|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
29-1178 |
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: 1903.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 29 IKKLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVGAGKSPVGAYLDIDSIIQIAKENNIDAIHP 108
Cdd:COG1038 4 IKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDAIHP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 109 GYGFLSENVGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGTDGPVHTLEEARAFIDSgVGYPVIIKA 188
Cdd:COG1038 84 GYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEE-IGYPVMLKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 189 SMGGGGRGMRVVNRAEDLEENFERASSEALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVVHLYHRDCSVQRRHQKVL 268
Cdd:COG1038 163 AAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 269 ETAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAGGE 348
Cdd:COG1038 243 EIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 349 TF--KDLGL-SQDKIKPRGHAMQCRVTTENPSTGFQPDSGVIEVFRSPGGMGIRLDDGPGFVGAHITPHYDSLLVKVTAR 425
Cdd:COG1038 323 SLddPEIGIpSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDSLLVKVTAW 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 426 ALDRGDCAHKLKRALSEFRVRGVTTNKSFLTNVLNHPDFIRGVVDTSFIASNPDLLEPSKSTNRGQKMLKYIGNTIVNGP 505
Cdd:COG1038 403 GRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVNGP 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 506 EKALGATGP--PPSKVdPIIPTLAAPPaskeKSLRQIYVEQGPEAFAKAVRAKKGLLLTDTTWRDAHQSLLATRMRTRDM 583
Cdd:COG1038 483 PGVKGRPKPdfPKPKL-PKVDLGAPPP----KGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDM 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 584 LAIAPATSIAMRDAFSLEMWGGATFDVSMRFLREDPWDRLAILREAVPDIPFQMLLRGANAVGYTSYPDNVVYKFCEKAQ 663
Cdd:COG1038 558 LKIAPATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAA 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 664 ATGMDVFRVFDSLNYLENMKLGIDAVGAAGGIIEAAMCYTGDVSDPTRGPYNLEYYLDFVRQLVAQGIHVLAIKDMAGLL 743
Cdd:COG1038 638 EAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKDMAGLL 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 744 KPQAAQILISAIRNEFpDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDVASDAMSGTTSQPSMGAVVAALKGSKYDTGVN 823
Cdd:COG1038 718 KPYAAYKLVKALKEEV-DLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLD 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 824 AEDIMEINDYWETMRGVYAPFESGQKSGSADVYNHEMPGGQYTNLLFQSTQLGLAGQWPAIKRAYATANRLLGDIIKVTP 903
Cdd:COG1038 797 LDALQELSNYWEAVRKYYAPFESGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTP 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 904 SSKVVGDFAQFIVQNKLTEQEVIDQAETLSFPKSVVEYFQGYLGIPHHGFPEPLRSRVLKGKvlpngqEMFHGRPGAEME 983
Cdd:COG1038 877 SSKVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGR------KPITVRPGELLP 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 984 PYDFEAAEKELKEKYGADkIRDVDVISHAIYPDVFTGFQKFKDEYGSMHFLDTRTFLTGLEVDTEVEVEMEHGKTVFIKL 1063
Cdd:COG1038 951 PVDFDALRAELEEKLGRE-PSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKL 1029
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1064 IAVGGVsKKDGMRDVIFELNGRQRVIKVKDEAAGVSTAVKPKA-TGLPGSVGAPMPGVVLDVRVKKGENVKAGDALLVLS 1142
Cdd:COG1038 1030 LAIGEP-DEDGMRTVFFELNGQPREVRVRDRSVKVTVASREKAdPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIE 1108
|
1130 1140 1150
....*....|....*....|....*....|....*.
gi 570336760 1143 AMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEI 1178
Cdd:COG1038 1109 AMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
29-1180 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 1790.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 29 IKKLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVGAGKSPVGAYLDIDSIIQIAKENNIDAIHP 108
Cdd:PRK12999 5 IKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVDAIHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 109 GYGFLSENVGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGTDGPVHTLEEARAFIDsGVGYPVIIKA 188
Cdd:PRK12999 85 GYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAE-EIGYPIMLKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 189 SMGGGGRGMRVVNRAEDLEENFERASSEALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVVHLYHRDCSVQRRHQKVL 268
Cdd:PRK12999 164 SAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 269 ETAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAGGE 348
Cdd:PRK12999 244 EIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 349 TFKDLG---LSQDKIKPRGHAMQCRVTTENPSTGFQPDSGVIEVFRSPGGMGIRLDDGPGFVGAHITPHYDSLLVKVTAR 425
Cdd:PRK12999 324 TLHDLEigiPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDSLLVKLTAW 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 426 ALDRGDCAHKLKRALSEFRVRGVTTNKSFLTNVLNHPDFIRGVVDTSFIASNPDLLEPSKSTNRGQKMLKYIGNTIVNGP 505
Cdd:PRK12999 404 GRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTVNGF 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 506 EkalGATGPPPSKVDPIIPTLAAPPASKEKSlRQIYVEQGPEAFAKAVRAKKGLLLTDTTWRDAHQSLLATRMRTRDMLA 585
Cdd:PRK12999 484 P---GVKKKPPVFPDPRLPKVDLSAPPPAGT-KQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLLR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 586 IAPATSIAMRDAFSLEMWGGATFDVSMRFLREDPWDRLAILREAVPDIPFQMLLRGANAVGYTSYPDNVVYKFCEKAQAT 665
Cdd:PRK12999 560 IAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAAA 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 666 GMDVFRVFDSLNYLENMKLGIDAVGAAGGIIEAAMCYTGDVSDPTRGPYNLEYYLDFVRQLVAQGIHVLAIKDMAGLLKP 745
Cdd:PRK12999 640 GIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMAGLLKP 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 746 QAAQILISAIRNEFpDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDVASDAMSGTTSQPSMGAVVAALKGSKYDTGVNAE 825
Cdd:PRK12999 720 AAAYELVSALKEEV-DLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDLD 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 826 DIMEINDYWETMRGVYAPFESGQKSGSADVYNHEMPGGQYTNLLFQSTQLGLAGQWPAIKRAYATANRLLGDIIKVTPSS 905
Cdd:PRK12999 799 AIRKLSPYWEAVRPYYAPFESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVTPSS 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 906 KVVGDFAQFIVQNKLTEQEVIDQAETLSFPKSVVEYFQGYLGIPHHGFPEPLRSRVLKgkvlpnGQEMFHGRPGAEMEPY 985
Cdd:PRK12999 879 KVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLK------GEEPITVRPGELLEPV 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 986 DFEAAEKELKEKYGaDKIRDVDVISHAIYPDVFTGFQKFKDEYGSMHFLDTRTFLTGLEVDTEVEVEMEHGKTVFIKLIA 1065
Cdd:PRK12999 953 DFEAERAELEEKLG-REVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEA 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1066 VGGVsKKDGMRDVIFELNGRQRVIKVKDEAAGVSTAVKPKA-TGLPGSVGAPMPGVVLDVRVKKGENVKAGDALLVLSAM 1144
Cdd:PRK12999 1032 IGEP-DEDGMRTVYFELNGQPREVQVRDRSVKSTVAAREKAdPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAM 1110
|
1130 1140 1150
....*....|....*....|....*....|....*.
gi 570336760 1145 KMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEIDE 1180
Cdd:PRK12999 1111 KMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
31-1179 |
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: 1576.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 31 KLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVGAG--KSPVGAYLDIDSIIQIAKENNIDAIHP 108
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 109 GYGFLSENVGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGTDGPVHTLEEARAFIDSgVGYPVIIKA 188
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAA-IGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 189 SMGGGGRGMRVVNRAEDLEENFERASSEALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVVHLYHRDCSVQRRHQKVL 268
Cdd:TIGR01235 160 SWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 269 ETAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAGGE 348
Cdd:TIGR01235 240 EVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 349 TF--KDLGL-SQDKIKPRGHAMQCRVTTENPSTGFQPDSGVIEVFRSPGGMGIRLDDGPGFVGAHITPHYDSLLVKVTAR 425
Cdd:TIGR01235 320 SLptPQLGVpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 426 ALDRGDCAHKLKRALSEFRVRGVTTNKSFLTNVLNHPDFIRGVVDTSFIASNPDLLEPSKSTNRGQKMLKYIGNTIVNGP 505
Cdd:TIGR01235 400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNGH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 506 EKalGATGPPPSKVDPIIPTLAAPPASKEKSLRQIYVEQGPEAFAKAVRAKKGLLLTDTTWRDAHQSLLATRMRTRDMLA 585
Cdd:TIGR01235 480 PE--AKDKLKPLENAPRVVVLYADQNPVPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 586 IAPATSIAMRDAFSLEMWGGATFDVSMRFLREDPWDRLAILREAVPDIPFQMLLRGANAVGYTSYPDNVVYKFCEKAQAT 665
Cdd:TIGR01235 558 IAPTTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQG 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 666 GMDVFRVFDSLNYLENMKLGIDAVGAAGGIIEAAMCYTGDVSDPTRGPYNLEYYLDFVRQLVAQGIHVLAIKDMAGLLKP 745
Cdd:TIGR01235 638 GIDIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLLKP 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 746 QAAQILISAIRnEFPDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDVASDAMSGTTSQPSMGAVVAALKGSKYDTGVNAE 825
Cdd:TIGR01235 718 AAAKLLIKALR-EKTDLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVA 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 826 DIMEINDYWETMRGVYAPFESGQKSGSADVYNHEMPGGQYTNLLFQSTQLGLAGQWPAIKRAYATANRLLGDIIKVTPSS 905
Cdd:TIGR01235 797 WIRELSAYWEAVRNLYAAFESDLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSS 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 906 KVVGDFAQFIVQNKLTEQEVIDQAETLSFPKSVVEYFQGYLGIPHHGFPEPLRSRVLKgkvlpnGQEMFHGRPGAEMEPY 985
Cdd:TIGR01235 877 KVVGDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLK------GEKPITVRPGSLLEPA 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 986 DFEAAEKELKEKYGADkIRDVDVISHAIYPDVFTGFQKFKDEYGSMHFLDTRTFLTGLEVDTEVEVEMEHGKTVFIKLIA 1065
Cdd:TIGR01235 951 DLDAIRKDLQEKHERE-VSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQA 1029
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1066 VgGVSKKDGMRDVIFELNGRQRVIKVKDEAAGVSTAVKPKAT-GLPGSVGAPMPGVVLDVRVKKGENVKAGDALLVLSAM 1144
Cdd:TIGR01235 1030 V-GATDSQGEREVFFELNGQPRRIKVPDRSHKAEAAVRRKADpGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAM 1108
|
1130 1140 1150
....*....|....*....|....*....|....*
gi 570336760 1145 KMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEID 1179
Cdd:TIGR01235 1109 KMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
29-484 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 644.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 29 IKKLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVGaGKSPVGAYLDIDSIIQIAKENNIDAIHP 108
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIG-PAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 109 GYGFLSENVGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGTDGPVHTLEEARAFIDSgVGYPVIIKA 188
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEE-IGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 189 SmggggrgmrvvNRAEDLEENFERASSEALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVVHLYHRDCSVQRRHQKVL 268
Cdd:COG4770 160 SaggggkgmrvvRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 269 ETAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAGGE 348
Cdd:COG4770 240 EEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 349 TfkdLGLSQDKIKPRGHAMQCRVTTENPSTGFQPDSGVIEVFRSPGGMGIRLDDGpGFVGAHITPHYDSLLVKVTARALD 428
Cdd:COG4770 320 P---LPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDSMIAKLIVWGPD 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 570336760 429 RGDCAHKLKRALSEFRVRGVTTNKSFLTNVLNHPDFIRGVVDTSFIASNPDLLEPS 484
Cdd:COG4770 396 REEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAA 451
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
28-474 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 549.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 28 TIKKLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVG---AGKSpvgaYLDIDSIIQIAKENNID 104
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGpapSKKS----YLNIPAIISAAEITGAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 105 AIHPGYGFLSENVGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGTDGPVHTLEEARAfIDSGVGYPV 184
Cdd:PRK08591 77 AIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALA-IAKEIGYPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 185 IIKASMGGGGRGMRVVNRAEDLEENFERASSEALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVVHLYHRDCSVQRRH 264
Cdd:PRK08591 156 IIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 265 QKVLETAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRI 344
Cdd:PRK08591 236 QKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 345 AGGEtfkDLGLSQDKIKPRGHAMQCRVTTENPSTGFQPDSGVIEVFRSPGGMGIRLDDG--PGFVgahITPHYDSLLVKV 422
Cdd:PRK08591 316 AAGE---PLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAvyTGYT---IPPYYDSMIGKL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 570336760 423 TARALDRGDCAHKLKRALSEFRVRGVTTNKSFLTNVLNHPDFIRGVVDTSFI 474
Cdd:PRK08591 390 IVHGETREEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL 441
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
30-497 |
1.56e-176 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 528.79 E-value: 1.56e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 30 KKLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVGAGkSPVGAYLDIDSIIQIAKENNIDAIHPG 109
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPA-PPSKSYLNIERIIDVAKKAGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 110 YGFLSENVGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGTDGPVHTLEEARAFIDSgVGYPVIIKAS 189
Cdd:PRK08654 82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEE-IGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 190 MGGGGRGMRVVNRAEDLEENFERASSEALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVVHLYHRDCSVQRRHQKVLE 269
Cdd:PRK08654 161 AGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 270 TAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDqQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAGGEt 349
Cdd:PRK08654 241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGE- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 350 fkDLGLSQDKIKPRGHAMQCRVTTENPSTGFQPDSGVIEVFRSPGGMGIRLDDGPgFVGAHITPHYDSLLVKVTARALDR 429
Cdd:PRK08654 319 --ELSFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGV-HMGYEIPPYYDSMISKLIVWGRTR 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 570336760 430 GDCAHKLKRALSEFRVRGVTTNKSFLTNVLNHPDFIRGVVDTSFIASNPDLLEpskstnrgqKMLKYI 497
Cdd:PRK08654 396 EEAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTILE---------EMKRYA 454
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
29-474 |
2.97e-169 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 508.03 E-value: 2.97e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 29 IKKLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVGagKSPVG-AYLDIDSIIQIAKENNIDAIH 107
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIG--GPRVQeSYLNLEKIIEIAKKTGAEAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 108 PGYGFLSENVGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGTDGPVHTLEEARAfIDSGVGYPVIIK 187
Cdd:PRK06111 80 PGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIA-IARQIGYPVMLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 188 ASMGGGGRGMRVVNRAEDLEENFERASSEALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVVHLYHRDCSVQRRHQKV 267
Cdd:PRK06111 159 ASAGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 268 LETAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAGG 347
Cdd:PRK06111 239 IEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 348 ETfkdLGLSQDKIKPRGHAMQCRVTTENPSTgFQPDSGVIEVFRSPGGMGIRLDDgpgFV--GAHITPHYDSLLVKVTAR 425
Cdd:PRK06111 319 EK---LSFTQDDIKRSGHAIEVRIYAEDPKT-FFPSPGKITDLTLPGGEGVRHDH---AVenGVTVTPFYDPMIAKLIAH 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 570336760 426 ALDRGDCAHKLKRALSEFRVRGVTTNKSFLTNVLNHPDFIRGVVDTSFI 474
Cdd:PRK06111 392 GETREEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
29-494 |
9.79e-169 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 507.33 E-value: 9.79e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 29 IKKLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVGAgkSPVGAYLDIDSIIQIAKENNIDAIHP 108
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGA--DPLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 109 GYGFLSENVGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGTDGPVHTLEEARAFIDsGVGYPVIIKA 188
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAE-RIGYPVMLKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 189 SMGGGGRGMRVVNRAEDLEENFERASSEALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVVHLYHRDCSVQRRHQKVL 268
Cdd:PRK07178 159 TSGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 269 ETAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAGGE 348
Cdd:PRK07178 239 EIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 349 TfkdLGLSQDKIKPRGHAMQCRVTTENPSTGFQPDSGVIEVFRSPGGMGIRLdDGPGFVGAHITPHYDSLLVKVTARALD 428
Cdd:PRK07178 319 P---LSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRT-DTAIYTGYTIPPYYDSMCAKLIVWALT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 570336760 429 RGDCAHKLKRALSEFRVRGVTTNKSFLTNVLNHPDFIRGVVDTSFIASNPDLLEPSKSTNRGQKML 494
Cdd:PRK07178 395 WEEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNYSIKRKPEELAA 460
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
556-1178 |
5.63e-167 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 507.46 E-value: 5.63e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 556 KKGLLLTDTTWRDAHQSLLATRMRTRDMLAIAPAtsiaMRDA--FSLEMWGGATFDVSMRFLREDPWDRLAILREAVPDI 633
Cdd:PRK09282 1 MKKVKITDTTLRDAHQSLLATRMRTEDMLPIAEK----LDKVgfWSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 634 PFQMLLRGANAVGYTSYPDNVVYKFCEKAQATGMDVFRVFDSLNYLENMKLGIDAVGAAGGIIEAAMCYtgdvsdpTRGP 713
Cdd:PRK09282 77 PLQMLLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISY-------TTSP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 714 Y-NLEYYLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFpDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDV 792
Cdd:PRK09282 150 VhTIEKYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEV-DLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 793 ASDAMSGTTSQPSMGAVVAALKGSKYDTGVNAEDIMEINDYWETMRGVYAPFESGQKSGSADVYNHEMPGGQYTNLLFQS 872
Cdd:PRK09282 229 AISPLAFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTIVDTRVLIHQVPGGMISNLVSQL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 873 TQLGLAGQWPAIKRAYATANRLLGDIIKVTPSSKVVGDFAqfiVQNKLTEQ--EVIdqaetlsfPKSVVEYFQGYLGIPh 950
Cdd:PRK09282 309 KEQNALDKLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQA---VLNVLTGEryKVI--------TKEVKDYVKGLYGRP- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 951 hgfPEPLrSRVLKGKVLPNgQEMFHGRPGAEMEPyDFEAAEKELKEKygaDKIRDVDVISHAIYPDVFTGFQKF--KDEY 1028
Cdd:PRK09282 377 ---PAPI-NEELRKKIIGD-EEPITCRPADLLEP-ELEKARKEAEEL---GKSEKEDVLTYALFPQIAKKFLEEreAGEL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1029 GSMHFLDTRTFLTGLEVDTEVEVEMeHGKTVFIKLIAVGGvskkDGMRDVIFELNGRQRVIKVKdEAAGVSTAVKPKATG 1108
Cdd:PRK09282 448 KPEPEPKEAAAAGAEGIPTEFKVEV-DGEKYEVKIEGVKA----EGKRPFYLRVDGMPEEVVVE-PLKEIVVGGRPRASA 521
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1109 lPGSVGAPMPGVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEI 1178
Cdd:PRK09282 522 -PGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
561-844 |
2.52e-160 |
|
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: 477.69 E-value: 2.52e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 561 LTDTTWRDAHQSLLATRMRTRDMLAIAPATSIAMrdAFSLEMWGGATFDVSMRFLREDPWDRLAILREAVPDIPFQMLLR 640
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 641 GANAVGYTSYPDNVVYKFCEKAQATGMDVFRVFDSLNYLENMKLGIDAVGAAGGIIEAAMCYTGDvsdptrGPYNLEYYL 720
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 721 DFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFPdLPIHVHTHDTAGTGVSSMLEAAYAGADAVDVASDAMSGT 800
Cdd:cd07937 153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVG-LPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 570336760 801 TSQPSMGAVVAALKGSKYDTGVNAEDIMEINDYWETMRGVYAPF 844
Cdd:cd07937 232 TSQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
29-477 |
1.23e-156 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 474.97 E-value: 1.23e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 29 IKKLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVGAGkSPVGAYLDIDSIIQIAKENNIDAIHP 108
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPA-SSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 109 GYGFLSENVGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGTDGPVHTLEEARAfIDSGVGYPVIIKA 188
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALE-IAKEIGYPVMVKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 189 SMGGGGRGMRVVNRAEDLEENFERASSEALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVVHLYHRDCSVQRRHQKVL 268
Cdd:PRK05586 160 SAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 269 ETAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAGGE 348
Cdd:PRK05586 240 EEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 349 tfkDLGLSQDKIKPRGHAMQCRVTTENPSTGFQPDSGVIEVFRSPGGMGIRLDDGPgFVGAHITPHYDSLLVKVTARALD 428
Cdd:PRK05586 320 ---KLSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAV-YSGYTIPPYYDSMIGKLIVYGKD 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 570336760 429 RGDCAHKLKRALSEFRVRGVTTNKSFLTNVLNHPDFIRGVVDTSFIASN 477
Cdd:PRK05586 396 REEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKK 444
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
29-474 |
3.61e-153 |
|
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: 465.77 E-value: 3.61e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 29 IKKLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVGAGKSpVGAYLDIDSIIQIAKENNIDAIHP 108
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPS-AKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 109 GYGFLSENVGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGTDGPVHTLEEARAfIDSGVGYPVIIKA 188
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVR-IAKRIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 189 SMGGGGRGMRVVNRAEDLEENFERASSEALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVVHLYHRDCSVQRRHQKVL 268
Cdd:TIGR00514 160 TAGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 269 ETAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAGGE 348
Cdd:TIGR00514 240 EEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 349 tfkDLGLSQDKIKPRGHAMQCRVTTENPSTGFQPDSGVIEVFRSPGGMGIRLdDGPGFVGAHITPHYDSLLVKVTARALD 428
Cdd:TIGR00514 320 ---PLSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRW-DSHVYSGYTVPPYYDSMIGKLITYGKT 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 570336760 429 RGDCAHKLKRALSEFRVRGVTTNKSFLTNVLNHPDFIRGVVDTSFI 474
Cdd:TIGR00514 396 REVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYL 441
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
27-493 |
1.02e-149 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 457.68 E-value: 1.02e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 27 STIKKLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVG---AGKSpvgaYLDIDSIIQIAKENNI 103
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGpshAAKS----YLNPAAILAAARQCGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 104 DAIHPGYGFLSENVGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGTDGPVHTLEEARAFIDSgVGYP 183
Cdd:PRK12833 79 DAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAAR-IGYP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 184 VIIKASMGGGGRGMRVVNRAEDLEENFERASSEALAAFGDGTVFIERYVDRPRHIEVQILGDGQgNVVHLYHRDCSVQRR 263
Cdd:PRK12833 158 LMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 264 HQKVLETAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVD-QQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQI 342
Cdd:PRK12833 237 RQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEML 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 343 RIAGGETfkdLGLSQDKIKPRGHAMQCRVTTENPSTGFQPDSGVIEVFRSPGGMGIRLDDG--PGFVgahITPHYDSLLV 420
Cdd:PRK12833 317 RIADGEP---LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLlyPGYR---VPPFYDSLLA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 570336760 421 KVTARALDRGDCAHKLKRALSEFRVRGVTTNKSFLTNVLNHPDFIRGVVDTSFI----ASNPDLLEPSKSTNRGQKM 493
Cdd:PRK12833 391 KLIVHGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLeawlAEWRAALDAAASAAVGEAA 467
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
29-477 |
1.55e-142 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 438.02 E-value: 1.55e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 29 IKKLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVGAGKSPvGAYLDIDSIIQIAKENNIDAIHP 108
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSS-ESYLNIPAIISAAEIFEADAIFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 109 GYGFLSENVGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGTDGPVHTLEEARAFIDSgVGYPVIIKA 188
Cdd:PRK08462 83 GYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKE-IGYPVILKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 189 SMGGGGRGMRVVNRAEDLEENFERASSEALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVVHLYHRDCSVQRRHQKVL 268
Cdd:PRK08462 162 AAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 269 ETAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAGGE 348
Cdd:PRK08462 242 EESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 349 TFkdlgLSQDKIKPRGHAMQCRVTTENPSTgFQPDSGVIEVFRSPGGMGIRLDDGpGFVGAHITPHYDSLLVKVTARALD 428
Cdd:PRK08462 322 EL----PSQESIKLKGHAIECRITAEDPKK-FYPSPGKITKWIAPGGRNVRMDSH-AYAGYVVPPYYDSMIGKLIVWGED 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 570336760 429 RGDCAHKLKRALSEFRVRGVTTNKSFLTNVLNHPDFIRGVVDTSFIASN 477
Cdd:PRK08462 396 RNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
556-1132 |
1.23e-140 |
|
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: 436.63 E-value: 1.23e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 556 KKGLLLTDTTWRDAHQSLLATRMRTRDMLAIAPAtsiaMRDA--FSLEMWGGATFDVSMRFLREDPWDRLAILREAVPDI 633
Cdd:COG5016 1 MKKVKITDTTLRDGHQSLFATRMRTEDMLPIAEK----LDEAgfWSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 634 PFQMLLRGANAVGYTSYPDNVVYKFCEKAQATGMDVFRVFDSLNYLENMKLGIDAVGAAGGIIEAAMCYTgdVSdptrgP 713
Cdd:COG5016 77 PLQMLLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYT--IS-----P 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 714 -YNLEYYLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFpDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDV 792
Cdd:COG5016 150 vHTVEYYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEAL-DIPIELHTHATSGLAPATYLKAIEAGVDIIDT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 793 ASDAMSGTTSQPSMGAVVAALKGSKYDTGVNAEDIMEINDYWETMRGVYAPFESGQKSGSADVYNHEMPGGQYTNLLFQS 872
Cdd:COG5016 229 AISPLAGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGVDPRVLVHQVPGGMLSNLVSQL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 873 TQLGLAGQWPAIKRAYATANRLLGDIIKVTPSSKVVGDFAqfiVQNKLTEQ--EVIdqaetlsfPKSVVEYFQGYLGIPh 950
Cdd:COG5016 309 KEQGALDRLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQA---VLNVLTGEryKMI--------TKEVKDYVLGYYGKT- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 951 hgfPEP----LRSRVLKGKvlpngqEMFHGRPGAEMEPyDFEAAEKELKEKygadkiRDVDVISHAIYPDVFTGFqkFKD 1026
Cdd:COG5016 377 ---PAPidpeVRKKALGDE------EPITCRPADLLEP-ELEKLRKEGLAK------SDEDVLTYALFPQVAIKF--LKG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1027 EYGSMHFLDtrtfLTGLEVDTEVEVEMEHGKTVFIKLIAVGGVSKKDGMRDVIFElngrQRVIKVKDEAAGVSTAVKPKA 1106
Cdd:COG5016 439 RAAGEARPD----APLAELAAVEEVVVVAEGVVVVVVVGGGAEGVVVVVVGVPGA----GAVAVVAAAAAVAAAAAAAAA 510
|
570 580
....*....|....*....|....*.
gi 570336760 1107 TGLPGSVGAPMPGVVLDVRVKKGENV 1132
Cdd:COG5016 511 AAAAAAGAAVKKVVAVGGAVVVGVEV 536
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
29-484 |
1.03e-137 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 426.54 E-value: 1.03e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 29 IKKLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVGagKSPVGAYLDIDSIIQIAKENNIDAIHP 108
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIG--TDPIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 109 GYGFLSENVGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGTDgPV--HTLEEARAFIDSgVGYPVII 186
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTE-KLnsESMEEIKIFARK-IGYPVIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 187 KASMGGGGRGMRVVNRAEDLEENFERASSEALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVVHLYHRDCSVQRRHQK 266
Cdd:PRK08463 158 KASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 267 VLETAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAG 346
Cdd:PRK08463 238 VIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 347 GETfkdLGLSQDKIKPRGHAMQCRVTTENPSTGFQPDSGVIEVFRSPGGMGIRLDDGPgFVGAHITPHYDSLLVKVTARA 426
Cdd:PRK08463 318 GEI---LDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHI-YKDYTIPPYYDSMLAKLIVKA 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 570336760 427 LDRGDCAHKLKRALSEFRVRGVTTNKSFLTNVLNHPDFIRGVVDTSFIASN-PDLLEPS 484
Cdd:PRK08463 394 TSYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHmQELLEKT 452
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
561-1175 |
2.52e-136 |
|
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate decarboxylase alpha subunit and its equivalents in archaea. The oxaloacetate decarboxylase Na+ pump is the paradigm of the family of Na+ transport decarboxylases that present in bacteria and archaea. It a multi subunit enzyme consisting of a peripheral alpha-subunit and integral membrane subunits beta and gamma. The energy released by the decarboxylation reaction of oxaloacetate is coupled to Na+ ion pumping across the membrane. [Transport and binding proteins, Cations and iron carrying compounds, Energy metabolism, Other]
Pssm-ID: 273447 [Multi-domain] Cd Length: 582 Bit Score: 426.90 E-value: 2.52e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 561 LTDTTWRDAHQSLLATRMRTRDMLAIAPAtsiaMRDA--FSLEMWGGATFDVSMRFLREDPWDRLAILREAVPDIPFQML 638
Cdd:TIGR01108 1 ITDVVLRDAHQSLFATRMRTEDMLPIAEK----LDDVgyWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 639 LRGANAVGYTSYPDNVVYKFCEKAQATGMDVFRVFDSLNYLENMKLGIDAVGAAGGIIEAAMCYTgdvsdpTRGPYNLEY 718
Cdd:TIGR01108 77 LRGQNLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT------TSPVHTLET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 719 YLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFpDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDVASDAMS 798
Cdd:TIGR01108 151 YLDLAEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRF-GLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 799 GTTSQPSMGAVVAALKGSKYDTGVNAEDIMEINDYWETMRGVYAPFESGQKSGSADVYNHEMPGGQYTNLLFQSTQLGLA 878
Cdd:TIGR01108 230 GGTSHPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFEGQLKGPDSRILVAQVPGGMLSNLESQLKEQNAL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 879 GQWPAIKRAYATANRLLGDIIKVTPSSKVVGDFAqfiVQNKLTEQevidQAETLSfpKSVVEYFQGYLGIPHHGFPEPLR 958
Cdd:TIGR01108 310 DKLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQA---VLNVLTGE----RYKTIT--KETKGYLKGEYGRTPAPINAELQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 959 SRVLKGKVLPngqemFHGRPGAEMEPyDFEAAEKELKEKyGADKIRDVDVISHAIYPDVftgfqkfkdeygSMHFLDTRT 1038
Cdd:TIGR01108 381 RKILGDEKPI-----VDCRPADLLEP-ELDKLRAEVREA-GAEKNSIEDVLTYALFPQV------------GLKFLENRH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1039 FLTGLE-VDTEVEVEMEHGKTVFIKLIAVGGVS---KKDGMRDVIFELNGRQRVIKVKDEAAGVSTAVKPKATGLPGSVG 1114
Cdd:TIGR01108 442 NPAAFEpKPEEKVIEQEHAQVVGKYEETHASGSytvEVEGKAFVVKVSPGGDVSQITASAPANTSGGTVAAKAGAGTPVT 521
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 570336760 1115 APMPGVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLL 1175
Cdd:TIGR01108 522 APIAGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREILVKVGDAVSVGQVL 582
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
555-1178 |
2.07e-114 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 368.87 E-value: 2.07e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 555 AKKGLLLTDTTWRDAHQSLLATRMRTRDMLAIApatsiAMRDA---FSLEMWGGATFDVSMRFLREDPWDRLAILREAVP 631
Cdd:PRK14040 1 MSKPLAITDVVLRDAHQSLFATRLRLDDMLPIA-----AKLDKvgyWSLESWGGATFDACIRFLGEDPWERLRELKKAMP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 632 DIPFQMLLRGANAVGYTSYPDNVVYKFCEKAQATGMDVFRVFDSLNYLENMKLGIDAVGAAGGIIEAAMCYTgdvsdpTR 711
Cdd:PRK14040 76 NTPQQMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT------TS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 712 GPYNLEYYLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFpDLPIHVHTHDTAGTGVSSMLEAAYAGADAVD 791
Cdd:PRK14040 150 PVHTLQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRV-DVPLHLHCHATTGLSTATLLKAIEAGIDGVD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 792 VASDAMSGTTSQPSMGAVVAALKGSKYDTGVNAEDIMEINDYWETMRGVYAPFESGQKSGSADVYNHEMPGGQYTNLLFQ 871
Cdd:PRK14040 229 TAISSMSMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFEGQLKGVDSRILVAQVPGGMLTNMESQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 872 STQLGLAGQWPAIKRAYATANRLLGDIIKVTPSSKVVGDFAqfiVQNKLTEQEVidqaetlsfpKSVVEYFQGYLGIPHH 951
Cdd:PRK14040 309 LKEQGAADKLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQA---VLNVLTGERY----------KTITKETAGVLKGEYG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 952 GFPEP----LRSRVLKGKvlpngqEMFHGRPGAEMEPyDFEAAEKELKEKYGADKIR-----DVDVISHAIYPDVftGFQ 1022
Cdd:PRK14040 376 ATPAPvnaeLQARVLEGA------EPITCRPADLLAP-ELDKLEAELRRQAQEKGITlaenaIDDVLTYALFPQI--GLK 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1023 kfkdeygsmhFLDTRTFLTGLEVDTEVEVEMEhgktvfikliAVGGVSKKDGMRDVifELNGRQRVIKVKDE-------- 1094
Cdd:PRK14040 447 ----------FLENRHNPAAFEPVPQAEAAQP----------AAKAEPAGSETYTV--EVEGKAYVVKVSEGgdisqitp 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1095 ----AAGVSTAVKPKATGLPGSVGAPMPGVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNML 1170
Cdd:PRK14040 505 aapaAAPAAAAAAAPAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVA 584
|
....*...
gi 570336760 1171 GGDLLVEI 1178
Cdd:PRK14040 585 VGDTLLTL 592
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
561-1025 |
1.29e-106 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 342.84 E-value: 1.29e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 561 LTDTTWRDAHQSLLATRMRTRDMLAIapatsIAMRDA---FSLEMWGGATFDVSMRFLREDPWDRLAILREAVPDIPFQM 637
Cdd:PRK12331 6 ITETVLRDGQQSLIATRMTTEEMLPI-----LEKLDNagyHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 638 LLRGANAVGYTSYPDNVVYKFCEKAQATGMDVFRVFDSLNYLENMKLGIDAVGAAGGIIEAAMCYTgdvsdpTRGPYNLE 717
Cdd:PRK12331 81 LLRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT------TSPVHTID 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 718 YYLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFpDLPIHVHTHDTAgtGVSSM--LEAAYAGADAVDVASD 795
Cdd:PRK12331 155 YFVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAV-TVPLEVHTHATS--GIAEMtyLKAIEAGADIIDTAIS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 796 AMSGTTSQPSMGAVVAALKGSKYDTGVNAEDIMEINDYWETMRGVYapFESGQ-----KSGSADVYNHEMPGGQYTNLLF 870
Cdd:PRK12331 232 PFAGGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHY--REEGIlnpkvKDVEPKTLIYQVPGGMLSNLLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 871 QSTQLGLAGQWPAIKRAYATANRLLGDIIKVTPSSKVVGDFAqfiVQNKLTEQ--EVIdqaetlsfPKSVVEYFQGYLGI 948
Cdd:PRK12331 310 QLKEQGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQA---LMNVISGEryKMV--------PNEIKDYVRGLYGR 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 570336760 949 PhhgfPEPLrSRVLKGKVLPNgQEMFHGRPGAEMEPyDFEAAEKELKEKYGADKirdvDVISHAIYPDVFTGFQKFK 1025
Cdd:PRK12331 379 P----PAPI-AEEIKKKIIGD-EEVITCRPADLIEP-QLEKLREEIAEYAESEE----DVLSYALFPQQAKDFLGRR 444
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
560-1179 |
1.19e-95 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 318.20 E-value: 1.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 560 LLTDTTWRDAHQSLLATRMRTRDMLAIAPAtsiaMRDA--FSLEMWGGATFDVSMRFLREDPWDRLAILREAVPDIPFQM 637
Cdd:PRK14042 5 FITDVTLRDAHQCLIATRMRTEDMLPICNK----MDDVgfWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 638 LLRGANAVGYTSYPDNVVYKFCEKAQATGMDVFRVFDSLNYLENMKLGIDAVGAAGGIIEAAMCYTgdvsdpTRGPYNLE 717
Cdd:PRK14042 81 LLRGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYT------TSPVHTLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 718 YYLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRnEFPDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDVASDAM 797
Cdd:PRK14042 155 NFLELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLK-QATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 798 SGTTSQPSMGAVVAALKGSKYDTGVNAEDIMEINDYWETMRGVYAPFESGQKSGSADVYNHEMPGGQYTNLLFQSTQLGL 877
Cdd:PRK14042 234 SGGASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLYQVPGGMISNLYNQLKEQNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 878 AGQWPAIKRAYATANRLLGDIIKVTPSSKVVGDFAqfiVQNKLTEQevidQAETLSfpKSVVEYFQGYLGIPHHGFPEPL 957
Cdd:PRK14042 314 LDKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQA---VINVLTGE----RYKTIT--NEVKLYCQGKYGTPPGKISSAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 958 RSRVLkGKVlpngqEMFHGRPGaEMEPYDFEAAEKELKEKygadKIRDVDVISHAIYPDVftgFQKFKDEYGSMHFLDTR 1037
Cdd:PRK14042 385 RKKAI-GRT-----EVIEVRPG-DLLPNELDQLQNEISDL----ALSDEDVLLYAMFPEI---GRQFLEQRKNNQLIPEP 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1038 TFLTGLEVDTEVEVEME---HGKTVFIKLIAVGGVskKDGMRDVIFELNGRQRVIKV-------KDEAAGVSTAVKpkat 1107
Cdd:PRK14042 451 LLTQSSAPDNSVMSEFDiilHGESYHVKVAGYGMI--EHGQQSCFLWVDGVPEEVVVqhselhdKIERSSVNNKIG---- 524
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 570336760 1108 glPGSVGAPMPGVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEID 1179
Cdd:PRK14042 525 --PGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
560-1028 |
5.49e-94 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 309.41 E-value: 5.49e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 560 LLTDTTWRDAHQSLLATRMRTRDMLAIAPATSIAmrDAFSLEMWGGATFDVSMRFLREDPWDRLAILREAVPDIPFQMLL 639
Cdd:PRK14041 4 MFVDTTLRDGHQSLIATRMRTEDMLPALEAFDRM--GFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQMLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 640 RGANAVGYTSYPDNVVYKFCEKAQATGMDVFRVFDSLNYLENMKLGIDAVGAAGGIIEAAMCYTgdVSdPTrgpYNLEYY 719
Cdd:PRK14041 82 RGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT--VS-PV---HTLEYY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 720 LDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFpDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDVASDAMSG 799
Cdd:PRK14041 156 LEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKF-GVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPFSM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 800 TTSQPSMGAVVAALKGSKYDTGVNAEDIMEINDYWETMRGVYAPFESGQKSGSADVYNHEMPGGQYTNLLFQSTQLGLAG 879
Cdd:PRK14041 235 GTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYDVGMKSPDSRILVSQIPGGMYSNLVKQLKEQKMLH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 880 QWPAIKRAYATANRLLGDIIKVTPSSKVVGDFAqfiVQNKLTEQ--EVIdqaetlsfPKSVVEYFQGYLGIPhhgfPEPL 957
Cdd:PRK14041 315 KLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQA---VLNVLTGEryKRV--------TNETKNYVKGLYGRP----PAPI 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 570336760 958 RSRVLKgKVLPNgQEMFHGRPGAEMEPyDFEAAEKELkekyGADKIRDVDVISHAIYPDVftGFQKFKDEY 1028
Cdd:PRK14041 380 DEELMK-KILGD-EKPIDCRPADLLEP-ELEKARKEL----GILAETDEDLLIYVILGEV--GKKFLKKKY 441
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
855-1062 |
3.43e-91 |
|
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: 291.28 E-value: 3.43e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 855 VYNHEMPGGQYTNLLFQSTQLGLAGQWPAIKRAYATANRLLGDIIKVTPSSKVVGDFAQFIVQNKLTEQEVIDQAETLSF 934
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 935 PKSVVEYFQGYLGIPHHGFPEPLRSRVLKGKvlpngqEMFHGRPGAEMEPYDFEAAEKELKEKYGaDKIRDVDVISHAIY 1014
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGE------EPITCRPGDLLPPVDLEKLRKELEEKAG-RETTEEDVLSYALY 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 570336760 1015 PDVFTGFQKFKDEYGSMHFLDTRTFLTGLEVDTEVEVEMEHGKTVFIK 1062
Cdd:pfam02436 154 PKVAEKFLKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
561-1021 |
7.44e-82 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 277.03 E-value: 7.44e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 561 LTDTTWRDAHQSLLATRMRTRDMlaIAPATSIAMRDAFSLEMWGGATFDVSMRFLREDPWDRLAILREAVPDIPFQMLLR 640
Cdd:PRK12330 7 VTELALRDAHQSLMATRMAMEDM--VGACEDIDNAGYWSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQMLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 641 GANAVGYTSYPDNVVYKFCEKAQATGMDVFRVFDSLNYLENMKLGIDAVGAAGGIIEAAMCYTgdVSdPTRGPynlEYYL 720
Cdd:PRK12330 85 GQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYT--VS-PIHTV---EGFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 721 DFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEF-PDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDVASDAMS- 798
Cdd:PRK12330 159 EQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgEDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAISSMSl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 799 GTTSQPSMgAVVAALKGSKYDTGVNAEDIMEINDYWETMRGVYAPFESGQKSGSADVYNHEMPGGQYTNLLFQSTQLGLA 878
Cdd:PRK12330 239 GPGHNPTE-SLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTTGVETEIFKSQIPGGMLSNMESQLKQQGAG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 879 GQWPAIKRAYATANRLLGDIIKVTPSSKVVGDFAQFivqNKLTEQEVIDQAEtlsfpksVVEYFQGYLGIPhhgfPEPLR 958
Cdd:PRK12330 318 DRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQAVF---NVLMGRYKVLTGE-------FADLMLGYYGET----PGERN 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 570336760 959 SRVLKGKVLPNGQEMFHGRPGAEMEP--YDFEAAEKELKEKYGADKirdvDVISHAIYPDVFTGF 1021
Cdd:PRK12330 384 PEVVEQAKKQAKKEPITCRPADLLEPewDKLRAEALALEGCDGSDE----DVLTYALFPQVAPKF 444
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
143-349 |
5.38e-75 |
|
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: 246.83 E-value: 5.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 143 DKTAAREIAIEQKVPVVPGTDGPVHTLEEARAFIDSgVGYPVIIKASMGGGGRGMRVVNRAEDLEENFERASSEALAAFG 222
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKE-IGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 223 DGTVFIERYVDRPRHIEVQILGDGQGNVVHLYHRDCSVQRRHQKVLETAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGT 302
Cdd:pfam02786 80 NPQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 570336760 303 VEFLVDQ-QGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAGGET 349
Cdd:pfam02786 160 VEFALDPfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYP 207
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
562-835 |
8.59e-72 |
|
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: 240.05 E-value: 8.59e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 562 TDTTWRDAHQSLLATrMRTRDMLAIAPATSiamrDA--FSLEMWGGATFDVSmrFLREDPWDRLAILREAVPDIPFQMLL 639
Cdd:cd03174 1 TDTTLRDGLQSEGAT-FSTEDKLEIAEALD----EAgvDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 640 RGanavgytsypdnvVYKFCEKAQATGMDVFRVFDSLNY--------------LENMKLGIDAVGAAGGIIEAAMCYTgd 705
Cdd:cd03174 74 RN-------------REKGIERALEAGVDEVRIFDSASEthsrknlnksreedLENAEEAIEAAKEAGLEVEGSLEDA-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 706 vsdpTRGPYNLEYYLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFPDLPIHVHTHDTAGTGVSSMLEAAYA 785
Cdd:cd03174 139 ----FGCKTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEA 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 570336760 786 GADAVDVASDAMSGTTSQPSMGAVVAALKGSKYDTGVNAEDIMEINDYWE 835
Cdd:cd03174 215 GADRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVE 264
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
556-1021 |
8.32e-69 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 239.25 E-value: 8.32e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 556 KKGLLLTDTTWRDAHQSLLATRMRTRDMLAIApaTSIAMRDAFSLEMWGGATFDVSMRFLREDPWDRLAILREAVPDIPF 635
Cdd:PRK12581 10 QQQVAITETVLRDGHQSLMATRLSIEDMLPVL--TILDKIGYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 636 QMLLRGANAVGYTSYPDNVVYKFCEKAQATGMDVFRVFDSLNYLENMKLGIDAVGAAGGiiEAAMCytgdVSDPTRGPYN 715
Cdd:PRK12581 88 QMLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGK--EAQLC----IAYTTSPVHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 716 LEYYLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRnEFPDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDVASD 795
Cdd:PRK12581 162 LNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIK-AMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 796 AMSGTTSQPSMGAVVAALKGSKYDTGVNAEDIMEINDYWETMRGVY---APFESGQKSGSADVYNHEMPGGQYTNLLFQS 872
Cdd:PRK12581 241 PFSEGTSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYladGILDPSLLFPDPRTLQYQVPGGMLSNMLSQL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 873 TQLGLAGQWPAIKRAYATANRLLGDIIKVTPSSKVVGDFAQFIVQNKLTEQEVidqaetlsfPKSVVEYFQGYLGiphhG 952
Cdd:PRK12581 321 KQANAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNVILGKPYQMV---------SKEIKQYLAGDYG----K 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 570336760 953 FPEPLRSRVLKGKVlpNGQEMFHGRPGAEMEPyDFEAAEKELKEKYGADKirdvDVISHAIYPDVFTGF 1021
Cdd:PRK12581 388 TPAPVNEDLKRSQI--GSAPVTTNRPADQLSP-EFEVLKAEVADLAQTDE----DVLTYALFPSVAKPF 449
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
90-348 |
9.21e-50 |
|
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: 177.37 E-value: 9.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 90 DIDSII----QIAKENNIDAIhpgygfLSEN----VGFAEQCAKNGIKfvGPTPENLQRFGDKTAAREIAIEQKVPVvPG 161
Cdd:COG0439 1 DIDAIIaaaaELARETGIDAV------LSESefavETAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 162 TDgPVHTLEEARAFIDSgVGYPVIIKASMGGGGRGMRVVNRAEDLEENFERASSEALAAFGDGTVFIERYVDRpRHIEVQ 241
Cdd:COG0439 72 FA-LVDSPEEALAFAEE-IGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 242 ILGDgQGNVVHlyhrdCSVQRRHQK---VLE---TAPAVgLDPKTEKAMIDDAVRLTSAAKYLN-AGTVEFLVDQQGRHY 314
Cdd:COG0439 149 GLVR-DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGEPY 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 570336760 315 FIEVNPRIQVEH--TITEEITGIDLVQSQIRIAGGE 348
Cdd:COG0439 222 LIEINARLGGEHipPLTELATGVDLVREQIRLALGE 257
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
29-136 |
9.90e-50 |
|
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: 171.13 E-value: 9.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 29 IKKLMAANRGEIATRIMRAGNELGLRTVGIFSKEDRFTQHRYKADESFLVGAGkSPVGAYLDIDSIIQIAKENNIDAIHP 108
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPG-PASESYLNIDAIIDAAKETGADAIHP 79
|
90 100
....*....|....*....|....*...
gi 570336760 109 GYGFLSENVGFAEQCAKNGIKFVGPTPE 136
Cdd:pfam00289 80 GYGFLSENAEFARACEEAGIIFIGPSPE 107
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
368-475 |
1.03e-44 |
|
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: 156.80 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 368 QCRVTTENPSTGFQPDSGVIEVFRSPGGMGIRLDDGpGFVGAHITPHYDSLLVKVTARALDRGDCAHKLKRALSEFRVRG 447
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSG-VYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 570336760 448 VTTNKSFLTNVLNHPDFIRGVVDTSFIA 475
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
368-475 |
6.53e-38 |
|
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: 137.24 E-value: 6.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 368 QCRVTTENPSTGFQPDSGVIEVFRSPGGMGIRLDDGpGFVGAHITPHYDSLLVKVTARALDRGDCAHKLKRALSEFRVRG 447
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSG-VYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*...
gi 570336760 448 VTTNKSFLTNVLNHPDFIRGVVDTSFIA 475
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLE 107
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
561-833 |
1.69e-34 |
|
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: 133.24 E-value: 1.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 561 LTDTTWRDAHQSLlATRMRTRDMLAIAPAtsiamrdafsLEMWGGATFDVSMRFLREDPWDRLAILREAVPDIPFQMLLR 640
Cdd:pfam00682 4 ICDTTLRDGEQAL-GVAFSIDEKLAIARA----------LDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVLCR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 641 GAnavgytsypDNVVYKFCEKAQATGMDVFRVFDSLNYLE-NMKLGIDAVGAAG---GIIEAAMCYTGDVS----DPTRG 712
Cdd:pfam00682 73 AR---------EHDIKAAVEALKGAGAVRVHVFIATSDLHrKYKLGKDREEVAKravAAVKAARSRGIDVEfspeDASRT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 713 PynLEYYLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFPD-LPIHVHTHDTAGTGVSSMLEAAYAGADAVD 791
Cdd:pfam00682 144 D--PEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRVD 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 570336760 792 VASDAMSGTTSQPSMGAVVAALKGSKYDTGVNAEDIMEINDY 833
Cdd:pfam00682 222 GTVNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANL 263
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1113-1178 |
8.46e-25 |
|
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: 98.64 E-value: 8.46e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 570336760 1113 VGAPMPGVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEI 1178
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1095-1179 |
2.17e-16 |
|
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: 76.86 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1095 AAGVSTAVKPKATGLPGSVGAPMPGVV-------LDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGD 1167
Cdd:COG0511 45 AAAPAAAAAAAAASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQ 124
|
90
....*....|..
gi 570336760 1168 NMLGGDLLVEID 1179
Cdd:COG0511 125 PVEYGQPLFVIE 136
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1113-1178 |
6.78e-16 |
|
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: 73.40 E-value: 6.78e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 570336760 1113 VGAPMPGV-----VLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEI 1178
Cdd:pfam00364 3 IKSPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1096-1178 |
1.68e-14 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 72.20 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1096 AGVSTAVKPKATGlPGSVGAPMPGVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLL 1175
Cdd:PRK05641 71 APAAPAPAPASAG-ENVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPL 149
|
...
gi 570336760 1176 VEI 1178
Cdd:PRK05641 150 IEL 152
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
44-322 |
6.58e-13 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 71.88 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 44 IMRAGNELGLRTVGIFSKEDRFTQH-RYkADESFLVGAGKSPVGAYldIDSIIQIAKENNIDAIHPGY----GFLSENVG 118
Cdd:COG3919 20 VARSLGEAGVRVIVVDRDPLGPAARsRY-VDEVVVVPDPGDDPEAF--VDALLELAERHGPDVLIPTGdeyvELLSRHRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 119 FAEQcaknGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVvPGTDgPVHTLEEARAFIDsGVGYPVIIKASMGGGGRGMR 198
Cdd:COG3919 97 ELEE----HYRLPYPDADLLDRLLDKERFYELAEELGVPV-PKTV-VLDSADDLDALAE-DLGFPVVVKPADSVGYDELS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 199 VVNR-----AEDLEEnFERASSEALAAfgDGTVFIERYVDRPRHIEVQILG--DGQGNVVHLYHrdcsvqrrHQKVLETA 271
Cdd:COG3919 170 FPGKkkvfyVDDREE-LLALLRRIAAA--GYELIVQEYIPGDDGEMRGLTAyvDRDGEVVATFT--------GRKLRHYP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 570336760 272 PAVG----LDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQ-GRHYFIEVNPRI 322
Cdd:COG3919 239 PAGGnsaaRESVDDPELEEAARRLLEALGYHGFANVEFKRDPRdGEYKLIEINPRF 294
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
120-355 |
1.09e-12 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 72.72 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 120 AEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGtdGPVHTLEEARAFIdSGVGYPVIIKASMGGGGRGMRV 199
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFA-SEIGYPVLVRPSYVLGGRAMEI 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 200 VNRAEDLEENFErassEALAAFGDGTVFIERYVDRPRHIEVQILGDGqGNV-------------VHLYHRDCSVqrrhqk 266
Cdd:TIGR01369 723 VYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDG-EEVlipgimehieeagVHSGDSTCVL------ 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 267 vletaPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDqQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAG 346
Cdd:TIGR01369 792 -----PPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVML 865
|
....*....
gi 570336760 347 GETFKDLGL 355
Cdd:TIGR01369 866 GKKLEELGV 874
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1095-1178 |
1.19e-12 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 65.99 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1095 AAGVSTAVKPKATGLPGSVGAPMPGVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDL 1174
Cdd:PRK06549 46 PQVEAQAPQPAAAAGADAMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDG 125
|
....
gi 570336760 1175 LVEI 1178
Cdd:PRK06549 126 LITI 129
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1113-1179 |
3.05e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 57.10 E-value: 3.05e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 570336760 1113 VGAPMPGVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEID 1179
Cdd:PRK08225 4 VYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
89-355 |
3.07e-10 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 64.13 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 89 LDIDSIIQIAKENNIDAIHPGYGflsenvG-----FAEQCAKN----GIKFVGPTP------ENLQRFgdKTAAREIAIe 153
Cdd:COG0458 57 LTVEDVLDIIEKEKPDGVIVQFG------GqtalnLAVELEEAgileGVKILGTSPdaidlaEDRELF--KELLDKLGI- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 154 qkvPVVPGtdGPVHTLEEARAFIDSgVGYPVIIKASmggggrgmrvvNRAEDLEEnFERASSEALAAFGDGTVFIERYVD 233
Cdd:COG0458 128 ---PQPKS--GTATSVEEALAIAEE-IGYPVIVRPSyvlg---grgmGIVYNEEE-LEEYLERALKVSPDHPVLIDESLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 234 RPRHIEVQILGDGQGNVV------HLyhrD----------CSvqrrhqkvletAPAVGLDPKTEKAMIDDAVRLtsaAKY 297
Cdd:COG0458 198 GAKEIEVDVVRDGEDNVIivgimeHI---EpagvhsgdsiCV-----------APPQTLSDKEYQRLRDATLKI---ARA 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 570336760 298 LN-AGT--VEFLVDqQGRHYFIEVNPRiqVEHTIT--EEITGIDLVQSQIRIAGGETFKDLGL 355
Cdd:COG0458 261 LGvVGLcnIQFAVD-DGRVYVIEVNPR--ASRSSPfaSKATGYPIAKIAAKLALGYTLDELGN 320
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
97-322 |
4.45e-09 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 60.78 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 97 IAKENnIDAIHPGYG---FLSENVGFAEQ--CAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGtdGPVHTLEE 171
Cdd:TIGR01369 77 IEKER-PDAILPTFGgqtALNLAVELEESgvLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIAHSVEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 172 ARAFIDSgVGYPVIIKASMGGGGRGMRVVNRAEDLEENFERasseALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVV 251
Cdd:TIGR01369 154 ALAAAKE-IGYPVIVRPAFTLGGTGGGIAYNREELKEIAER----ALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCI 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 570336760 252 HLyhrdCSVQRRHQKVLET------APAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVD-QQGRHYFIEVNPRI 322
Cdd:TIGR01369 229 TV----CNMENFDPMGVHTgdsivvAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNpDSGRYYVIEVNPRV 302
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
660-830 |
3.33e-08 |
|
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163676 Cd Length: 274 Bit Score: 56.25 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 660 EKAQATGMDVFRVF----DSLNyLENMKLGID-AVGAAGGIIEAAMCY----TGDVS----DPTRGPYNLEYYLDFVRQL 726
Cdd:cd07938 80 ERALAAGVDEVAVFvsasETFS-QKNINCSIAeSLERFEPVAELAKAAglrvRGYVStafgCPYEGEVPPERVAEVAERL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 727 VAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFPDLPIHVHTHDTAGTGVSSMLeAAY-AGADAVDvASdaMSGTTSQP- 804
Cdd:cd07938 159 LDLGCDEISLGDTIGVATPAQVRRLLEAVLERFPDEKLALHFHDTRGQALANIL-AALeAGVRRFD-SS--VGGLGGCPf 234
|
170 180 190
....*....|....*....|....*....|....
gi 570336760 805 SMGA--------VVAALKGSKYDTGVNAEDIMEI 830
Cdd:cd07938 235 APGAtgnvatedLVYMLEGMGIETGIDLDKLLAA 268
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
70-321 |
5.26e-08 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 56.05 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 70 YKADESFLVGAGKSPvgAYldIDSIIQIAKENNIDAIHPGY----GFLSENvgfAEQCAKNGIKFVGPTPENLQRFGDKT 145
Cdd:PRK12767 41 YFADKFYVVPKVTDP--NY--IDRLLDICKKEKIDLLIPLIdpelPLLAQN---RDRFEEIGVKVLVSSKEVIEICNDKW 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 146 AAREIAIEQKVPVvPGTDGPVHTLEEARAFIDSGVGYPVIIK-----ASmggggrgmRVVNRAEDLEEnFERASSEALAa 220
Cdd:PRK12767 114 LTYEFLKENGIPT-PKSYLPESLEDFKAALAKGELQFPLFVKprdgsAS--------IGVFKVNDKEE-LEFLLEYVPN- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 221 fgdgtVFIERYVDrprHIE--VQILGDGQGNVVHlyhrdcSVQRRHQKVL--ETAPAV-GLDPKTEKaMIDDAVRLTSAA 295
Cdd:PRK12767 183 -----LIIQEFIE---GQEytVDVLCDLNGEVIS------IVPRKRIEVRagETSKGVtVKDPELFK-LAERLAEALGAR 247
|
250 260
....*....|....*....|....*.
gi 570336760 296 KYLNagtVEFLVDqQGRHYFIEVNPR 321
Cdd:PRK12767 248 GPLN---IQCFVT-DGEPYLFEINPR 269
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1113-1179 |
8.56e-08 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 50.19 E-value: 8.56e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 570336760 1113 VGAPMPGVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEID 1179
Cdd:PRK05889 5 VRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVIS 71
|
|
| DRE_TIM_CMS |
cd07945 |
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ... |
715-843 |
2.15e-07 |
|
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic TIM barrel domain; Citramalate synthase (CMS) catalyzes the conversion of pyruvate and acetyl-CoA to (R)-citramalate in the first dedicated step of the citramalate pathway. Citramalate is only found in Leptospira interrogans and a few other microorganisms. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163683 [Multi-domain] Cd Length: 280 Bit Score: 53.92 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 715 NLEYYLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFPDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDVAS 794
Cdd:cd07945 145 SPDYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFHAHNDYDLAVANVLAAVKAGIKGLHTTV 224
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 570336760 795 DAMSGTTSQPSMGAVVAALKG-SKYDTGVNAEDIMEINDYWETMRGVYAP 843
Cdd:cd07945 225 NGLGERAGNAPLASVIAVLKDkLKVKTNIDEKRLNRASRLVETFSGKRIP 274
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1113-1178 |
2.32e-07 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 49.36 E-value: 2.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 570336760 1113 VGAPMP------GVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEI 1178
Cdd:cd06663 2 ILIPDLaqhlgdGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1119-1178 |
2.81e-07 |
|
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: 48.91 E-value: 2.81e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1119 GVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEI 1178
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
89-358 |
5.17e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 54.20 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 89 LDIDSIIQIAKENNIDAIHPGYGFLSENvGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGtdGPVHT 168
Cdd:PRK12815 617 LTLEDVLNVAEAENIKGVIVQFGGQTAI-NLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATD 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 169 LEEARAFIDSgVGYPVIIKASMGGGGRGMRVVNRAEDLEENFERASSealaafGDGTVFIERYVDrPRHIEVQILGDGQ- 247
Cdd:PRK12815 694 EEEAFAFAKR-IGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENAS------QLYPILIDQFID-GKEYEVDAISDGEd 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 248 ----GNVVHL----YHRDCSVqrrhqKVLetaPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVdQQGRHYFIEVN 319
Cdd:PRK12815 766 vtipGIIEHIeqagVHSGDSI-----AVL---PPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL-ANDEIYVLEVN 836
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 570336760 320 PRiqVEHT--ITEEITGIDLVQSQIRIAGGETFKDLGLSQD 358
Cdd:PRK12815 837 PR--ASRTvpFVSKATGVPLAKLATKVLLGKSLAELGYPNG 875
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
715-830 |
8.95e-07 |
|
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; Isopropylmalate/homocitrate/citramalate synthases is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439889 [Multi-domain] Cd Length: 452 Bit Score: 52.86 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 715 NLEYYLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFPDLPIHVHTHDTAGTGVSSMLEAAYAGADAVdvas 794
Cdd:COG0119 146 DPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHNDLGLAVANSLAAVEAGADQV---- 221
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 570336760 795 damSGT-------TSQPSMGAVVAALKgSKY--DTGVNAEDIMEI 830
Cdd:COG0119 222 ---EGTingigerAGNAALEEVVMNLK-LKYgvDTGIDLSKLTEL 262
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
77-320 |
9.32e-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: 52.03 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 77 LVGAGKSPVGAYLDIDSIIQIAKENNID----AIHPGYGflsENV---GFAEQCaknGIKFVGPTPENLQRFGDKTAARE 149
Cdd:COG1181 28 LDKAGYDVVPIGIDVEDLPAALKELKPDvvfpALHGRGG---EDGtiqGLLELL---GIPYTGSGVLASALAMDKALTKR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 150 IAIEQKVPVVPG---TDGPVHTLEEarafIDSGVGYPVIIKASmggggrgmrvvN--------RAEDLEEnFERASSEAL 218
Cdd:COG1181 102 VLAAAGLPTPPYvvlRRGELADLEA----IEEELGLPLFVKPA-----------RegssvgvsKVKNAEE-LAAALEEAF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 219 AafGDGTVFIERYVDrPRHIEVQILGDGQGNVVHL---------------YHRDcsvqrrhqKVLETAPAvGLDPKTEKA 283
Cdd:COG1181 166 K--YDDKVLVEEFID-GREVTVGVLGNGGPRALPPieivpengfydyeakYTDG--------GTEYICPA-RLPEELEER 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 570336760 284 MIDDAVRltsAAKYLNA---GTVEFLVDQQGRHYFIEVNP 320
Cdd:COG1181 234 IQELALK---AFRALGCrgyARVDFRLDEDGEPYLLEVNT 270
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
720-843 |
6.19e-06 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 50.32 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 720 LDFVRQLVAQGIHVLA----IKDMAGLLKPQAAQILISAIRNEfPDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDVASD 795
Cdd:PRK09389 142 LDFLKELYKAGIEAGAdricFCDTVGILTPEKTYELFKRLSEL-VKGPVSIHCHNDFGLAVANTLAALAAGADQVHVTIN 220
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 570336760 796 AMSGTTSQPSMGAVVAALK-GSKYDTGVNAEDIMEINDYWETMRGVYAP 843
Cdd:PRK09389 221 GIGERAGNASLEEVVMALKhLYDVETGIKLEELYELSRLVSRLTGIPVP 269
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
723-832 |
1.44e-05 |
|
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy 2-ketovalerate aldolase (Also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. This family includes the Escherichia coli MhpE aldolase, the Pseudomonas DmpG aldolase, and the Burkholderia xenovorans BphI pyruvate aldolase. In Pseudomonas, the DmpG aldolase tightly associates with a dehydrogenase (DmpF ) and is inactive without it. HOA has a canonical TIM-barrel fold with a C-terminal extension that forms a funnel leading to the active site. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163681 Cd Length: 263 Bit Score: 47.88 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 723 VRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFPDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDVASDAM---SG 799
Cdd:cd07943 147 AKLMESYGADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATRIDGSLAGLgagAG 226
|
90 100 110
....*....|....*....|....*....|...
gi 570336760 800 TTsqpSMGAVVAALKGSKYDTGVNAEDIMEIND 832
Cdd:cd07943 227 NT---PLEVLVAVLERMGIETGIDLYKLMDAAE 256
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
120-362 |
2.59e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 48.55 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 120 AEQCAKNGIKFVGPTPENL------QRFGDktAAREIAIEQkvPvvPGtdGPVHTLEEARAFIDSgVGYPVIIKASMGGG 193
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAIdlaedrERFSK--LLEKLGIPQ--P--PN--GTATSVEEALEVAEE-IGYPVLVRPSYVLG 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 194 GRGMRVVNRAEDLEENFErassEALAAFGDGTVFIERYVDRPRHIEVQILGDGQgNVV------Hlyhrdcsvqrrhqkv 267
Cdd:PRK05294 717 GRAMEIVYDEEELERYMR----EAVKVSPDHPVLIDKFLEGAIEVDVDAICDGE-DVLiggimeH--------------- 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 268 LETA-----------PAVGLDPKTEKAMIDDAVRLtsaAKYLN-AG--TVEFLVdQQGRHYFIEVNPRiqVEHTI--TEE 331
Cdd:PRK05294 777 IEEAgvhsgdsacslPPQTLSEEIIEEIREYTKKL---ALELNvVGlmNVQFAV-KDDEVYVIEVNPR--ASRTVpfVSK 850
|
250 260 270
....*....|....*....|....*....|.
gi 570336760 332 ITGIDLVQSQIRIAGGETFKDLGLSQDKIKP 362
Cdd:PRK05294 851 ATGVPLAKIAARVMLGKKLAELGYTKGLIPP 881
|
|
| PRK05692 |
PRK05692 |
hydroxymethylglutaryl-CoA lyase; Provisional |
709-839 |
3.07e-05 |
|
hydroxymethylglutaryl-CoA lyase; Provisional
Pssm-ID: 180206 Cd Length: 287 Bit Score: 47.19 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 709 PTRGPYNLEYYLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFPDLPIHVHTHDTAGTGVSSMLEAAYAGAD 788
Cdd:PRK05692 147 PYEGEVPPEAVADVAERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAEFPAERLAGHFHDTYGQALANIYASLEEGIT 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 570336760 789 AVDVASDAMSGTTSQPsmGA--------VVAALKGSKYDTGVNAEDIMEINDYWETMRG 839
Cdd:PRK05692 227 VFDASVGGLGGCPYAP--GAsgnvatedVLYMLHGLGIETGIDLDKLVRAGQFIQSKLG 283
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
97-189 |
5.01e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 47.78 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 97 IAKENnIDAIHPGYG---------FLSENvGFAEqcaKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGtdGPVH 167
Cdd:PRK05294 78 IEKER-PDAILPTMGgqtalnlavELAES-GVLE---KYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRS--GIAH 150
|
90 100
....*....|....*....|..
gi 570336760 168 TLEEARAFIDSgVGYPVIIKAS 189
Cdd:PRK05294 151 SMEEALEVAEE-IGYPVIIRPS 171
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
708-830 |
1.72e-04 |
|
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate synthase (IPMS) catalyzes an aldol-type condensation of acetyl-CoA and 2-oxoisovalerate yielding 2-isopropylmalate and CoA, the first committed step in leucine biosynthesis. This family includes the Arabidopsis thaliana IPMS1 and IPMS2 proteins, the Glycine max GmN56 protein, and the Brassica insularis BatIMS protein. This family also includes a group of archeal IPMS-like proteins represented by the Methanocaldococcus jannaschii AksA protein. AksA catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form trans-homoaconitate, one of 13 steps in the conversion of alpha-ketoglutarate and acetylCoA to alpha-ketosuberate, a precursor to coenzyme B and biotin. AksA also catalyzes the condensation of alpha-ketoadipate or alpha-ketopimelate with acetylCoA to form, respectively, the (R)-homocitrate homologs (R)-2-hydroxy-1,2,5-pentanetricarboxylic acid and (R)-2-hydroxy-1,2,6- hexanetricarboxylic acid. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163678 Cd Length: 268 Bit Score: 44.75 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 708 DPTRGPynLEYYLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFP--DLPIHVHTHDTAGTGVSSMLEAAYA 785
Cdd:cd07940 136 DATRTD--LDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVPniKVPISVHCHNDLGLAVANSLAAVEA 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 570336760 786 GADAVDVASDAM---SGTTsqpSMGAVVAALK----GSKYDTGVNAEDIMEI 830
Cdd:cd07940 214 GARQVECTINGIgerAGNA---ALEEVVMALKtrydYYGVETGIDTEELYET 262
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1121-1185 |
1.93e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 45.58 E-value: 1.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 570336760 1121 VLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEIDETGDDD 1185
Cdd:PRK11855 18 VIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAGAAA 82
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1091-1184 |
2.03e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 45.38 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1091 VKDEAAGVSTAVKPKATGLPGSVGAPMPGV----VLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVG 1166
Cdd:PRK11854 86 AQAEEKKEAAPAAAPAAAAAKDVHVPDIGSdeveVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVG 165
|
90
....*....|....*...
gi 570336760 1167 DNMLGGDLLVEIDETGDD 1184
Cdd:PRK11854 166 DKVSTGSLIMVFEVAGEA 183
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
708-840 |
2.11e-04 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 45.17 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 708 DPTRGPynLEYYLDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRnEFPDLPIHVHTHDTAGTGVSSMLEAAYAGA 787
Cdd:PRK11858 138 DASRTD--LDFLIEFAKAAEEAGADRVRFCDTVGILDPFTMYELVKELV-EAVDIPIEVHCHNDFGMATANALAGIEAGA 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 570336760 788 DAVDV--------ASDAmsgttsqpSMGAVVAALKGS-KYDTGVNAEDIMEINDYWETMRGV 840
Cdd:PRK11858 215 KQVHTtvnglgerAGNA--------ALEEVVMALKYLyGIDLGIDTERLYELSRLVSKASGI 268
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
88-339 |
2.38e-04 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 44.55 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 88 YLDIDSIIQIAKENNI---DAI-----HPGYGFlsenvGFAEQCAKNGIKFVGPtPENLQRFGDKTAAREIAIEQKVPVv 159
Cdd:COG0189 39 TLDLGRAPELYRGEDLsefDAVlpridPPFYGL-----ALLRQLEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPV- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 160 pgtdgP----VHTLEEARAFIDSgVGYPVIIKASMGGGGRGMRVVNRAEDLEENFerassEALAAFGDGTVFIERYVDRP 235
Cdd:COG0189 112 -----PptlvTRDPDDLRAFLEE-LGGPVVLKPLDGSGGRGVFLVEDEDALESIL-----EALTELGSEPVLVQEFIPEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 236 RHIEVQI--LGdgqGNVVHLYHRDCSVQ--RRHQKVLETAPAVGLDPKtekaMIDDAVRLTSAAKYLNAGtVEFLVDQQG 311
Cdd:COG0189 181 DGRDIRVlvVG---GEPVAAIRRIPAEGefRTNLARGGRAEPVELTDE----ERELALRAAPALGLDFAG-VDLIEDDDG 252
|
250 260
....*....|....*....|....*...
gi 570336760 312 rHYFIEVNPRIQVEHtiTEEITGIDLVQ 339
Cdd:COG0189 253 -PLVLEVNVTPGFRG--LERATGVDIAE 277
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1121-1179 |
2.48e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 45.20 E-value: 2.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 570336760 1121 VLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEID 1179
Cdd:PRK11855 135 VIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
1115-1180 |
2.71e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 40.77 E-value: 2.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 570336760 1115 APMPGVVL-------DVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEIDE 1180
Cdd:PRK07051 8 SPLPGTFYrrpspdaPPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
89-322 |
4.42e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 44.57 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 89 LDIDSIIQIAKENNIDAIHPGYG---FLSENVGFAEQ--CAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVvpGTD 163
Cdd:PRK12815 69 LTVEFVKRIIAREKPDALLATLGgqtALNLAVKLHEDgiLEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPV--PES 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 164 GPVHTLEEARAFIDSgVGYPVIIKASMGGGGRGMRVVNRAEDLEENFERAssEALAAFGDgtVFIERYVDRPRHIEVQIL 243
Cdd:PRK12815 147 EIVTSVEEALAFAEK-IGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQG--LQASPIHQ--CLLEESIAGWKEIEYEVM 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 244 GDGQGNVVHLyhrdCSVQRrhqkvLE-----------TAPAVGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQG- 311
Cdd:PRK12815 222 RDRNGNCITV----CNMEN-----IDpvgihtgdsivVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSk 292
|
250
....*....|.
gi 570336760 312 RHYFIEVNPRI 322
Cdd:PRK12815 293 QYYLIEVNPRV 303
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1088-1182 |
5.89e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 43.84 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 1088 VIKVKDEAAGVSTAVKPKATGLPGSVGAP------MP------GVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVS 1155
Cdd:PRK11854 176 VFEVAGEAPAAAPAAAEAAAPAAAPAAAAgvkdvnVPdiggdeVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFA 255
|
90 100
....*....|....*....|....*..
gi 570336760 1156 GRVVSIHADVGDNMLGGDLLVEIDETG 1182
Cdd:PRK11854 256 GTVKEIKVNVGDKVKTGSLIMRFEVEG 282
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
170-320 |
9.77e-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: 41.92 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 170 EEARAFIDSGVGYPVIIKASMGGGGRGMRVVNRAEDLEENFERASSEalaafgDGTVFIERYVDrPRHIEVQILGDGQgN 249
Cdd:pfam07478 25 KEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQY------DEKVLVEEGIE-GREIECAVLGNED-P 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 250 VVHLYHR---DCSVQRRHQKVLETA-----PAvGLDPKTEKAMIDDAVRltsAAKYLNA---GTVEFLVDQQGRHYFIEV 318
Cdd:pfam07478 97 EVSPVGEivpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALK---AYKALGCrglARVDFFLTEDGEIVLNEV 172
|
..
gi 570336760 319 NP 320
Cdd:pfam07478 173 NT 174
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
276-348 |
1.08e-03 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 42.60 E-value: 1.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 570336760 276 LDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQqGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAGGE 348
Cdd:COG2232 218 LPPALAEEMRAIAEALVAALGLVGLNGVDFILDG-DGPYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRGE 289
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
90-188 |
1.27e-03 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 42.69 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 90 DIDSIIQIAKENNIDAIHPGygflSEN---VGFAEQCAKNGIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPG---TD 163
Cdd:COG0151 50 DIEALVAFAKEENIDLVVVG----PEAplvAGIVDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYrvfTD 125
|
90 100
....*....|....*....|....*
gi 570336760 164 gpvhtLEEARAFIDSgVGYPVIIKA 188
Cdd:COG0151 126 -----LEEALAYLEE-QGAPIVVKA 144
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
85-317 |
1.40e-03 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 42.37 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 85 VGAYLDIDSIIQIAKenNIDAIhpgyGFLSENVGFA--EQCAKngIKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGT 162
Cdd:COG0026 37 VADYDDEEALREFAE--RCDVV----TFEFENVPAEalEALEA--EVPVRPGPEALEIAQDRLLEKAFLAELGIPVAPFA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 163 dgPVHTLEEARAFIDSgVGYPVIIKASmggggrgmrvvnR-------------AEDLEenferassEALAAFGDGTVFIE 229
Cdd:COG0026 109 --AVDSLEDLEAAIAE-LGLPAVLKTR------------RggydgkgqvviksAADLE--------AAWAALGGGPCILE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 230 RYVD--RprhiEVQILG----DGQGN---VVHLYHRDcsvqrrHQKVLETAPAvGLDPKTEKAMIDDAVRLTSAAKYLna 300
Cdd:COG0026 166 EFVPfeR----ELSVIVarspDGEVAtypVVENVHRN------GILDESIAPA-RISEALAAEAEEIAKRIAEALDYV-- 232
|
250 260 270
....*....|....*....|....*....|...
gi 570336760 301 GT--VEFLVDQQGR--------------HYFIE 317
Cdd:COG0026 233 GVlaVEFFVTKDGEllvneiaprphnsgHWTIE 265
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1119-1180 |
1.86e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 42.30 E-value: 1.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 570336760 1119 GVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEIDE 1180
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFES 76
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
128-411 |
1.92e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.46 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 128 IKFVGPTPENLQRFGDKTAAREIAIEQKVPVVPGtdGPVHTLEEARAfIDSGVGYPVIIKASMGGGGRGMRVVNRAEDLE 207
Cdd:PLN02735 687 VKIWGTSPDSIDAAEDRERFNAILNELKIEQPKG--GIARSEADALA-IAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLK 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 208 ENFErassEALAAFGDGTVFIERYVDRPRHIEVQILGDGQGNVV-------------HLYHRDCSVQRRhqkvleTAPAV 274
Cdd:PLN02735 764 TYLE----TAVEVDPERPVLVDKYLSDATEIDVDALADSEGNVViggimehieqagvHSGDSACSLPTQ------TIPSS 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 275 GLDpktekaMIDDAVrlTSAAKYLNAG---TVEFLVDQQGRHYFIEVNPRIQVEHTITEEITGIDLVQSQIRIAGGETFK 351
Cdd:PLN02735 834 CLA------TIRDWT--TKLAKRLNVCglmNCQYAITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSGKSLK 905
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 570336760 352 DLGLSQDkIKPRGHAMQCRVTtenPSTGFQ-PDSGVIEVFRSPG-GMGIRLDDGPGFVGAHI 411
Cdd:PLN02735 906 DLGFTEE-VIPAHVSVKEAVL---PFDKFQgCDVLLGPEMRSTGeVMGIDYEFSKAFAKAQI 963
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1147-1181 |
3.58e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.80 E-value: 3.58e-03
10 20 30
....*....|....*....|....*....|....*
gi 570336760 1147 ETVVAAPVSGRVVSIHADVGDNMLGGDLLVEIDET 1181
Cdd:COG1566 45 VVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPT 79
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
1119-1182 |
4.87e-03 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 40.82 E-value: 4.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 570336760 1119 GVVLDVRVKKGENVKAGDALLVLSAMKMETVVAAPVSGRVVSIHADVGDNMLGGDLLVEIDETG 1182
Cdd:PTZ00144 59 GTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGG 122
|
|
| DRE_TIM_HCS |
cd07948 |
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ... |
720-792 |
6.25e-03 |
|
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel domain; Homocitrate synthase (HCS) catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate, the first step in the lysine biosynthesis pathway. This family includes the Yarrowia lipolytica LYS1 protein as well as the Saccharomyces cerevisiae LYS20 and LYS21 proteins. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163685 Cd Length: 262 Bit Score: 40.01 E-value: 6.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 570336760 720 LDFVRQLVAQGIHVLAIKDMAGLLKPQAAQILISAIRNEFpDLPIHVHTHDTAGTGVSSMLEAAYAGADAVDV 792
Cdd:cd07948 144 LRVYRAVDKLGVNRVGIADTVGIATPRQVYELVRTLRGVV-SCDIEFHGHNDTGCAIANAYAALEAGATHIDT 215
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
165-321 |
7.14e-03 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 38.77 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 165 PVHTLEEARAFIDSgVGYPVIIKASMGGGGRG-MRVVNRAEDLEEnferasseALAAFGDGTVFIERYVDRPRHIEVQIL 243
Cdd:pfam02222 12 AAESLEELIEAGQE-LGYPCVVKARRGGYDGKgQYVVRSEADLPQ--------AWEELGDGPVIVEEFVPFDRELSVLVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 570336760 244 GDGQGN-----VVHLYHRD--CsvqrrhqkVLETAPAvGLDPKTEKAMIDDAVRLTSAAKYLNAGTVEFLVDQQGRHYFI 316
Cdd:pfam02222 83 RSVDGEtafypVVETIQEDgiC--------RLSVAPA-RVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLIN 153
|
....*
gi 570336760 317 EVNPR 321
Cdd:pfam02222 154 ELAPR 158
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1112-1141 |
8.03e-03 |
|
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: 36.24 E-value: 8.03e-03
10 20 30
....*....|....*....|....*....|
gi 570336760 1112 SVGAPMPGVVLDVRVKKGENVKAGDALLVL 1141
Cdd:cd06850 38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| |
