|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-1127 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 1977.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1 MFSKVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGDIGHPVHAYLSVDEIVATARRAGADAIY 80
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 81 PGYGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLMSSA-PSASVDELLSVAAGMPFPLFVKA 159
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEgPIDDIEEALEFAEEIGYPIMLKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 160 VAGGGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNLGDVIHLYERDCSVQRRHQKVI 239
Cdd:PRK12999 164 SAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 240 ELAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDERGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAGE 319
Cdd:PRK12999 244 EIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 320 TLEQLG---LRQEDIAPHGAALQCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGSTNL-GAEISPYFDSMLVKLTCR 395
Cdd:PRK12999 324 TLHDLEigiPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFaGAEITPYYDSLLVKLTAW 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 396 GRDLPTAVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFIDERPQLLTARASADRGTKILNFLADVTVNNP 475
Cdd:PRK12999 404 GRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTVNGF 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 476 YGSRP-STIYPDDKLPDLDLRAAPPAGSKQRLVKLGPEGFARWLRESAAVGVTDTTFRDAHQSLLATRVRTSGLSRVAPY 554
Cdd:PRK12999 484 PGVKKkPPVFPDPRLPKVDLSAPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLLRIAPA 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 555 LARTMPQLLSVECWGGATYDVALRFLKEDPWERLATLRAAMPNICLQMLLRGRNTVGYTPYPEIVTSAFVQEATATGIDI 634
Cdd:PRK12999 564 TARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAAAGIDV 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 635 FRIFDALNNIESMRPAIDAVRETGsAIAEVAMCYTGDLTDPGEQLYTLDYYLKLAEQIVDAGAHVLAIKDMAGLLRPPAA 714
Cdd:PRK12999 644 FRIFDSLNWVENMRVAIDAVRETG-KIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMAGLLKPAAA 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 715 QRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAVDGAAAPLAGTTSQPALSSIVAAAAHTEYDTGLSLSAVCA 794
Cdd:PRK12999 723 YELVSALKEEVDLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDLDAIRK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 795 LEPYWEALRKVYAPFESGLPGPTGRVYHHEIPGGQLSNLRQQAIALGLGDRFEEIEEAYAGADRVLGRLVKVTPTSKVVG 874
Cdd:PRK12999 803 LSPYWEAVRPYYAPFESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVTPSSKVVG 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 875 DLALALVGAGVSADEFASDPARFGIPESVLGFLRGELGDPPGGWPEPLRT-------AALAGRGAARPTAQLAADDEIAL 947
Cdd:PRK12999 883 DMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKkvlkgeePITVRPGELLEPVDFEAERAELE 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 948 SSVG--AKRQATLNRLLFPSPTKEFNEHREAYGDTSQLSANQFFYGLRQGEEHRVKLERGVELLIGLEAISEPDERGMRT 1025
Cdd:PRK12999 963 EKLGreVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEPDEDGMRT 1042
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1026 VMCILNGQLRPVLVRDRSIASAVPAAEKADRGNPGHIAAPFA-GVVTVGVCVGERVGAGQTIATIEAMKMEAPITAPVAG 1104
Cdd:PRK12999 1043 VYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPgSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDG 1122
|
1130 1140
....*....|....*....|...
gi 622707843 1105 TVERVAVSDTAQVEGGDLLVVVS 1127
Cdd:PRK12999 1123 TVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-1126 |
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: 1942.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1 MFSKVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGDIGHPVHAYLSVDEIVATARRAGADAIY 80
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 81 PGYGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLMSS-APSASVDELLSVAAGMPFPLFVKA 159
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTeGPVDDLEEALAFAEEIGYPVMLKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 160 VAGGGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNLGDVIHLYERDCSVQRRHQKVI 239
Cdd:COG1038 163 AAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 240 ELAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDERGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAGE 319
Cdd:COG1038 243 EIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 320 TL--EQLGL-RQEDIAPHGAALQCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGST-NLGAEISPYFDSMLVKLTCR 395
Cdd:COG1038 323 SLddPEIGIpSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNaYTGAVITPYYDSLLVKVTAW 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 396 GRDLPTAVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFIDERPQLLTARASADRGTKILNFLADVTVNNP 475
Cdd:COG1038 403 GRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVNGP 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 476 YGSRPSTI--YPDDKLPDLDLRAAPPAGSKQRLVKLGPEGFARWLRESAAVGVTDTTFRDAHQSLLATRVRTSGLSRVAP 553
Cdd:COG1038 483 PGVKGRPKpdFPKPKLPKVDLGAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLKIAP 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 554 YLARTMPQLLSVECWGGATYDVALRFLKEDPWERLATLRAAMPNICLQMLLRGRNTVGYTPYPEIVTSAFVQEATATGID 633
Cdd:COG1038 563 ATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAAEAGID 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 634 IFRIFDALNNIESMRPAIDAVRETGsAIAEVAMCYTGDLTDPGEQLYTLDYYLKLAEQIVDAGAHVLAIKDMAGLLRPPA 713
Cdd:COG1038 643 VFRIFDSLNWVENMRVAIDAVRETG-KIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKDMAGLLKPYA 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 714 AQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAVDGAAAPLAGTTSQPALSSIVAAAAHTEYDTGLSLSAVC 793
Cdd:COG1038 722 AYKLVKALKEEVDLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLDLDALQ 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 794 ALEPYWEALRKVYAPFESGLPGPTGRVYHHEIPGGQLSNLRQQAIALGLGDRFEEIEEAYAGADRVLGRLVKVTPTSKVV 873
Cdd:COG1038 802 ELSNYWEAVRKYYAPFESGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTPSSKVV 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 874 GDLALALVGAGVSADEFASDPARFGIPESVLGFLRGELGDPPGGWPEPLRTA--ALAGRGAARPTAQLAADDEIALSSVG 951
Cdd:COG1038 882 GDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKvlKGRKPITVRPGELLPPVDFDALRAEL 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 952 AK-------RQATLNRLLFPSPTKEFNEHREAYGDTSQLSANQFFYGLRQGEEHRVKLERGVELLIGLEAISEPDERGMR 1024
Cdd:COG1038 962 EEklgrepsDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPDEDGMR 1041
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1025 TVMCILNGQLRPVLVRDRSIASAVPAAEKADRGNPGHIAAPFA-GVVTVGVCVGERVGAGQTIATIEAMKMEAPITAPVA 1103
Cdd:COG1038 1042 TVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPgTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRD 1121
|
1130 1140
....*....|....*....|...
gi 622707843 1104 GTVERVAVSDTAQVEGGDLLVVV 1126
Cdd:COG1038 1122 GTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
4-1126 |
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: 1252.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 4 KVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGDIGH--PVHAYLSVDEIVATARRAGADAIYP 81
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDlgPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 82 GYGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLMSS-APSASVDELLSVAAGMPFPLFVKAV 160
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTdGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 161 AGGGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNLGDVIHLYERDCSVQRRHQKVIE 240
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 241 LAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDERGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAGET 320
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 321 L--EQLGL-RQEDIAPHGAALQCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGSTNL-GAEISPYFDSMLVKLTCRG 396
Cdd:TIGR01235 321 LptPQLGVpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYaGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 397 RDLPTAVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFIDERPQLLTARASADRGTKILNFLADVTVNN-- 474
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNGhp 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 475 PYGSRPSTIYPDDKLPDLDLRAAP-PAGSKQRLVKLGPEGFARWLRESAAVGVTDTTFRDAHQSLLATRVRTSGLSRVAP 553
Cdd:TIGR01235 481 EAKDKLKPLENAPRVVVLYADQNPvPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIAP 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 554 YLARTMPQLLSVECWGGATYDVALRFLKEDPWERLATLRAAMPNICLQMLLRGRNTVGYTPYPEIVTSAFVQEATATGID 633
Cdd:TIGR01235 561 TTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGID 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 634 IFRIFDALNNIESMRPAIDAVRETGsAIAEVAMCYTGDLTDPGEQLYTLDYYLKLAEQIVDAGAHVLAIKDMAGLLRPPA 713
Cdd:TIGR01235 641 IFRVFDSLNWVENMRVGMDAVAEAG-KVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLLKPAA 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 714 AQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAVDGAAAPLAGTTSQPALSSIVAAAAHTEYDTGLSLSAVC 793
Cdd:TIGR01235 720 AKLLIKALREKTDLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVAWIR 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 794 ALEPYWEALRKVYAPFESGLPGPTGRVYHHEIPGGQLSNLRQQAIALGLGDRFEEIEEAYAGADRVLGRLVKVTPTSKVV 873
Cdd:TIGR01235 800 ELSAYWEAVRNLYAAFESDLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSSKVV 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 874 GDLALALVGAGVSADEFASDPARFGIPESVLGFLRGELGDPPGGWPEPLRTAA--LAGRGAARPTAQLAADDEIALSSVG 951
Cdd:TIGR01235 880 GDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVlkGEKPITVRPGSLLEPADLDAIRKDL 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 952 AKR-------QATLNRLLFPSPTKEFNEHREAYGDTSQLSANQFFYGLRQGEEHRVKLERGVELLIGLEAISEPDERGMR 1024
Cdd:TIGR01235 960 QEKherevsdFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQGER 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1025 TVMCILNGQLRPVLVRDRSIASAVPAAEKADRGNPGHIAAPFA-GVVTVGVCVGERVGAGQTIATIEAMKMEAPITAPVA 1103
Cdd:TIGR01235 1040 EVFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPgVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKD 1119
|
1130 1140
....*....|....*....|...
gi 622707843 1104 GTVERVAVSDTAQVEGGDLLVVV 1126
Cdd:TIGR01235 1120 GTIKEVLVKAGEQIDAKDLLLVL 1142
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-458 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 607.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1 MFSKVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGDiGHPVHAYLSVDEIVATARRAGADAIY 80
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGP-APAAESYLNIDAIIAAAKATGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 81 PGYGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLM-SSAPSASVDELLSVAAGMPFPLFVKA 159
Cdd:COG4770 80 PGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPgSDGPVQDAEEALAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 160 VA----------GgggrgmrrvgDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNLGDVIHLYERDC 229
Cdd:COG4770 160 SAggggkgmrvvR----------SEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDC 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 230 SVQRRHQKVIELAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDERGEYVFIEMNPRVQVEHTVTEEITDVDLV 309
Cdd:COG4770 230 SIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 310 ASQLRIAAGETleqLGLRQEDIAPHGAALQCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGSTNLGAEISPYFDSML 389
Cdd:COG4770 310 EEQIRIAAGEP---LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMI 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 622707843 390 VKLTCRGRDLPTAVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFIDERPQLLTARASAD 458
Cdd:COG4770 387 AKLIVWGPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-453 |
4.46e-180 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 536.10 E-value: 4.46e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1 MFSKVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGDiGHPVHAYLSVDEIVATARRAGADAIY 80
Cdd:PRK08654 1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGP-APPSKSYLNIERIIDVAKKAGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 81 PGYGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLM-SSAPSASVDELLSVAAGMPFPLFVKA 159
Cdd:PRK08654 80 PGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPgTEEGIEDIEEAKEIAEEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 160 VAGGGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNLGDVIHLYERDCSVQRRHQKVI 239
Cdd:PRK08654 160 SAGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 240 ELAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDErGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAGE 319
Cdd:PRK08654 240 EEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSN-GNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 320 TLEqlgLRQEDIAPHGAALQCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGSTNLGAEISPYFDSMLVKLTCRGRDL 399
Cdd:PRK08654 319 ELS---FKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 622707843 400 PTAVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFIDERPQLLTA 453
Cdd:PRK08654 396 EEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTILEE 449
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-447 |
6.64e-180 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 533.61 E-value: 6.64e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1 MFSKVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGDiGHPVHAYLSVDEIVATARRAGADAIY 80
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGP-APSKKSYLNIPAIISAAEITGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 81 PGYGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLMSSA-PSASVDELLSVAAGMPFPLFVKA 159
Cdd:PRK08591 80 PGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDgPVDDEEEALAIAKEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 160 VAGGGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNLGDVIHLYERDCSVQRRHQKVI 239
Cdd:PRK08591 160 TAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 240 ELAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDERGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAGe 319
Cdd:PRK08591 240 EEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAG- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 320 tlEQLGLRQEDIAPHGAALQCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGSTNLGAEISPYFDSMLVKLTCRGRDL 399
Cdd:PRK08591 319 --EPLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 622707843 400 PTAVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFIDER 447
Cdd:PRK08591 397 EEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-444 |
1.46e-163 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 491.46 E-value: 1.46e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1 MFSKVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGdiGHPV-HAYLSVDEIVATARRAGADAI 79
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIG--GPRVqESYLNLEKIIEIAKKTGAEAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 80 YPGYGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLM-SSAPSASVDELLSVAAGMPFPLFVK 158
Cdd:PRK06111 79 HPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPgITTNLEDAEEAIAIARQIGYPVMLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 159 AVAGGGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNLGDVIHLYERDCSVQRRHQKV 238
Cdd:PRK06111 159 ASAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 239 IELAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDERGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAG 318
Cdd:PRK06111 239 IEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 319 etlEQLGLRQEDIAPHGAALQCRITTEDPaNGFRPDTGRISALRTAGGAGVRLDGSTNLGAEISPYFDSMLVKLTCRGRD 398
Cdd:PRK06111 319 ---EKLSFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGET 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 622707843 399 LPTAVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFI 444
Cdd:PRK06111 395 REEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-451 |
9.09e-162 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 487.69 E-value: 9.09e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1 MFSKVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGDigHPVHAYLSVDEIVATARRAGADAIY 80
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGA--DPLAGYLNPRRLVNLAVETGCDALH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 81 PGYGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLMSSAPS-ASVDELLSVAAGMPFPLFVKA 159
Cdd:PRK07178 79 PGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNlADLDEALAEAERIGYPVMLKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 160 VAGGGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNLGDVIHLYERDCSVQRRHQKVI 239
Cdd:PRK07178 159 TSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 240 ELAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDERGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAGE 319
Cdd:PRK07178 239 EIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 320 TLEqlgLRQEDIAPHGAALQCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGSTNLGAEISPYFDSMLVKLTCRGRDL 399
Cdd:PRK07178 319 PLS---YKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTW 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 622707843 400 PTAVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFIDERPQLL 451
Cdd:PRK07178 396 EEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELT 447
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-446 |
4.96e-155 |
|
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: 469.24 E-value: 4.96e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1 MFSKVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGDiGHPVHAYLSVDEIVATARRAGADAIY 80
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGP-APSAKSYLNIPNIISAAEITGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 81 PGYGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLM-SSAPSASVDELLSVAAGMPFPLFVKA 159
Cdd:TIGR00514 80 PGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPgSDGLVEDEEENVRIAKRIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 160 VAGGGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNLGDVIHLYERDCSVQRRHQKVI 239
Cdd:TIGR00514 160 TAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 240 ELAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDERGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAGe 319
Cdd:TIGR00514 240 EEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAG- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 320 tlEQLGLRQEDIAPHGAALQCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGSTNLGAEISPYFDSMLVKLTCRGRDL 399
Cdd:TIGR00514 319 --EPLSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 622707843 400 PTAVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFIDE 446
Cdd:TIGR00514 397 EVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-447 |
3.89e-149 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 453.78 E-value: 3.89e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1 MFSKVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGDiGHPVHAYLSVDEIVATARRAGADAIY 80
Cdd:PRK05586 1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGP-ASSKDSYLNIQNIISATVLTGAQAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 81 PGYGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLM-SSAPSASVDELLSVAAGMPFPLFVKA 159
Cdd:PRK05586 80 PGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPgSEGEIENEEEALEIAKEIGYPVMVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 160 VAGGGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNLGDVIHLYERDCSVQRRHQKVI 239
Cdd:PRK05586 160 SAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 240 ELAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDERGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAGE 319
Cdd:PRK05586 240 EEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 320 TLEqlgLRQEDIAPHGAALQCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGSTNLGAEISPYFDSMLVKLTCRGRDL 399
Cdd:PRK05586 320 KLS---IKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 622707843 400 PTAVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFIDER 447
Cdd:PRK05586 397 EEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKK 444
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
4-460 |
8.88e-143 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 438.03 E-value: 8.88e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 4 KVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGdighPVHA---YLSVDEIVATARRAGADAIY 80
Cdd:PRK12833 7 KVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIG----PSHAaksYLNPAAILAAARQCGADAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 81 PGYGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLMSSAPS-ASVDELLSVAAGMPFPLFVKA 159
Cdd:PRK12833 83 PGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVvASLDAALEVAARIGYPLMIKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 160 VAGGGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNlGDVIHLYERDCSVQRRHQKVI 239
Cdd:PRK12833 163 AAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDG-ERVVHLFERECSLQRRRQKIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 240 ELAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLD-ERGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAG 318
Cdd:PRK12833 242 EEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 319 EtleQLGLRQEDIAPHGAALQCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGSTNLGAEISPYFDSMLVKLTCRGRD 398
Cdd:PRK12833 322 E---PLRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGED 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 622707843 399 LPTAVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFID----ERPQLLTARASADRG 460
Cdd:PRK12833 399 RAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEawlaEWRAALDAAASAAVG 464
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-451 |
6.56e-142 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 436.17 E-value: 6.56e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1 MFSKVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGDigHPVHAYLSVDEIVATARRAGADAIY 80
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGT--DPIKGYLDVKRIVEIAKACGADAIH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 81 PGYGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLMSSAP--SASVDELLSVAAGMPFPLFVK 158
Cdd:PRK08463 79 PGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKlnSESMEEIKIFARKIGYPVILK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 159 AVAGGGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNLGDVIHLYERDCSVQRRHQKV 238
Cdd:PRK08463 159 ASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 239 IELAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDERGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAG 318
Cdd:PRK08463 239 IEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 319 ETLEqlgLRQEDIAPHGAALQCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGSTNLGAEISPYFDSMLVKLTCRGRD 398
Cdd:PRK08463 319 EILD---LEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATS 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 622707843 399 LPTAVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFIDERPQLL 451
Cdd:PRK08463 396 YDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQEL 448
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
526-809 |
6.18e-138 |
|
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: 417.60 E-value: 6.18e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 526 VTDTTFRDAHQSLLATRVRTSGLSRVAPYLARTMpqLLSVECWGGATYDVALRFLKEDPWERLATLRAAMPNICLQMLLR 605
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 606 GRNTVGYTPYPEIVTSAFVQEATATGIDIFRIFDALNNIESMRPAIDAVRETGsAIAEVAMCYTGDltdpgeQLYTLDYY 685
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAG-KHVEGAICYTGS------PVHTLEYY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 686 LKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAVDGAAAPLAGT 765
Cdd:cd07937 152 VKLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVGLPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 622707843 766 TSQPALSSIVAAAAHTEYDTGLSLSAVCALEPYWEALRKVYAPF 809
Cdd:cd07937 232 TSQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
524-1126 |
4.41e-134 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 419.63 E-value: 4.41e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 524 VGVTDTTFRDAHQSLLATRVRT-------SGLSRVAPYlartmpqllSVECWGGATYDVALRFLKEDPWERLATLRAAMP 596
Cdd:PRK09282 4 VKITDTTLRDAHQSLLATRMRTedmlpiaEKLDKVGFW---------SLEVWGGATFDVCIRYLNEDPWERLRKLKKALP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 597 NICLQMLLRGRNTVGYTPYPEIVTSAFVQEATATGIDIFRIFDALNNIESMRPAIDAVRETGsAIAEVAMCYTgdlTDPg 676
Cdd:PRK09282 75 NTPLQMLLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAG-AHVQGTISYT---TSP- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 677 eqLYTLDYYLKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAVD 756
Cdd:PRK09282 150 --VHTIEKYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEVDLPVQLHSHCTSGLAPMTYLKAVEAGVDIID 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 757 GAAAPLAGTTSQPALSSIVAAAAHTEYDTGLSLSAVCALEPYWEALRKVYAPFESGLPGPTGRVYHHEIPGGQLSNLRQQ 836
Cdd:PRK09282 228 TAISPLAFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTIVDTRVLIHQVPGGMISNLVSQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 837 AIALGLGDRFEEI-EEayagADRV---LGRLVKVTPTSKVVGDLALALVGAGvsadefasdpARFG-IPESVLGFLRGEL 911
Cdd:PRK09282 308 LKEQNALDKLDEVlEE----IPRVredLGYPPLVTPTSQIVGTQAVLNVLTG----------ERYKvITKEVKDYVKGLY 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 912 GDPPGGWPEPLRTaalAGRGAARPTAQLAAD-------------DEIALSsvgaKRQATLNRLLFPSPTKEFNEHREAYG 978
Cdd:PRK09282 374 GRPPAPINEELRK---KIIGDEEPITCRPADllepelekarkeaEELGKS----EKEDVLTYALFPQIAKKFLEEREAGE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 979 DTSQLSANQFFYGLRQGEEHRVKLE-RGVELLIGLEAISEPderGMRTVMCILNGQLRPVLVrdrSIASAVPAAEKADRG 1057
Cdd:PRK09282 447 LKPEPEPKEAAAAGAEGIPTEFKVEvDGEKYEVKIEGVKAE---GKRPFYLRVDGMPEEVVV---EPLKEIVVGGRPRAS 520
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1058 NPGHIAAPFA-GVVTVGVCVGERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLLVVV 1126
Cdd:PRK09282 521 APGAVTSPMPgTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
3-446 |
1.09e-128 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 400.27 E-value: 1.09e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 3 SKVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGDiGHPVHAYLSVDEIVATARRAGADAIYPG 82
Cdd:PRK08462 5 KRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGG-AKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 83 YGFLSENPDLAAACAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLMSSAPS-ASVDELLSVAAGMPFPLFVKAVA 161
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGAlKSYEEAKKIAKEIGYPVILKAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 162 GGGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVYLEQAVINPRHIEVQILADNLGDVIHLYERDCSVQRRHQKVIEL 241
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 242 APAPHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDERGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAGETL 321
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 322 eqlgLRQEDIAPHGAALQCRITTEDPaNGFRPDTGRISALRTAGGAGVRLDGSTNLGAEISPYFDSMLVKLTCRGRDLPT 401
Cdd:PRK08462 324 ----PSQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 622707843 402 AVSRARRAIAEFRIRGVSTNIPFLQAVLDDPDFRAGRVTTSFIDE 446
Cdd:PRK08462 399 AIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
524-916 |
1.16e-126 |
|
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: 398.11 E-value: 1.16e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 524 VGVTDTTFRDAHQSLLATRVRTSGLSRVAPYLARTmpQLLSVECWGGATYDVALRFLKEDPWERLATLRAAMPNICLQML 603
Cdd:COG5016 4 VKITDTTLRDGHQSLFATRMRTEDMLPIAEKLDEA--GFWSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 604 LRGRNTVGYTPYPEIVTSAFVQEATATGIDIFRIFDALNNIESMRPAIDAVRETGsAIAEVAMCYTgdlTDPgeqLYTLD 683
Cdd:COG5016 82 LRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAG-AHAQGAISYT---ISP---VHTVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 684 YYLKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAVDGAAAPLA 763
Cdd:COG5016 155 YYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEALDIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 764 GTTSQPALSSIVAAAAHTEYDTGLSLSAVCALEPYWEALRKVYAPFESGLPGPTGRVYHHEIPGGQLSNLRQQAIALGLG 843
Cdd:COG5016 235 GGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGVDPRVLVHQVPGGMLSNLVSQLKEQGAL 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 622707843 844 DRFEEIEEAYAgadRV---LGRLVKVTPTSKVVGDLALALVGAGvsadefasdpARFG-IPESVLGFLRGELGDPPG 916
Cdd:COG5016 315 DRLDEVLEEIP---RVredLGYPPLVTPTSQIVGTQAVLNVLTG----------ERYKmITKEVKDYVLGYYGKTPA 378
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
526-1123 |
6.86e-117 |
|
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: 373.74 E-value: 6.86e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 526 VTDTTFRDAHQSLLATRVRTSGLSRVAPYLARTmpQLLSVECWGGATYDVALRFLKEDPWERLATLRAAMPNICLQMLLR 605
Cdd:TIGR01108 1 ITDVVLRDAHQSLFATRMRTEDMLPIAEKLDDV--GYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 606 GRNTVGYTPYPEIVTSAFVQEATATGIDIFRIFDALNNIESMRPAIDAVRETGsAIAEVAMCYTgdlTDPgeqLYTLDYY 685
Cdd:TIGR01108 79 GQNLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHG-AHAQGTISYT---TSP---VHTLETY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 686 LKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAVDGAAAPLAGT 765
Cdd:TIGR01108 152 LDLAEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRFGLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 766 TSQPALSSIVAAAAHTEYDTGLSLSAVCALEPYWEALRKVYAPFESGLPGPTGRVYHHEIPGGQLSNLRQQAIALGLGDR 845
Cdd:TIGR01108 232 TSHPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFEGQLKGPDSRILVAQVPGGMLSNLESQLKEQNALDK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 846 FEEIEEAYAGADRVLGRLVKVTPTSKVVGDLALALVGAGvsadefasdpARFG-IPESVLGFLRGELGDPPGGWPEPLRT 924
Cdd:TIGR01108 312 LDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTG----------ERYKtITKETKGYLKGEYGRTPAPINAELQR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 925 ---AALAGRGAARPTAQLAadDEIALSSVGAKRQATLNR--------LLFPSPTKEFNEHREAYGDTSQLSANQffyglR 993
Cdd:TIGR01108 382 kilGDEKPIVDCRPADLLE--PELDKLRAEVREAGAEKNsiedvltyALFPQVGLKFLENRHNPAAFEPKPEEK-----V 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 994 QGEEHRVKLERGVelligleaisEPDERGMRTVmcILNGQLRPVLV---RDRS-IASAVPAA-----EKADRGNPGHIAA 1064
Cdd:TIGR01108 455 IEQEHAQVVGKYE----------ETHASGSYTV--EVEGKAFVVKVspgGDVSqITASAPANtsggtVAAKAGAGTPVTA 522
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1065 PFA-GVVTVGVCVGERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLL 1123
Cdd:TIGR01108 523 PIAgSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREILVKVGDAVSVGQVL 582
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
521-1124 |
6.38e-92 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 306.86 E-value: 6.38e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 521 SAAVGVTDTTFRDAHQSLLATRVRTSGLSRVAPYLARTmpQLLSVECWGGATYDVALRFLKEDPWERLATLRAAMPNICL 600
Cdd:PRK14040 2 SKPLAITDVVLRDAHQSLFATRLRLDDMLPIAAKLDKV--GYWSLESWGGATFDACIRFLGEDPWERLRELKKAMPNTPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 601 QMLLRGRNTVGYTPYPEIVTSAFVQEATATGIDIFRIFDALNNIESMRPAIDAVRETGsAIAEVAMCYTgdlTDPgeqLY 680
Cdd:PRK14040 80 QMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVG-AHAQGTLSYT---TSP---VH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 681 TLDYYLKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAVDGAAA 760
Cdd:PRK14040 153 TLQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRVDVPLHLHCHATTGLSTATLLKAIEAGIDGVDTAIS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 761 PLAGTTSQPALSSIVAAAAHTEYDTGLSLSAVCALEPYWEALRKVYAPFESGLPGPTGRVYHHEIPGGQLSNLRQQAIAL 840
Cdd:PRK14040 233 SMSMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNMESQLKEQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 841 GLGDRFEEIEEAYAgadRV---LGRLVKVTPTSKVVGDLALALVGAGvsadefasdpARFG-IPESVLGFLRGELGDPP- 915
Cdd:PRK14040 313 GAADKLDEVLAEIP---RVredLGFIPLVTPTSQIVGTQAVLNVLTG----------ERYKtITKETAGVLKGEYGATPa 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 916 ------------GGWPEPLRTAALAGRGAARPTAQL---AADDEIALSSvgAKRQATLNRLLFPSPTKEFNEHReayGDT 980
Cdd:PRK14040 380 pvnaelqarvleGAEPITCRPADLLAPELDKLEAELrrqAQEKGITLAE--NAIDDVLTYALFPQIGLKFLENR---HNP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 981 SqlsanqFFYGLRQGEEHRVKlergvelligleAISEPDERGMRTVMciLNGQLRPVLVRD----------RSIASAVPA 1050
Cdd:PRK14040 455 A------AFEPVPQAEAAQPA------------AKAEPAGSETYTVE--VEGKAYVVKVSEggdisqitpaAPAAAPAAA 514
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 622707843 1051 AEKADRGNPGH-IAAPFA-GVVTVGVCVGERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLLV 1124
Cdd:PRK14040 515 AAAAPAAAAGEpVTAPLAgNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLL 590
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
524-915 |
1.13e-91 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 301.62 E-value: 1.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 524 VGVTDTTFRDAHQSLLATRVRTSglsRVAPyLARTMPQL--LSVECWGGATYDVALRFLKEDPWERLATLRAAMPNICLQ 601
Cdd:PRK12331 4 IKITETVLRDGQQSLIATRMTTE---EMLP-ILEKLDNAgyHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 602 MLLRGRNTVGYTPYPEIVTSAFVQEATATGIDIFRIFDALNNIESMRPAIDAVRETGsAIAEVAMCYTgdlTDPgeqLYT 681
Cdd:PRK12331 80 MLLRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAG-GHAQVAISYT---TSP---VHT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 682 LDYYLKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAVDGAAAP 761
Cdd:PRK12331 153 IDYFVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAVTVPLEVHTHATSGIAEMTYLKAIEAGADIIDTAISP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 762 LAGTTSQPALSSIVAAAAHTEYDTGLSLSAVCALEPYWEALRKVYapFESGLPGPT-----GRVYHHEIPGGQLSNLRQQ 836
Cdd:PRK12331 233 FAGGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHY--REEGILNPKvkdvePKTLIYQVPGGMLSNLLSQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 837 AIALGLGDRFEEIEEAYAGADRVLGRLVKVTPTSKVVGDLALALVGAGvsadefasdpARFG-IPESVLGFLRGELGDPP 915
Cdd:PRK12331 311 LKEQGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQALMNVISG----------ERYKmVPNEIKDYVRGLYGRPP 380
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
526-874 |
3.61e-83 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 278.98 E-value: 3.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 526 VTDTTFRDAHQSLLATRVRTSGLsrvAPYLaRTMPQL--LSVECWGGATYDVALRFLKEDPWERLATLRAAMPNICLQML 603
Cdd:PRK14041 5 FVDTTLRDGHQSLIATRMRTEDM---LPAL-EAFDRMgfYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 604 LRGRNTVGYTPYPEIVTSAFVQEATATGIDIFRIFDALNNIESMRPAIDAVRETGSAIaEVAMCYTgdlTDPgeqLYTLD 683
Cdd:PRK14041 81 LRGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHV-QGAISYT---VSP---VHTLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 684 YYLKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAVDGAAAPLA 763
Cdd:PRK14041 154 YYLEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKFGVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPFS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 764 GTTSQPALSSIVAAAAHTEYDTGLSLSAVCALEPYWEALRKVYAPFESGLPGPTGRVYHHEIPGGQLSNLRQQAIALGLG 843
Cdd:PRK14041 234 MGTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYDVGMKSPDSRILVSQIPGGMYSNLVKQLKEQKML 313
|
330 340 350
....*....|....*....|....*....|.
gi 622707843 844 DRFEEIEEAYAGADRVLGRLVKVTPTSKVVG 874
Cdd:PRK14041 314 HKLDKVLEEVPRVRKDLGYPPLVTPTSQIVG 344
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
526-1126 |
4.16e-82 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 280.07 E-value: 4.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 526 VTDTTFRDAHQSLLATRVRTSGLSRVAPYLARTmpQLLSVECWGGATYDVALRFLKEDPWERLATLRAAMPNICLQMLLR 605
Cdd:PRK14042 6 ITDVTLRDAHQCLIATRMRTEDMLPICNKMDDV--GFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSMLLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 606 GRNTVGYTPYPEIVTSAFVQEATATGIDIFRIFDALNNIESMRPAIDAVReTGSAIAEVAMCYTgdlTDPgeqLYTLDYY 685
Cdd:PRK14042 84 GQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIK-SHKKHAQGAICYT---TSP---VHTLDNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 686 LKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAVDGAAAPLAGT 765
Cdd:PRK14042 157 LELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLKQATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFSGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 766 TSQPALSSIVAAAAHTEYDTGLSLSAVCALEPYWEALRKVYAPFESGLPGPTGRVYHHEIPGGQLSNLRQQAIALGLGDR 845
Cdd:PRK14042 237 ASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLYQVPGGMISNLYNQLKEQNALDK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 846 FEEIEEAYAGADRVLGRLVKVTPTSKVVGDLALALVgagVSADEFASdparfgIPESVLGFLRGELGDPPGGWPEPLRTA 925
Cdd:PRK14042 317 MDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQAVINV---LTGERYKT------ITNEVKLYCQGKYGTPPGKISSALRKK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 926 A--LAGRGAARPTAQLAAD-DEIA--LSSVGAKRQATLNRLLFPSPTKEFNEHRE-------------AYGDTSQLSAnq 987
Cdd:PRK14042 388 AigRTEVIEVRPGDLLPNElDQLQneISDLALSDEDVLLYAMFPEIGRQFLEQRKnnqlipeplltqsSAPDNSVMSE-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 988 fFYGLRQGEEHRVKLErGVELLigleaisepdERGMRTVMCILNGQLRPVLVRDRSIASAVPAAEKADRGNPGHIAAPF- 1066
Cdd:PRK14042 466 -FDIILHGESYHVKVA-GYGMI----------EHGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIp 533
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1067 AGVVTVGVCVGERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLLVVV 1126
Cdd:PRK14042 534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRV 593
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
524-891 |
1.11e-75 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 258.92 E-value: 1.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 524 VGVTDTTFRDAHQSLLATRVrtsGLSRVAPYLART-MPQLLSVECWGGATYDVALRFLKEDPWERLATLRAAMPNICLQM 602
Cdd:PRK12330 5 IGVTELALRDAHQSLMATRM---AMEDMVGACEDIdNAGYWSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 603 LLRGRNTVGYTPYPEIVTSAFVQEATATGIDIFRIFDALNNIESMRPAIDAVRETGSAiAEVAMCYTgdlTDPgeqLYTL 682
Cdd:PRK12330 82 LLRGQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKH-AQGTICYT---VSP---IHTV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 683 DYYLKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRF--DLPVHLHTHDTPGGQLASYVAAWHAGADAVDGAAA 760
Cdd:PRK12330 155 EGFVEQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgeDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAIS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 761 PLAGTTSQPALSSIVAAAAHTEYDTGLSLSAVCALEPYWEALRKVYAPFESGLPGPTGRVYHHEIPGGQLSNLRQQAIAL 840
Cdd:PRK12330 235 SMSLGPGHNPTESLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTTGVETEIFKSQIPGGMLSNMESQLKQQ 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 622707843 841 GLGDRFEEIEEAYAGADRVLGRLVKVTPTSKVVGDLALALVGAG---VSADEFA 891
Cdd:PRK12330 315 GAGDRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQAVFNVLMGrykVLTGEFA 368
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
820-1010 |
1.95e-72 |
|
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: 239.28 E-value: 1.95e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 820 VYHHEIPGGQLSNLRQQAIALGLGDRFEEIEEAYAGADRVLGRLVKVTPTSKVVGDLALALVGAGVSADEFASDPARFGI 899
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 900 PESVLGFLRGELGDPPGGWPEPLRTA--ALAGRGAARPTAQLAADD------EIA-LSSVGAKRQATLNRLLFPSPTKEF 970
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKvlKGEEPITCRPGDLLPPVDleklrkELEeKAGRETTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 622707843 971 NEHREAYGDTSQLSANQFFYGLRQGEEHRVKLERGVELLI 1010
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIV 200
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
524-985 |
1.85e-71 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 246.18 E-value: 1.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 524 VGVTDTTFRDAHQSLLATRVRTSGLSRVAPYLARTmpQLLSVECWGGATYDVALRFLKEDPWERLATLRAAMPNICLQML 603
Cdd:PRK12581 13 VAITETVLRDGHQSLMATRLSIEDMLPVLTILDKI--GYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRLQML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 604 LRGRNTVGYTPYPEIVTSAFVQEATATGIDIFRIFDALNNIESMRPAIDAVRETGSAiAEVAMCYTgdlTDPgeqLYTLD 683
Cdd:PRK12581 91 LRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKE-AQLCIAYT---TSP---VHTLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 684 YYLKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAVDGAAAPLA 763
Cdd:PRK12581 164 YYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIKAMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALSPFS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 764 GTTSQPALSSIVAAAAHTEYDTGLSLSAVCALEPYWEALRKVY---APFESGLPGPTGRVYHHEIPGGQLSNLRQQAIAL 840
Cdd:PRK12581 244 EGTSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYladGILDPSLLFPDPRTLQYQVPGGMLSNMLSQLKQA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 841 GLGDRFEEIEEAYAGADRVLGRLVKVTPTSKVVGDLALALVGAGvsadefasDPARFgIPESVLGFLRGELGDPPGGWPE 920
Cdd:PRK12581 324 NAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNVILG--------KPYQM-VSKEIKQYLAGDYGKTPAPVNE 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 921 PLRTAA--LAGRGAARPTAQLAADDEI---ALSSVGAKRQATLNRLLFPSPTKEFNEHREAYGDTSQLSA 985
Cdd:PRK12581 395 DLKRSQigSAPVTTNRPADQLSPEFEVlkaEVADLAQTDEDVLTYALFPSVAKPFLTTKYQTDDVIKVTA 464
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
117-322 |
5.81e-64 |
|
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: 215.63 E-value: 5.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 117 KSRAIAAAREAGLPVLMSSA-PSASVDELLSVAAGMPFPLFVKAVAGGGGRGMRRVGDIAALPEAIEAASREAESAFGDP 195
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAgPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 196 TVYLEQAVINPRHIEVQILADNLGDVIHLYERDCSVQRRHQKVIELAPAPHLDAELRYKMCVDAVAFARHIGYSCAGTVE 275
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 622707843 276 FLLDER-GEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAGETLE 322
Cdd:pfam02786 162 FALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
527-800 |
3.59e-52 |
|
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: 184.20 E-value: 3.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 527 TDTTFRDAHQSLLATRvRTSGLSRVAPYLARTMpqLLSVECWGGATYDVAlrFLKEDPWERLATLRAAMPNICLQMLLRG 606
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDEAG--VDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 607 RNtvgytpypeivtsAFVQEATATGIDIFRIFDALN--------------NIESMRPAIDAVRETGsAIAEVAMCYTGDL 672
Cdd:cd03174 76 RE-------------KGIERALEAGVDEVRIFDSASethsrknlnksreeDLENAEEAIEAAKEAG-LEVEGSLEDAFGC 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 673 tdpgeqLYTLDYYLKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRF-DLPVHLHTHDTPGGQLASYVAAWHAG 751
Cdd:cd03174 142 ------KTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALpDVPLGLHTHNTLGLAVANSLAALEAG 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 622707843 752 ADAVDGAAAPLAGTTSQPALSSIVAAAAHTEYDTGLSLSAVCALEPYWE 800
Cdd:cd03174 216 ADRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVE 264
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
339-445 |
3.03e-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: 172.60 E-value: 3.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 339 QCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGSTNLGAEISPYFDSMLVKLTCRGRDLPTAVSRARRAIAEFRIRGV 418
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|....*..
gi 622707843 419 STNIPFLQAVLDDPDFRAGRVTTSFID 445
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
339-446 |
6.02e-47 |
|
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: 163.05 E-value: 6.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 339 QCRITTEDPANGFRPDTGRISALRTAGGAGVRLDGSTNLGAEISPYFDSMLVKLTCRGRDLPTAVSRARRAIAEFRIRGV 418
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100
....*....|....*....|....*...
gi 622707843 419 STNIPFLQAVLDDPDFRAGRVTTSFIDE 446
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
2-110 |
1.59e-45 |
|
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: 159.19 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 2 FSKVLVANRGEIAIRAFRAAYELGVGTVAVYPYEDRNSQHRLKADESYQIGDiGHPVHAYLSVDEIVATARRAGADAIYP 81
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGP-GPASESYLNIDAIIDAAKETGADAIHP 79
|
90 100
....*....|....*....|....*....
gi 622707843 82 GYGFLSENPDLAAACAAAGISFVGPSAEV 110
Cdd:pfam00289 80 GYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
105-319 |
8.15e-43 |
|
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: 157.34 E-value: 8.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 105 GPSAEVLELAGNKSRAIAAAREAGLPVLmSSAPSASVDELLSVAAGMPFPLFVKAVAGGGGRGMRRVGDIAALPEAIEAA 184
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVP-GFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 185 SREAESAFGDPTVYLEQAVINpRHIEVQILADNlGDVIHlyerdCSVQRRHQK---VIEL---APAPhLDAELRYKMCVD 258
Cdd:COG0439 122 RAEAKAGSPNGEVLVEEFLEG-REYSVEGLVRD-GEVVV-----CSITRKHQKppyFVELgheAPSP-LPEELRAEIGEL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 622707843 259 AVAFARHIGYS-CAGTVEFLLDERGEYVFIEMNPRVQVEH--TVTEEITDVDLVASQLRIAAGE 319
Cdd:COG0439 194 VARALRALGYRrGAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGE 257
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
523-796 |
6.76e-19 |
|
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: 87.78 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 523 AVGVTDTTFRDAHQSLlATRVRTSGLSRVAPYLARtmpqllsvecWGGATYDVALRFLKEDPWERLATLRAAMPNICLQM 602
Cdd:pfam00682 1 AVAICDTTLRDGEQAL-GVAFSIDEKLAIARALDA----------AGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 603 LLRGRntvgytpypEIVTSAFVQEATATGIDIFRIFDALNNIE-------SMRPAIDAVRETGSAIAEVAMCYTGDLTDP 675
Cdd:pfam00682 70 LCRAR---------EHDIKAAVEALKGAGAVRVHVFIATSDLHrkyklgkDREEVAKRAVAAVKAARSRGIDVEFSPEDA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 676 GEQlyTLDYYLKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFD--LPVHLHTHDTPGGQLASYVAAWHAGAD 753
Cdd:pfam00682 141 SRT--DPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPnkAIISVHCHNDLGMAVANSLAAVEAGAD 218
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 622707843 754 AVDGAAAPLAGTTSQPALSSIVAAAAHTEYDTGLSLSAVCALE 796
Cdd:pfam00682 219 RVDGTVNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIA 261
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1078-1126 |
3.43e-18 |
|
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: 79.77 E-value: 3.43e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 622707843 1078 ERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLLVVV 1126
Cdd:cd06850 19 DKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1045-1126 |
1.32e-12 |
|
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: 66.07 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 1045 ASAVPAAEKADRGNPGHIAAP----FAGVVTVGVCVG----ERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQ 1116
Cdd:COG0511 46 AAPAAAAAAAAASGGGAVKSPmvgtFYRAPSPGAKPFvkvgDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQP 125
|
90
....*....|
gi 622707843 1117 VEGGDLLVVV 1126
Cdd:COG0511 126 VEYGQPLFVI 135
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1078-1126 |
9.50e-12 |
|
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: 61.46 E-value: 9.50e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 622707843 1078 ERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLLVVV 1126
Cdd:pfam00364 25 DKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
14-293 |
2.02e-10 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 64.18 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 14 AIRAFraaYELGVGTVAVYPYED---RNSQHrlkADESYQIGDIGHPVHAYlsVDEIVATARRAGADAIYPGY----GFL 86
Cdd:COG3919 20 VARSL---GEAGVRVIVVDRDPLgpaARSRY---VDEVVVVPDPGDDPEAF--VDALLELAERHGPDVLIPTGdeyvELL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 87 SENPDlaaaCAAAGISFVGPSAEVLELAGNKSRAIAAAREAGLPVLMSSAPSaSVDELLSVAAGMPFPLFVKAV----AG 162
Cdd:COG3919 92 SRHRD----ELEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLD-SADDLDALAEDLGFPVVVKPAdsvgYD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 163 GGGRGMRRVGDIAALPEAIEAASREAESAFGDPTVyleQAVI---NPRHIEVQILADNLGDVIHLyerdCSVQRRHQK-- 237
Cdd:COG3919 167 ELSFPGKKKVFYVDDREELLALLRRIAAAGYELIV---QEYIpgdDGEMRGLTAYVDRDGEVVAT----FTGRKLRHYpp 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 622707843 238 ------VIELAPAPhldaelryKMCVDAVAFARHIGYSCAGTVEFLLDER-GEYVFIEMNPRV 293
Cdd:COG3919 240 aggnsaARESVDDP--------ELEEAARRLLEALGYHGFANVEFKRDPRdGEYKLIEINPRF 294
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1078-1124 |
5.70e-08 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 50.56 E-value: 5.70e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 622707843 1078 ERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLLV 1124
Cdd:PRK08225 21 DTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLL 67
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
100-291 |
2.82e-07 |
|
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: 53.57 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 100 GISFVGPSAEVLELAGNKSRAIAAAREAGLPVlmssAPSASVD-----ELLSVAAGMPFPLFVKA-----------Vagg 163
Cdd:COG1181 79 GIPYTGSGVLASALAMDKALTKRVLAAAGLPT----PPYVVLRrgelaDLEAIEEELGLPLFVKParegssvgvskV--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 164 ggrgmrrvGDIAALPEAIEAASREaesafgDPTVYLEQAvINPRHIEVQILADnlGDVIHL-----------------YE 226
Cdd:COG1181 152 --------KNAEELAAALEEAFKY------DDKVLVEEF-IDGREVTVGVLGN--GGPRALppieivpengfydyeakYT 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 622707843 227 RDcsvqrrhqKVIELAPAPhLDAELRYKMCVDAVAFARHIGysCAGT--VEFLLDERGEYVFIEMNP 291
Cdd:COG1181 215 DG--------GTEYICPAR-LPEELEERIQELALKAFRALG--CRGYarVDFRLDEDGEPYLLEVNT 270
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1078-1127 |
3.50e-07 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 48.65 E-value: 3.50e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 622707843 1078 ERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLLVVVS 1127
Cdd:PRK05889 22 DQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVIS 71
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1078-1126 |
1.03e-06 |
|
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: 47.44 E-value: 1.03e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 622707843 1078 ERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLLVVV 1126
Cdd:cd06663 25 DKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
1078-1126 |
3.16e-05 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 43.46 E-value: 3.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 622707843 1078 ERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLLVVV 1126
Cdd:PRK07051 30 DAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
45-292 |
3.81e-05 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 47.19 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 45 ADESYQIGDIGHPvhAYLsvDEIVATARRAGADAIYPGY----GFLSENPDlaaACAAAGISFVGPSAEVLELAGNKSRA 120
Cdd:PRK12767 43 ADKFYVVPKVTDP--NYI--DRLLDICKKEKIDLLIPLIdpelPLLAQNRD---RFEEIGVKVLVSSKEVIEICNDKWLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 121 IAAAREAGLPVlmssAPSASVDELLSVAAG-----MPFPLFVKAVAGGGGRGMRRVGDIAALPEAIEAASreaesafgDP 195
Cdd:PRK12767 116 YEFLKENGIPT----PKSYLPESLEDFKAAlakgeLQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVP--------NL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 196 TVyleQAVINPRHIEVQILADNLGDVIHlyerdcSVQRRHQKVI----ELAPAPHlDAELRyKMCVDAVAFARHIGYSca 271
Cdd:PRK12767 184 II---QEFIEGQEYTVDVLCDLNGEVIS------IVPRKRIEVRagetSKGVTVK-DPELF-KLAERLAEALGARGPL-- 250
|
250 260
....*....|....*....|.
gi 622707843 272 gTVEFLLDErGEYVFIEMNPR 292
Cdd:PRK12767 251 -NIQCFVTD-GEPYLFEINPR 269
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
100-334 |
5.01e-05 |
|
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: 47.69 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 100 GISFVGPSAEVLELAGNKSRAIAAAREAGLPVLMSSAPSaSVDELLSVAAGMPFPLFVKAVAGGGGRGMRRVGDIAALPE 179
Cdd:TIGR01369 653 GVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTAT-SVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRR 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 180 AIEAASREAESAfgdPTV---YLEQAVinprHIEVQILADNLGDVIH-LYErdcsvqrrHqkvIELA-----------PA 244
Cdd:TIGR01369 732 YLEEAVAVSPEH---PVLidkYLEDAV----EVDVDAVSDGEEVLIPgIME--------H---IEEAgvhsgdstcvlPP 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 245 PHLDAELRYKMCVDAVAFARHIGYSCAGTVEFLLDERGEYVfIEMNPRVQVEHTVTEEITDVDLVASQLRIAAGETLEQL 324
Cdd:TIGR01369 794 QTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYV-IEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEEL 872
|
250
....*....|
gi 622707843 325 GLRQEDIAPH 334
Cdd:TIGR01369 873 GVGKEKEPKY 882
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
682-747 |
6.21e-05 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 46.86 E-value: 6.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 622707843 682 LDYYLKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAA 747
Cdd:PRK09389 142 LDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSELVKGPVSIHCHNDFGLAVANTLAA 207
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1078-1124 |
1.27e-04 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 43.70 E-value: 1.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 622707843 1078 ERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLLV 1124
Cdd:PRK05641 104 QQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLI 150
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
686-748 |
1.81e-04 |
|
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: 44.69 E-value: 1.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 622707843 686 LKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRF-DLPVHLHTHDTPGGQLASYVAAW 748
Cdd:cd07938 152 AEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERFpDEKLALHFHDTRGQALANILAAL 215
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
111-324 |
6.73e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 44.00 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 111 LELAGNKSRAIAAA------REAGLPVLMSSAPSA---SVDELLSVAAGM-PFPLFVKAvaggGGRGMRRVGDIAALPEA 180
Cdd:PLN02735 129 VELIGAKLDAIKKAedrelfKQAMEKIGLKTPPSGiatTLDECFEIAEDIgEFPLIIRP----AFTLGGTGGGIAYNKEE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 181 IEAASREAESAFGDPTVYLEQAVINPRHIEVQI---LADNLgdVIhlyerDCSVQR------RHQKVIELAPAPHL-DAE 250
Cdd:PLN02735 205 FETICKAGLAASITSQVLVEKSLLGWKEYELEVmrdLADNV--VI-----ICSIENidpmgvHTGDSITVAPAQTLtDKE 277
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 622707843 251 lrYKMCVDA-VAFARHIGYSCAGT-VEFLLD-ERGEYVFIEMNPRVQVEHTVTEEITDVDLVASQLRIAAGETLEQL 324
Cdd:PLN02735 278 --YQRLRDYsVAIIREIGVECGGSnVQFAVNpVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTLDQI 352
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
127-291 |
7.07e-04 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 42.30 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 127 AGLPV------LMSSAPSASVDELLSVAAGMPFPLFVKAVAGGGGRGMRRVGDIAALPEAIEAASREaesafgDPTVYLE 200
Cdd:pfam07478 5 AGLPVvpfvtfTRADWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQY------DEKVLVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 201 QAvINPRHIEVQILADNLGDVIHLYER--DCSVQRRHQKVIE-----LAPApHLDAELRYKmcVDAVAFARHIGYSCAGT 273
Cdd:pfam07478 79 EG-IEGREIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDdsaqiVVPA-DLEEEQEEQ--IQELALKAYKALGCRGL 154
|
170 180
....*....|....*....|
gi 622707843 274 --VEFLLDERGEYVFIEMNP 291
Cdd:pfam07478 155 arVDFFLTEDGEIVLNEVNT 174
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
682-795 |
1.25e-03 |
|
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) of Streptomyces rubellomurinus catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate and CoA, a reaction similar to one catalyzed by homocitrate synthase. The gene encoding FrbC is one of several genes required for the biosynthesis of FR900098, a potent antimalarial antibiotic. This protein is also required for assembly of the nitrogenase MoFe complex but its exact role is unknown. This family also includes the NifV proteins of Heliobacterium chlorum and Gluconacetobacter diazotrophicus, which appear to be orthologous to FrbC. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163677 [Multi-domain] Cd Length: 259 Bit Score: 42.11 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 682 LDYYLKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFDLPVHLHTHDTPGGQLASYVAAWHAGADAvdgaaap 761
Cdd:cd07939 138 PDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAATDLPLEFHAHNDLGLATANTLAAVRAGATH------- 210
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 622707843 762 lAGTT--------SQPALSSIVAAAAHTE-YDTGLSLSAVCAL 795
Cdd:cd07939 211 -VSVTvnglgeraGNAALEEVVMALKHLYgRDTGIDTTRLPEL 252
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
100-291 |
1.36e-03 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 42.42 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 100 GISFVGPSAEVLELAGNKSRAIAAAREAGLPVlmssAPSASVDE-------LLSVAAGMPFPLFVKA-----------Va 161
Cdd:PRK01966 107 GIPYVGCGVLASALSMDKILTKRLLAAAGIPV----APYVVLTRgdweeasLAEIEAKLGLPVFVKPanlgssvgiskV- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 622707843 162 ggggrgmrrvGDIAALPEAIEAASREaesafgDPTVYLEQAvINPRHIEVQILADN-----LGDVIHL-----YER---D 228
Cdd:PRK01966 182 ----------KNEEELAAALDLAFEY------DRKVLVEQG-IKGREIECAVLGNDpkasvPGEIVKPddfydYEAkylD 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 622707843 229 CSVQrrhqkviELAPAPhLDAELR----------YKMcVDAVAFARhigyscagtVEFLLDERGEYVFIEMNP 291
Cdd:PRK01966 245 GSAE-------LIIPAD-LSEELTekirelaikaFKA-LGCSGLAR---------VDFFLTEDGEIYLNEINT 299
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1078-1126 |
1.37e-03 |
|
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: 38.51 E-value: 1.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 622707843 1078 ERVGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLLVVV 1126
Cdd:COG0508 28 DTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1080-1127 |
2.62e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 39.02 E-value: 2.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 622707843 1080 VGAGQTIATIEAMKMEAPITAPVAGTVERVAVSDTAQVEGGDLLVVVS 1127
Cdd:PRK06549 83 VTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITIG 130
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
682-735 |
8.14e-03 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 39.77 E-value: 8.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 622707843 682 LDYYLKLAEQIVDAGAHVLAIKDMAGLLRPPAAQRLVSALRSRFDLPVHLHTHD 735
Cdd:PRK11858 144 LDFLIEFAKAAEEAGADRVRFCDTVGILDPFTMYELVKELVEAVDIPIEVHCHN 197
|
|
| |
