTHKQKADEAYvigevgqYTPvgayLAID 84
Cdd:TIGR01369 553 DKKKVLVLGSG--PNRIgqgveFdyccvhavLALRELGYETIMINYNPETVSTDYDTSDRLY-------FEP----LTFE 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 85 EIISIAQKHQVDFIHPGYGFLSENSeFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGtpGPIETVEEA 164
Cdd:TIGR01369 620 DVMNIIELEKPEGVIVQFGGQTPLN-LAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEA 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 165 LDFVNEYGYPVIIKAAFGGGGRGMRVVREGDDVADAFQRATSEArtafGNGTCFVERFLDKPKHIEVQLLADnHGNVV-- 242
Cdd:TIGR01369 697 VEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVS----PEHPVLIDKYLEDAVEVDVDAVSD-GEEVLip 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 243 HLFErdcsvqrrHqkvVEVA-----------PAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNqNRHYFIEINP 311
Cdd:TIGR01369 772 GIME--------H---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKD-GEVYVIEVNP 839
|
330
....*....|....*...
gi 1028056092 312 RIQVEHTITEEITGIDIV 329
Cdd:TIGR01369 840 RASRTVPFVSKATGVPLA 857
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
20-313 |
4.52e-11 |
|
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: 67.33 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 20 NKILVANRGeiPIRIFRTAH-------------ELSMQTVAIYSHEDRLSTHKQKADEAYvigevgqYTPVGAYlAIDEI 86
Cdd:TIGR01369 7 KKILVIGSG--PIVIGQAAEfdysgsqackalkEEGYRVILVNSNPATIMTDPEMADKVY-------IEPLTPE-AVEKI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 87 IsiaQKHQVDFIHPGYG-----FLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGtpGPIETV 161
Cdd:TIGR01369 77 I---EKERPDAILPTFGgqtalNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIAHSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 162 EEALDFVNEYGYPVIIKAAFGGGGRgmrvvreGDDVA---DAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNH 238
Cdd:TIGR01369 152 EEALAAAKEIGYPVIVRPAFTLGGT-------GGGIAynrEELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 239 GNVVHLferdCSVQR-----RH--QKVVeVAPAKTLPRE----VRDAiltdAVKLAKECGYRNAGTAEFLVDNQN-RHYF 306
Cdd:TIGR01369 225 DNCITV----CNMENfdpmgVHtgDSIV-VAPSQTLTDKeyqmLRDA----SIKIIRELGIEGGCNVQFALNPDSgRYYV 295
|
....*..
gi 1028056092 307 IEINPRI 313
Cdd:TIGR01369 296 IEVNPRV 302
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1103-1166 |
1.89e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 59.83 E-value: 1.89e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028056092 1103 IGAPMAGVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLV 1166
Cdd:PRK06549 64 MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
16-329 |
5.34e-10 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 63.83 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 16 LGEKNKILVANRGeiPIRI-----F--------RTAHELSMQTVAIYSHEDRLSTHKQKADEAYvigevgqYTPvgayLA 82
Cdd:PRK12815 552 SSEKKKVLILGSG--PIRIgqgieFdyssvhaaFALKKEGYETIMINNNPETVSTDYDTADRLY-------FEP----LT 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 83 IDEIISIAQKHQVDFIHPGYGFLSENSeFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGtpGPIETVE 162
Cdd:PRK12815 619 LEDVLNVAEAENIKGVIVQFGGQTAIN-LAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEE 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 163 EALDFVNEYGYPVIIKAAFGGGGRGMRVVREGDDVADAFQRATSEARTAfgngtcFVERFLDKpKHIEVQLLADnhGNVV 242
Cdd:PRK12815 696 EAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENASQLYPI------LIDQFIDG-KEYEVDAISD--GEDV 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 243 HL---FErdcsvqrrHqkvVE-----------VAPAKTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDNqNRHYFIE 308
Cdd:PRK12815 767 TIpgiIE--------H---IEqagvhsgdsiaVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAN-DEIYVLE 834
|
330 340
....*....|....*....|...
gi 1028056092 309 INPRiqVEHT--ITEEITGIDIV 329
Cdd:PRK12815 835 VNPR--ASRTvpFVSKATGVPLA 855
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
43-329 |
5.75e-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: 61.88 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 43 MQTVAIYSHEDRLSTHKQKADEAYVIG-EVGQYTPVGAYLAIDEIISIAQK---HQVDFI-----HPGYGFlsensEFAD 113
Cdd:COG0189 1 MMKIAILTDPPDKDSTKALIEAAQRRGhEVEVIDPDDLTLDLGRAPELYRGedlSEFDAVlpridPPFYGL-----ALLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 114 KVAKAGITWIGPPAEVIDSvGDKVSARNLAAKANVPTvpgtpgP----IETVEEALDFVNEYGYPVIIKAAFggggrgmr 189
Cdd:COG0189 76 QLEAAGVPVVNDPEAIRRA-RDKLFTLQLLARAGIPV------PptlvTRDPDDLRAFLEELGGPVVLKPLD-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 190 vVREGDDVA-----DAFqRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNhGNVVHLFERDcsVQRRHQKVVEVAPA 264
Cdd:COG0189 141 -GSGGRGVFlvedeDAL-ESILEALTELGSEPVLVQEFIPEEDGRDIRVLVVG-GEPVAAIRRI--PAEGEFRTNLARGG 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028056092 265 KTLPREVRDAILTDAVKLAKECGYRNAGTaEFLVDNqNRHYFIEINPRIQVEHtiTEEITGIDIV 329
Cdd:COG0189 216 RAEPVELTDEERELALRAAPALGLDFAGV-DLIEDD-DGPLVLEVNVTPGFRG--LERATGVDIA 276
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
663-826 |
5.78e-09 |
|
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: 59.80 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 663 NGVDIFRVFDALN-DLEQ-LKVGVDAVK--KAGGvveATVCFSG-DmlqpGKKYNLDYYLEIAEKIVQMGTHILGIKDMA 737
Cdd:COG0119 99 IKTSDLHVEYKLRkTREEvLEMAVEAVKyaKEHG---LEVEFSAeD----ATRTDPDFLLEVLEAAIEAGADRINLPDTV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 738 GTMKPAAAKLLIGSLRAKYPDLPIHVHTHDSAGTAVA-SMTAcALAGADVVDVAINsmsGL---TSQPSINALLASLE-- 811
Cdd:COG0119 172 GGATPNEVADLIEELRERVPDVILSVHCHNDLGLAVAnSLAA-VEAGADQVEGTIN---GIgerAGNAALEEVVMNLKlk 247
|
170
....*....|....*
gi 1028056092 812 GNIDTGINVEHVREL 826
Cdd:COG0119 248 YGVDTGIDLSKLTEL 262
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
712-832 |
1.23e-08 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 58.65 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 712 NLDYYLEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRaKYPDLPIHVHTHDSAGTAVASMTACALAGADVVDVAI 791
Cdd:PRK11858 143 DLDFLIEFAKAAEEAGADRVRFCDTVGILDPFTMYELVKELV-EAVDIPIEVHCHNDFGMATANALAGIEAGAKQVHTTV 221
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1028056092 792 NsmsGLTSQPSINAL---LASL--EGNIDTGINVEHVRELDAYWAE 832
Cdd:PRK11858 222 N---GLGERAGNAALeevVMALkyLYGIDLGIDTERLYELSRLVSK 264
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
713-826 |
1.35e-08 |
|
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: 57.46 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 713 LDYYLEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYP--DLPIHVHTHDSAGTAVASMTACALAGADVVDVA 790
Cdd:cd07940 142 LDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVPniKVPISVHCHNDLGLAVANSLAAVEAGARQVECT 221
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1028056092 791 INSM---SGltsqpsiNallASLE------------GNIDTGINVEHVREL 826
Cdd:cd07940 222 INGIgerAG-------N---AALEevvmalktrydyYGVETGIDTEELYET 262
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
627-821 |
1.00e-07 |
|
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: 54.71 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 627 LVPNipfqmlLRGAngvaysslpDNAIDHfvkqakdnGVDIFRVF----DALN----------DLEQLKVGVDAVKKAGG 692
Cdd:cd07938 72 LVPN------LRGA---------ERALAA--------GVDEVAVFvsasETFSqknincsiaeSLERFEPVAELAKAAGL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 693 VVEATV-----C-FSGDMlqpgkkyNLDYYLEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYPDLPIHVHTH 766
Cdd:cd07938 129 RVRGYVstafgCpYEGEV-------PPERVAEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERFPDEKLALHFH 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028056092 767 DSAGTAVASMTACALAGADVVDVainSMSGLTSQP-----SIN----ALLASLEG-NIDTGINVE 821
Cdd:cd07938 202 DTRGQALANILAALEAGVRRFDS---SVGGLGGCPfapgaTGNvateDLVYMLEGmGIETGIDLD 263
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
83-179 |
1.46e-07 |
|
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: 55.40 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 83 IDEIISIAQKHQVDFIHPGygflsenSE------FADKVAKAGITWIGPPA-----EvidsvGDKVSARNLAAKANVPTV 151
Cdd:COG0151 51 IEALVAFAKEENIDLVVVG-------PEaplvagIVDAFRAAGIPVFGPSKaaaqlE-----GSKAFAKEFMARYGIPTA 118
|
90 100
....*....|....*....|....*...
gi 1028056092 152 PGtpGPIETVEEALDFVNEYGYPVIIKA 179
Cdd:COG0151 119 AY--RVFTDLEEALAYLEEQGAPIVVKA 144
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1100-1166 |
6.18e-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: 47.82 E-value: 6.18e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028056092 1100 PLHIGAPMAGVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLV 1166
Cdd:cd06663 5 PDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLV 71
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
125-312 |
1.05e-06 |
|
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: 52.38 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 125 PPAEVIDSVGDKVSARNLAAKANVPTVPGTPgpIETVEEALDFVNEYGYPVIIKAAFggggrgmrvvrEG---------- 194
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAPFAA--VDSLEDLEAAIAELGLPAVLKTRR-----------GGydgkgqvvik 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 195 --DDVADAFQratseartAFGNGTCFVERFLD--KpkhiEVQLLA--DNHGNVVH--LFErdcSVQRRHQKVVEVAPAKt 266
Cdd:COG0026 146 saADLEAAWA--------ALGGGPCILEEFVPfeR----ELSVIVarSPDGEVATypVVE---NVHRNGILDESIAPAR- 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1028056092 267 LPREVRDAILTDAVKLAKECGYRnaGT--AEFLVDNQNRHYFIEINPR 312
Cdd:COG0026 210 ISEALAAEAEEIAKRIAEALDYV--GVlaVEFFVTKDGELLVNEIAPR 255
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1103-1168 |
1.39e-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: 1.39e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028056092 1103 IGAPMA-GVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLL 1168
Cdd:COG0508 10 LGESMTeGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
116-328 |
2.68e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 51.89 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 116 AKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPtVPGTpGPIETVEEALDFVNEYGYPVIIKAAFGGGGRGMRVVREGD 195
Cdd:PRK12815 109 EQYGVELLGTNIEAIQKGEDRERFRALMKELGEP-VPES-EIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 196 DVADAFQRATSEARTAfgngTCFVERFLDKPKHIEVQLLADNHGNVVHLferdCSVQRrhqkvVE-----------VAPA 264
Cdd:PRK12815 187 ELEQLFKQGLQASPIH----QCLLEESIAGWKEIEYEVMRDRNGNCITV----CNMEN-----IDpvgihtgdsivVAPS 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028056092 265 KTLP----REVRDAiltdAVKLAKECGYRNAGTAEFLVD-NQNRHYFIEINPRIQVEHTITEEITGIDI 328
Cdd:PRK12815 254 QTLTddeyQMLRSA----SLKIISALGVVGGCNIQFALDpKSKQYYLIEVNPRVSRSSALASKATGYPI 318
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
82-312 |
3.33e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 51.64 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 82 AIDEIIsiaQKHQVDFIHPGYG---FLSENSEFADK--VAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGtpG 156
Cdd:PRK05294 73 FVEKII---EKERPDAILPTMGgqtALNLAVELAESgvLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--G 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 157 PIETVEEALDFVNEYGYPVIIKAAFGGGGRgmrvvreGDDVA---DAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQL 233
Cdd:PRK05294 148 IAHSMEEALEVAEEIGYPVIIRPSFTLGGT-------GGGIAyneEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 234 LADNHGNVVHLferdCSvqrrhqkvVE--------------VAPAKTLP-RE---VRDAiltdAVKLAKECGYRNAGT-A 294
Cdd:PRK05294 221 MRDKNDNCIIV----CS--------IEnidpmgvhtgdsitVAPAQTLTdKEyqmLRDA----SIAIIREIGVETGGCnV 284
|
250
....*....|....*....
gi 1028056092 295 EFLVDNQN-RHYFIEINPR 312
Cdd:PRK05294 285 QFALNPKDgRYIVIEMNPR 303
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
655-828 |
5.35e-06 |
|
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: 49.42 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 655 HFVKQAKDNGVDIFRVFDALNDLEQLKVGVDAVKKAGgvVEaTVCF---SGdMLQPGKkynldyYLEIAEKIVQMGTHIL 731
Cdd:cd07943 89 DDLKMAADLGVDVVRVATHCTEADVSEQHIGAARKLG--MD-VVGFlmmSH-MASPEE------LAEQAKLMESYGADCV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 732 GIKDMAGTMKPAAAKLLIGSLRAKYPDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSM---SGLTsqpSINALLA 808
Cdd:cd07943 159 YVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATRIDGSLAGLgagAGNT---PLEVLVA 235
|
170 180
....*....|....*....|.
gi 1028056092 809 SLE-GNIDTGINVEHVreLDA 828
Cdd:cd07943 236 VLErMGIETGIDLYKL--MDA 254
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
135-311 |
1.20e-05 |
|
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: 48.56 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 135 DKVSARNLAAKANVPTVP------GTPGPIETVEEALdfvneyGYPVIIKAAFggggrgmrvvrEG-----------DDV 197
Cdd:COG1181 95 DKALTKRVLAAAGLPTPPyvvlrrGELADLEAIEEEL------GLPLFVKPAR-----------EGssvgvskvknaEEL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 198 ADAFQRATSEARTAfgngtcFVERFLDkPKHIEVQLLADNHGNVVHLFERDcsVQRR----HQK-----VVEVAPAKtLP 268
Cdd:COG1181 158 AAALEEAFKYDDKV------LVEEFID-GREVTVGVLGNGGPRALPPIEIV--PENGfydyEAKytdggTEYICPAR-LP 227
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1028056092 269 REVRDAILTDAVKLAKECGYRNAGTAEFLVDNQNRHYFIEINP 311
Cdd:COG1181 228 EELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
678-826 |
1.46e-05 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 49.17 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 678 EQLKVGVDAV---KKAGGVVEatvcFSGdmlQPGKKYNLDYYLEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLrA 754
Cdd:PRK09389 111 EVLETAVEAVeyaKDHGLIVE----LSG---EDASRADLDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRL-S 182
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028056092 755 KYPDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMSGLTSQPSINALLASLEG--NIDTGINVEHVREL 826
Cdd:PRK09389 183 ELVKGPVSIHCHNDFGLAVANTLAALAAGADQVHVTINGIGERAGNASLEEVVMALKHlyDVETGIKLEELYEL 256
|
|
| DRE_TIM_CMS |
cd07945 |
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ... |
708-823 |
1.76e-05 |
|
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: 47.76 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 708 GKKYNLDYYLEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYPDLPIHVHTHDSAGTAVASMTACALAGADVV 787
Cdd:cd07945 141 GMRDSPDYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFHAHNDYDLAVANVLAAVKAGIKGL 220
|
90 100 110
....*....|....*....|....*....|....*...
gi 1028056092 788 DVAINSMSGLTSQPSINALLASLEG--NIDTGINVEHV 823
Cdd:cd07945 221 HTTVNGLGERAGNAPLASVIAVLKDklKVKTNIDEKRL 258
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
125-312 |
4.99e-05 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 47.07 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 125 PPAEVIDSVGDKVSARNLAAKANVPTVPGTPgpIETVEEALDFVNEYGYPVIIKAAFggggrgmrvvrEG---------D 195
Cdd:PRK06019 90 PGPDALAIAQDRLTEKQFLDKLGIPVAPFAV--VDSAEDLEAALADLGLPAVLKTRR-----------GGydgkgqwviR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 196 DVADAfqratSEARTAFGNGTCFVERF--LDKpkhiEVQLLA--DNHGNVVH--LFErdcSVQRRHQKVVEVAPAKtLPR 269
Cdd:PRK06019 157 SAEDL-----EAAWALLGSVPCILEEFvpFER----EVSVIVarGRDGEVVFypLVE---NVHRNGILRTSIAPAR-ISA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1028056092 270 EVRDAILTDAVKLAKECGYRnaGTA--EFLVDNQNRHYFIEINPR 312
Cdd:PRK06019 224 ELQAQAEEIASRIAEELDYV--GVLavEFFVTGDGELLVNEIAPR 266
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
677-832 |
6.08e-05 |
|
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) of Streptomyces rubellomurinus catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate and CoA, a reaction similar to one catalyzed by homocitrate synthase. The gene encoding FrbC is one of several genes required for the biosynthesis of FR900098, a potent antimalarial antibiotic. This protein is also required for assembly of the nitrogenase MoFe complex but its exact role is unknown. This family also includes the NifV proteins of Heliobacterium chlorum and Gluconacetobacter diazotrophicus, which appear to be orthologous to FrbC. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163677 [Multi-domain] Cd Length: 259 Bit Score: 45.96 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 677 LEQLKVGVDAVKKAGgvveATVCFSGdmlQPGKKYNLDYYLEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKY 756
Cdd:cd07939 109 LDQLRRLVGRAKDRG----LFVSVGA---EDASRADPDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAAT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 757 pDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINsmsGLTSQpsinALLASLE---------GNIDTGINVEHVRELD 827
Cdd:cd07939 182 -DLPLEFHAHNDLGLATANTLAAVRAGATHVSVTVN---GLGER----AGNAALEevvmalkhlYGRDTGIDTTRLPELS 253
|
....*
gi 1028056092 828 AYWAE 832
Cdd:cd07939 254 QLVAR 258
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1105-1168 |
1.14e-04 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 41.33 E-value: 1.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028056092 1105 APMAGVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLL 1168
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
124-312 |
1.18e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 46.70 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 124 GPPAEVIDSVGDKVSARNLAAKANVPTVPGtpGPIETVEEALDFVNEYGYPVIIKAAFGGGGRGMRVVREGDDVadafQR 203
Cdd:PLN02735 691 GTSPDSIDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKL----KT 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 204 ATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVV-------------HLFERDCSVqrrhqkvvevaPAKTLPRE 270
Cdd:PLN02735 765 YLETAVEVDPERPVLVDKYLSDATEIDVDALADSEGNVViggimehieqagvHSGDSACSL-----------PTQTIPSS 833
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1028056092 271 VRDAILTDAVKLAKE---CGYRNagtAEFLVDNQNRHYFIEINPR 312
Cdd:PLN02735 834 CLATIRDWTTKLAKRlnvCGLMN---CQYAITPSGEVYIIEANPR 875
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1103-1178 |
2.30e-04 |
|
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: 45.25 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 1103 IGAPMAGVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLLE----DQVPVETKA 1178
Cdd:TIGR01348 8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEvgagAQAQAEAKK 87
|
|
| PLN03228 |
PLN03228 |
methylthioalkylmalate synthase; Provisional |
714-794 |
2.50e-04 |
|
methylthioalkylmalate synthase; Provisional
Pssm-ID: 178767 [Multi-domain] Cd Length: 503 Bit Score: 44.91 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 714 DYYLEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYP---DLPIHVHTHDSAGTAVASMTACALAGADVVDVA 790
Cdd:PLN03228 239 EFLCKILGEAIKAGATSVGIADTVGINMPHEFGELVTYVKANTPgidDIVFSVHCHNDLGLATANTIAGICAGARQVEVT 318
|
....
gi 1028056092 791 INSM 794
Cdd:PLN03228 319 INGI 322
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
115-328 |
2.50e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 45.54 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 115 VAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGtpGPIETVEEALDFVNEYG-YPVIIKAAFGGGGRgmrvvre 193
Cdd:PLN02735 124 LEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPS--GIATTLDECFEIAEDIGeFPLIIRPAFTLGGT------- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 194 GDDVA---DAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLferdCSVQRRHQKVVE------VAPA 264
Cdd:PLN02735 195 GGGIAynkEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVII----CSIENIDPMGVHtgdsitVAPA 270
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028056092 265 KTLP----REVRDAILTDAVKLAKECGYRNAGTAEFLVDNQnrHYFIEINPRIQVEHTITEEITGIDI 328
Cdd:PLN02735 271 QTLTdkeyQRLRDYSVAIIREIGVECGGSNVQFAVNPVDGE--VMIIEMNPRVSRSSALASKATGFPI 336
|
|
| PRK05692 |
PRK05692 |
hydroxymethylglutaryl-CoA lyase; Provisional |
717-834 |
4.13e-04 |
|
hydroxymethylglutaryl-CoA lyase; Provisional
Pssm-ID: 180206 Cd Length: 287 Bit Score: 43.72 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 717 LEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYPDLPIHVHTHDSAGTAVASMTACALAGADVVDVAINSMSG 796
Cdd:PRK05692 158 ADVAERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAEFPAERLAGHFHDTYGQALANIYASLEEGITVFDASVGGLGG 237
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1028056092 797 LTSQP------SINALLASLEG-NIDTGINVEHVRELDAYWAEMR 834
Cdd:PRK05692 238 CPYAPgasgnvATEDVLYMLHGlGIETGIDLDKLVRAGQFIQSKL 282
|
|
| PRK06524 |
PRK06524 |
biotin carboxylase-like protein; Validated |
104-325 |
6.73e-04 |
|
biotin carboxylase-like protein; Validated
Pssm-ID: 180605 [Multi-domain] Cd Length: 493 Bit Score: 43.58 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 104 FLSENSEFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPIETVEEALDFVNEYGYpviikaafgg 183
Cdd:PRK06524 111 FVMFDEETEALARQAGLEVMHPPAELRHRLDSKIVTTRLANEAGVPSVPHVLGRVDSYDELSALAHGAGL---------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 184 ggrgmrvvreGDDVAdafqratseARTAFGN---GTCFVERFLDKPKHIEvQLLADNHGNVV-HLFERDCSVQ---RRHQ 256
Cdd:PRK06524 181 ----------GDDLV---------VQTPYGDsgsTTFFVRGQRDWDKYAG-GIVGQPEIKVMkRIRNVEVCIEacvTRHG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 257 KVV-----------EVAPAK-----------TLPREVRDAILTDAVKLA---KECGYRNAGTAEFLVD-NQNRHYFIEIN 310
Cdd:PRK06524 241 TVIgpamtslvgypELTPYRggwcgndiwpgALPPAQTRKAREMVRKLGdvlSREGYRGYFEVDLLHDlDADELYLGEVN 320
|
250
....*....|....*
gi 1028056092 311 PRIQVEHTITEEITG 325
Cdd:PRK06524 321 PRLSGASPMTNLTTE 335
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1103-1170 |
7.54e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 43.66 E-value: 7.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028056092 1103 IGAPMAGVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLLED 1170
Cdd:PRK11855 10 IGEVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEA 77
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1103-1169 |
7.63e-04 |
|
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: 43.71 E-value: 7.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1028056092 1103 IGAPMAGVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLLE 1169
Cdd:TIGR01348 124 IGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLS 190
|
|
| PRK00915 |
PRK00915 |
2-isopropylmalate synthase; Validated |
713-792 |
1.45e-03 |
|
2-isopropylmalate synthase; Validated
Pssm-ID: 234864 [Multi-domain] Cd Length: 513 Bit Score: 42.79 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 713 LDYYLEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYP---DLPIHVHTHDSAGTAVASMTACALAGADVVDV 789
Cdd:PRK00915 148 LDFLCRVVEAAIDAGATTINIPDTVGYTTPEEFGELIKTLRERVPnidKAIISVHCHNDLGLAVANSLAAVEAGARQVEC 227
|
...
gi 1028056092 790 AIN 792
Cdd:PRK00915 228 TIN 230
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1111-1178 |
1.53e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 42.50 E-value: 1.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028056092 1111 IVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLLEDQVPVETKA 1178
Cdd:PRK11855 135 VIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAA 202
|
|
| MfnD |
COG1821 |
Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme ... |
110-313 |
2.83e-03 |
|
Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme transport and metabolism];
Pssm-ID: 441426 [Multi-domain] Cd Length: 323 Bit Score: 41.45 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 110 EFADKVAKAGITWIGPPAEVIDSVGDKVSARNLAAKANVPTVPGTPGPietveealDFVNEYGYPVIIKAafggggrgmr 189
Cdd:COG1821 99 RLTRIVEAAGKRNLGSSPEAIALAADKLLTAELLAAAGIPTPPTFPAD--------DAPPLLAGPWVVKP---------- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 190 vvregDDVADA-----FQRATSEARTAFGNGTCFVERFLDKpKHIEVQLLAdNHGNVVHLferdcSVQRRHqkvVEVAPA 264
Cdd:COG1821 161 -----DDGAGSegtrlFDDPAALRAREARGAGLIVQPYIEG-EAASLSLLC-GRGGALLL-----SINRQR---IEVDGG 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1028056092 265 K------TLP-REVRDAILTDAVKLAKEC-----GYrnAGtaeflVD---NQNRHYFIEINPRI 313
Cdd:COG1821 226 RfsylggTVPaEHPRKEELQALAQKVAEAlpglrGY--VG-----VDlilTADGPVVVEVNPRL 282
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1103-1170 |
3.12e-03 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 41.32 E-value: 3.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028056092 1103 IGAPMA-GVIVEVKVHKGSLIKKGQPVAVLSAMKMEMIISSPSDGQVKEVFVSDGENVDSSDLLVLLED 1170
Cdd:PRK11856 10 LGEGMTeGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEE 78
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
117-328 |
3.19e-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: 40.79 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 117 KAGITWIGPPaEVIDSVGDKVSARNLAAKANVPTvPGTpGPIETVEEALDFVNEYGYPVIIKAAFGGGgrgmrvvreGDD 196
Cdd:TIGR00768 71 SLGVPVINSS-DAILNAGDKFLSHQLLAKAGIPL-PRT-GLAGSPEEALKLIEEIGFPVVLKPVFGSW---------GRG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 197 VADAFQR----ATSEARTAFGN--GTCFVERFLDKPKHIEVQLLADNhGNVVHLFERdcsVQRRHQKVVEVAPAKTLPRE 270
Cdd:TIGR00768 139 VSLARDRqaaeSLLEHFEQLNGpqNLFLVQEYIKKPGGRDIRVFVVG-DEVVAAIYR---ITSGHWRSNLARGGKAEPCS 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1028056092 271 VRDAILTDAVKLAKECGYRNAGTAefLVDNQNRHYFIEINPriQVEHTITEEITGIDI 328
Cdd:TIGR00768 215 LTEEIEELAIKAAKALGLDVAGVD--LLESEDGLLVNEVNA--NPEFKNSVKTTGVNI 268
|
|
| PLN02746 |
PLN02746 |
hydroxymethylglutaryl-CoA lyase |
719-827 |
3.66e-03 |
|
hydroxymethylglutaryl-CoA lyase
Pssm-ID: 178347 Cd Length: 347 Bit Score: 40.93 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 719 IAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYPDLPIHVHTHDSAGTAVASMTACALAGADVVDvaiNSMSGLT 798
Cdd:PLN02746 202 VAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDKLAVHFHDTYGQALANILVSLQMGISTVD---SSVAGLG 278
|
90 100 110
....*....|....*....|....*....|....*..
gi 1028056092 799 SQPSinALLASleGNIDT--------GINVEHVRELD 827
Cdd:PLN02746 279 GCPY--AKGAS--GNVATedvvymlnGLGVSTNVDLG 311
|
|
| DRE_TIM_HCS |
cd07948 |
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ... |
717-832 |
5.19e-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: 40.01 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 717 LEIAEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRAKYpDLPIHVHTHDSAGTAVASMTACALAGADVVDVA---INS 793
Cdd:cd07948 144 LRVYRAVDKLGVNRVGIADTVGIATPRQVYELVRTLRGVV-SCDIEFHGHNDTGCAIANAYAALEAGATHIDTTvlgIGE 222
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1028056092 794 MSGLTSQPSINALLASLE-GNIDTGINVEHVRELDAYWAE 832
Cdd:cd07948 223 RNGITPLGGLIARMYTADpEYVVSKYKLELLPELERLVAD 262
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
83-328 |
5.41e-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: 40.67 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 83 IDEIISIAQKHQVDFIHPGYGFlsEN-SEFADKVAKAGItWIGPPAEVIDSVGDKVSARNLAAKANVPtVPgtpgPIETV 161
Cdd:COG2232 62 PAALLELAAADDPDGLVYGSGF--ENfPELLERLARRLP-LLGNPPEVVRRVKDPLRFFALLDELGIP-HP----ETRFE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 162 EEALDfvneygYPVIIKAAFGGGgrgmrvvreGDDVADAfqratseARTAFGNGTCFVERFLDKPkHIEVQLLADNHGNV 241
Cdd:COG2232 134 PPPDP------GPWLVKPIGGAG---------GWHIRPA-------DSEAPPAPGRYFQRYVEGT-PASVLFLADGSDAR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 242 VHLFERdcsvqrrhQKVVE-----------VAPAkTLPREVRDAILTDAVKLAKECGYRNAGTAEFLVDnQNRHYFIEIN 310
Cdd:COG2232 191 VLGFNR--------QLIGPagerpfryggnIGPL-ALPPALAEEMRAIAEALVAALGLVGLNGVDFILD-GDGPYVLEVN 260
|
250
....*....|....*...
gi 1028056092 311 PRIQVEHTITEEITGIDI 328
Cdd:COG2232 261 PRPQASLDLYEDATGGNL 278
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1085-1175 |
6.41e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 40.76 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028056092 1085 QKVETVTKSKADMHDPlhigAPMAGVIVEVKVHKGSLIKKGQPVAVL--------------SAMKMEMIISSPSDGQVKE 1150
Cdd:PRK11854 32 QSLITVEGDKASMEVP----SPQAGVVKEIKVKVGDKVETGALIMIFesadgaadaapaqaEEKKEAAPAAAPAAAAAKD 107
|
90 100
....*....|....*....|....*..
gi 1028056092 1151 VFVSD--GENVDSSDLLVLLEDQVPVE 1175
Cdd:PRK11854 108 VHVPDigSDEVEVTEILVKVGDTVEAE 134
|
|
| |
