|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
38-1179 |
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: 1911.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 38 PIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLSPVAAYLHIPDIIKVAKENNVDAIH 117
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 118 PGYGFLSERADFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPIIFKA 197
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 198 A-----------YggggrgmrvvrNYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVIHLYERD 266
Cdd:COG1038 163 AaggggrgmrvvR-----------SEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 267 CSIQRRHQKVVEIAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDL 346
Cdd:COG1038 232 CSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 347 VHAQLRVCEGRSL--PELGL-EQDKIQINGCAIQCRVTTEDPSRGFQPDTGRIEVFRSGEGMGIRLDSASAFQGAIISPH 423
Cdd:COG1038 312 VQSQILIAEGYSLddPEIGIpSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 424 YDSLLVKVIASGKDLPTAATKMHRALTEFRVRGVKTNIPFLQNVLSNSQFLYATVDTQFIDENQNLFNLKPTQNRAQKLL 503
Cdd:COG1038 392 YDSLLVKVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 504 HYLGHVMVNGPMTpIPVKAKPSPVDPVIPSVSLGEPPL-GFREVLLREGPEGFARAIRQHQGLLLMDTTFRDAHQSLLAT 582
Cdd:COG1038 472 TYLGDVTVNGPPG-VKGRPKPDFPKPKLPKVDLGAPPPkGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLAT 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 583 RVRTHDLKKIAPYVSHNFSNLFSLENWGGATFDVAMRFLSECPWKRLQELRALIPNVPFQMLLRGANAVGYTNYPDNAVF 662
Cdd:COG1038 551 RVRTRDMLKIAPATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVR 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 663 KFCEVAKENGMDIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISYTGDVSDPMRQKYSLDYYLKLADELVKAGTHILSI 742
Cdd:COG1038 631 AFVKEAAEAGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAI 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 743 KDMAGLLKPQASRLLIEALRDRFpDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVDSMAGMTSQPSMGAIVACTKGT 822
Cdd:COG1038 711 KDMAGLLKPYAAYKLVKALKEEV-DLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGT 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 823 KLDTGISLDKVFDYSEYWEVARGLYAPFDctATMKSGNADVYENEIPGGQYTNLHFQAHSMGLGNKFKEVKKAYTEANKL 902
Cdd:COG1038 790 ERDTGLDLDALQELSNYWEAVRKYYAPFE--SGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRL 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 903 LGDLIKVTPSSKIVGDLAQFMVQNSLSLAEVEKRADELSFPLSVVEFLQGHIGIPHGGFPEPFRSKVLKSLPRIEGRPGA 982
Cdd:COG1038 868 FGDIVKVTPSSKVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGE 947
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 983 SLPPMDFEALESGLRAAHGDEITPEDVMSAAMYPKVFQEFKEFTSTFGPVDCLNTRLFLDGPKIAEEFQVELERGKILHI 1062
Cdd:COG1038 948 LLPPVDFDALRAELEEKLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLII 1027
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 1063 KALALGDLNKSGQREVFFELNGQLRSVLVKDTAAMKEMHFHPKALKDVRGQVGAPMPGKVVEVKVKAGQKVEKGQPLCVL 1142
Cdd:COG1038 1028 KLLAIGEPDEDGMRTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTI 1107
|
1130 1140 1150
....*....|....*....|....*....|....*..
gi 922960042 1143 SAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:COG1038 1108 EAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
38-1179 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 1805.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 38 PIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLSPVAAYLHIPDIIKVAKENNVDAIH 117
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 118 PGYGFLSERADFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPIIFKA 197
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 198 AYGGGGRGMRVVRNYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVIHLYERDCSIQRRHQKVV 277
Cdd:PRK12999 164 SAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 278 EIAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRVCEGR 357
Cdd:PRK12999 244 EIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 358 SLPELG---LEQDKIQINGCAIQCRVTTEDPSRGFQPDTGRIEVFRSGEGMGIRLDSASAFQGAIISPHYDSLLVKVIAS 434
Cdd:PRK12999 324 TLHDLEigiPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDSLLVKLTAW 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 435 GKDLPTAATKMHRALTEFRVRGVKTNIPFLQNVLSNSQFLYATVDTQFIDENQNLFNLKPTQNRAQKLLHYLGHVMVNGP 514
Cdd:PRK12999 404 GRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTVNGF 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 515 mtPIPVKAKPSPVDPVIPSVSLGEP-PLGFREVLLREGPEGFARAIRQHQGLLLMDTTFRDAHQSLLATRVRTHDLKKIA 593
Cdd:PRK12999 484 --PGVKKKPPVFPDPRLPKVDLSAPpPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLLRIA 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 594 PYVSHNFSNLFSLENWGGATFDVAMRFLSECPWKRLQELRALIPNVPFQMLLRGANAVGYTNYPDNAVFKFCEVAKENGM 673
Cdd:PRK12999 562 PATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAAAGI 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 674 DIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISYTGDVSDPMRQKYSLDYYLKLADELVKAGTHILSIKDMAGLLKPQA 753
Cdd:PRK12999 642 DVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMAGLLKPAA 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 754 SRLLIEALRDRFpDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVDSMAGMTSQPSMGAIVACTKGTKLDTGISLDKV 833
Cdd:PRK12999 722 AYELVSALKEEV-DLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDLDAI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 834 FDYSEYWEVARGLYAPFdcTATMKSGNADVYENEIPGGQYTNLHFQAHSMGLGNKFKEVKKAYTEANKLLGDLIKVTPSS 913
Cdd:PRK12999 801 RKLSPYWEAVRPYYAPF--ESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVTPSS 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 914 KIVGDLAQFMVQNSLSLAEVEKRADELSFPLSVVEFLQGHIGIPHGGFPEPFRSKVLKSLPRIEGRPGASLPPMDFEALE 993
Cdd:PRK12999 879 KVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDFEAER 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 994 SGLRAAHGDEITPEDVMSAAMYPKVFQEFKEFTSTFGPVDCLNTRLFLDGPKIAEEFQVELERGKILHIKALALGDLNKS 1073
Cdd:PRK12999 959 AELEEKLGREVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEPDED 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 1074 GQREVFFELNGQLRSVLVKDTAAMKEMHFHPKALKDVRGQVGAPMPGKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNS 1153
Cdd:PRK12999 1039 GMRTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITA 1118
|
1130 1140
....*....|....*....|....*.
gi 922960042 1154 PISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:PRK12999 1119 PVDGTVKRVLVKAGDQVEAGDLLVEL 1144
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
41-1179 |
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: 1713.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 41 KVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRG--LSPVAAYLHIPDIIKVAKENNVDAIHP 118
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 119 GYGFLSERADFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPIIFKAA 198
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 199 YGGGGRGMRVVRNYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVIHLYERDCSIQRRHQKVVE 278
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 279 IAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRVCEGRS 358
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 359 LP--ELGL-EQDKIQINGCAIQCRVTTEDPSRGFQPDTGRIEVFRSGEGMGIRLDSASAFQGAIISPHYDSLLVKVIASG 435
Cdd:TIGR01235 321 LPtpQLGVpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 436 KDLPTAATKMHRALTEFRVRGVKTNIPFLQNVLSNSQFLYATVDTQFIDENQNLFNLKPTQNRAQKLLHYLGHVMVNGpM 515
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNG-H 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 516 TPIPVKAKPSPVDP--VIPSVSLGEPPLGFREVLLREGPEGFARAIRQHQGLLLMDTTFRDAHQSLLATRVRTHDLKKIA 593
Cdd:TIGR01235 480 PEAKDKLKPLENAPrvVVLYADQNPVPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 594 PYVSHNFSNLFSLENWGGATFDVAMRFLSECPWKRLQELRALIPNVPFQMLLRGANAVGYTNYPDNAVFKFCEVAKENGM 673
Cdd:TIGR01235 560 PTTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGI 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 674 DIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISYTGDVSDPMRQKYSLDYYLKLADELVKAGTHILSIKDMAGLLKPQA 753
Cdd:TIGR01235 640 DIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLLKPAA 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 754 SRLLIEALRDRFpDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVDSMAGMTSQPSMGAIVACTKGTKLDTGISLDKV 833
Cdd:TIGR01235 720 AKLLIKALREKT-DLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVAWI 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 834 FDYSEYWEVARGLYAPFDCtaTMKSGNADVYENEIPGGQYTNLHFQAHSMGLGNKFKEVKKAYTEANKLLGDLIKVTPSS 913
Cdd:TIGR01235 799 RELSAYWEAVRNLYAAFES--DLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSS 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 914 KIVGDLAQFMVQNSLSLAEVEKRADELSFPLSVVEFLQGHIGIPHGGFPEPFRSKVLKSLPRIEGRPGASLPPMDFEALE 993
Cdd:TIGR01235 877 KVVGDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAIR 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 994 SGLRAAHGDEITPEDVMSAAMYPKVFQEFKEFTSTFGPVDCLNTRLFLDGPKIAEEFQVELERGKILHIKALALGDLNKS 1073
Cdd:TIGR01235 957 KDLQEKHEREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQ 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 1074 GQREVFFELNGQLRSVLVKDTAAMKEMHFHPKALKDVRGQVGAPMPGKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNS 1153
Cdd:TIGR01235 1037 GEREVFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQA 1116
|
1130 1140
....*....|....*....|....*.
gi 922960042 1154 PISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:TIGR01235 1117 PKDGTIKEVLVKAGEQIDAKDLLLVL 1142
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
38-499 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 685.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 38 PIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGrGLSPVAAYLHIPDIIKVAKENNVDAIH 117
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIG-PAPAAESYLNIDAIIAAAKATGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 118 PGYGFLSERADFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPIIFKA 197
Cdd:COG4770 80 PGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 198 A-----------YggggrgmrvvrNYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVIHLYERD 266
Cdd:COG4770 160 SaggggkgmrvvR-----------SEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 267 CSIQRRHQKVVEIAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDL 346
Cdd:COG4770 229 CSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 347 VHAQLRVCEGRSLPelgLEQDKIQINGCAIQCRVTTEDPSRGFQPDTGRIEVFRSGEGMGIRLDSAsAFQGAIISPHYDS 426
Cdd:COG4770 309 VEEQIRIAAGEPLP---FTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDS 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922960042 427 LLVKVIASGKDLPTAATKMHRALTEFRVRGVKTNIPFLQNVLSNSQFLYATVDTQFIDENQNLFNLKPTQNRA 499
Cdd:COG4770 385 MIAKLIVWGPDREEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEEL 457
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
39-486 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 604.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 39 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLSPvAAYLHIPDIIKVAKENNVDAIHP 118
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSK-KSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 119 GYGFLSERADFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPIIFKAA 198
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 199 YGGGGRGMRVVRNYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVIHLYERDCSIQRRHQKVVE 278
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 279 IAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRVCEGRS 358
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 359 LPelgLEQDKIQINGCAIQCRVTTEDPSRGFQPDTGRIEVFRSGEGMGIRLDSAsAFQGAIISPHYDSLLVKVIASGKDL 438
Cdd:PRK08591 321 LS---IKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMIGKLIVHGETR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 922960042 439 PTAATKMHRALTEFRVRGVKTNIPFLQNVLSNSQFLYATVDTQFIDEN 486
Cdd:PRK08591 397 EEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
40-489 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 563.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 40 KKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlSPVAAYLHIPDIIKVAKENNVDAIHPG 119
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPA-PPSKSYLNIERIIDVAKKAGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 120 YGFLSERADFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPIIFKAAY 199
Cdd:PRK08654 82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 200 GGGGRGMRVVRNYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVIHLYERDCSIQRRHQKVVEI 279
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 280 APAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKhGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRVCEGRSL 359
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSN-GNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 360 PelgLEQDKIQINGCAIQCRVTTEDPSRGFQPDTGRIEVFRSGEGMGIRLDSaSAFQGAIISPHYDSLLVKVIASGKDLP 439
Cdd:PRK08654 321 S---FKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDS-GVHMGYEIPPYYDSMISKLIVWGRTRE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 922960042 440 TAATKMHRALTEFRVRGVKTNIPFLQNVLSNSQFLYATVDTQFIDENQNL 489
Cdd:PRK08654 397 EAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTI 446
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
39-483 |
3.52e-180 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 536.15 E-value: 3.52e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 39 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGrGLSPVAAYLHIPDIIKVAKENNVDAIHP 118
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIG-GPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 119 GYGFLSERADFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPIIFKAA 198
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 199 YGGGGRGMRVVRNYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVIHLYERDCSIQRRHQKVVE 278
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 279 IAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRVCEGRS 358
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 359 LPelgLEQDKIQINGCAIQCRVTTEDPSRgFQPDTGRIEVFRSGEGMGIRLDSASAfQGAIISPHYDSLLVKVIASGKDL 438
Cdd:PRK06111 321 LS---FTQDDIKRSGHAIEVRIYAEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVE-NGVTVTPFYDPMIAKLIAHGETR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 922960042 439 PTAATKMHRALTEFRVRGVKTNIPFLQNVLSNSQFLYATVDTQFI 483
Cdd:PRK06111 396 EEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
39-491 |
4.21e-174 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 521.20 E-value: 4.21e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 39 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRglSPVAAYLHIPDIIKVAKENNVDAIHP 118
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGA--DPLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 119 GYGFLSERADFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPIIFKAA 198
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 199 YGGGGRGMRVVRNYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVIHLYERDCSIQRRHQKVVE 278
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 279 IAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRVCEGRS 358
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 359 LPelgLEQDKIQINGCAIQCRVTTEDPSRGFQPDTGRIEVFRSGEGMGIRLDSAsAFQGAIISPHYDSLLVKVIASGKDL 438
Cdd:PRK07178 320 LS---YKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTA-IYTGYTIPPYYDSMCAKLIVWALTW 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 922960042 439 PTAATKMHRALTEFRVRGVKTNIPFLQNVLSNSQFLYATVDTQFIDENQNLFN 491
Cdd:PRK07178 396 EEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTN 448
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
39-485 |
8.32e-170 |
|
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: 509.30 E-value: 8.32e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 39 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLSpVAAYLHIPDIIKVAKENNVDAIHP 118
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPS-AKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 119 GYGFLSERADFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPIIFKAA 198
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 199 YGGGGRGMRVVRNYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVIHLYERDCSIQRRHQKVVE 278
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 279 IAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRVCEGRS 358
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 359 LPelgLEQDKIQINGCAIQCRVTTEDPSRGFQPDTGRIEVFRSGEGMGIRLDSAsAFQGAIISPHYDSLLVKVIASGKDL 438
Cdd:TIGR00514 321 LS---LKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSH-VYSGYTVPPYYDSMIGKLITYGKTR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 922960042 439 PTAATKMHRALTEFRVRGVKTNIPFLQNVLSNSQFLYATVDTQFIDE 485
Cdd:TIGR00514 397 EVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
39-486 |
1.10e-168 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 506.17 E-value: 1.10e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 39 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlSPVAAYLHIPDIIKVAKENNVDAIHP 118
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPA-SSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 119 GYGFLSERADFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPIIFKAA 198
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 199 YGGGGRGMRVVRNYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVIHLYERDCSIQRRHQKVVE 278
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 279 IAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRVCEGRs 358
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 359 lpELGLEQDKIQINGCAIQCRVTTEDPSRGFQPDTGRIEVFRSGEGMGIRLDSAsAFQGAIISPHYDSLLVKVIASGKDL 438
Cdd:PRK05586 320 --KLSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSA-VYSGYTIPPYYDSMIGKLIVYGKDR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 922960042 439 PTAATKMHRALTEFRVRGVKTNIPFLQNVLSNSQFLYATVDTQFIDEN 486
Cdd:PRK05586 397 EEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKK 444
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
38-484 |
1.31e-156 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 475.40 E-value: 1.31e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 38 PIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGrglsPVAA---YLHIPDIIKVAKENNVD 114
Cdd:PRK12833 4 RIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIG----PSHAaksYLNPAAILAAARQCGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 115 AIHPGYGFLSERADFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPII 194
Cdd:PRK12833 80 AIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 195 FKAAYGGGGRGMRVVRNYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYgNVIHLYERDCSIQRRHQ 274
Cdd:PRK12833 160 IKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 275 KVVEIAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKH-GKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRV 353
Cdd:PRK12833 239 KILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDArGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 354 CEGRSlpeLGLEQDKIQINGCAIQCRVTTEDPSRGFQPDTGRIEVFRSGEGMGIRLDSaSAFQGAIISPHYDSLLVKVIA 433
Cdd:PRK12833 319 ADGEP---LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDS-LLYPGYRVPPFYDSLLAKLIV 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 922960042 434 SGKDLPTAATKMHRALTEFRVRGVKTNIPFLQNVLSNSQFLYATVDTQFID 484
Cdd:PRK12833 395 HGEDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
39-501 |
1.44e-152 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 465.44 E-value: 1.44e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 39 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRglSPVAAYLHIPDIIKVAKENNVDAIHP 118
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGT--DPIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 119 GYGFLSERADFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDAPISC-LQEAQEFAKTYDFPIIFKA 197
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSEsMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 198 AYGGGGRGMRVVRNYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVIHLYERDCSIQRRHQKVV 277
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 278 EIAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRVCEGR 357
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 358 SLPelgLEQDKIQINGCAIQCRVTTEDPSRGFQPDTGRIEVFRSGEGMGIRLDSaSAFQGAIISPHYDSLLVKVIASGKD 437
Cdd:PRK08463 320 ILD---LEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDS-HIYKDYTIPPYYDSMLAKLIVKATS 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922960042 438 LPTAATKMHRALTEFRVRGVKTNIPFLQNVLSNSQFLYATVDTQFIDEN-QNLfnLKPTQNRAQK 501
Cdd:PRK08463 396 YDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHmQEL--LEKTEDRHQE 458
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
567-850 |
1.67e-151 |
|
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: 454.58 E-value: 1.67e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 567 LMDTTFRDAHQSLLATRVRTHDLKKIAPYVSHNFsnLFSLENWGGATFDVAMRFLSECPWKRLQELRALIPNVPFQMLLR 646
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 647 GANAVGYTNYPDNAVFKFCEVAKENGMDIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISYTGDvsdpmrQKYSLDYYL 726
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 727 KLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFPdIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVDSMAGM 806
Cdd:cd07937 153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVG-LPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 922960042 807 TSQPSMGAIVACTKGTKLDTGISLDKVFDYSEYWEVARGLYAPF 850
Cdd:cd07937 232 TSQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
39-486 |
3.96e-151 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 460.37 E-value: 3.96e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 39 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLSPvAAYLHIPDIIKVAKENNVDAIHP 118
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSS-ESYLNIPAIISAAEIFEADAIFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 119 GYGFLSERADFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPIIFKAA 198
Cdd:PRK08462 83 GYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 199 YGGGGRGMRVVRNYEELEENYQRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVIHLYERDCSIQRRHQKVVE 278
Cdd:PRK08462 163 AGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 279 IAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRVCEGRS 358
Cdd:PRK08462 243 ESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 359 LPelglEQDKIQINGCAIQCRVTTEDPSRgFQPDTGRIEVFRSGEGMGIRLDSaSAFQGAIISPHYDSLLVKVIASGKDL 438
Cdd:PRK08462 323 LP----SQESIKLKGHAIECRITAEDPKK-FYPSPGKITKWIAPGGRNVRMDS-HAYAGYVVPPYYDSMIGKLIVWGEDR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 922960042 439 PTAATKMHRALTEFRVRGVKTNIPFLQNVLSNSQFLYATVDTQFIDEN 486
Cdd:PRK08462 397 NRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
569-1179 |
5.91e-146 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 452.37 E-value: 5.91e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 569 DTTFRDAHQSLLATRVRTHDLKKIApyvshnfSNL-----FSLENWGGATFDVAMRFLSECPWKRLQELRALIPNVPFQM 643
Cdd:PRK09282 8 DTTLRDAHQSLLATRMRTEDMLPIA-------EKLdkvgfWSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPLQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 644 LLRGANAVGYTNYPDNAVFKFCEVAKENGMDIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISYTgdVSdPMrqkYSLD 723
Cdd:PRK09282 81 LLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT--TS-PV---HTIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 724 YYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFpDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVDSM 803
Cdd:PRK09282 155 KYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEV-DLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 804 AGMTSQPSMGAIVACTKGTKLDTGISLDKVFDYSEYWEVARGLYAPFDCTATMksGNADVYENEIPGGQYTNLHFQAHSM 883
Cdd:PRK09282 234 AFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTI--VDTRVLIHQVPGGMISNLVSQLKEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 884 GLGNKFKEVKKAYTEANKLLGDLIKVTPSSKIVGDLAqfmVQNSLSlAEVEKRadelsFPLSVVEFLQGHIGIPHGGFPE 963
Cdd:PRK09282 312 NALDKLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQA---VLNVLT-GERYKV-----ITKEVKDYVKGLYGRPPAPINE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 964 PFRSKVLKSLPRIEGRPGASLPP----MDFEALESGLRaahgdeiTPEDVMSAAMYPKV----FQEFKEFTSTFGPVDCL 1035
Cdd:PRK09282 383 ELRKKIIGDEEPITCRPADLLEPelekARKEAEELGKS-------EKEDVLTYALFPQIakkfLEEREAGELKPEPEPKE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 1036 NTRlfLDGPKIAEEFQVELErGKILHIKALALGDlnkSGQREVFFELNGQLRSVLVkdtAAMKEMHFHPKALKDVRGQVG 1115
Cdd:PRK09282 456 AAA--AGAEGIPTEFKVEVD-GEKYEVKIEGVKA---EGKRPFYLRVDGMPEEVVV---EPLKEIVVGGRPRASAPGAVT 526
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922960042 1116 APMPGKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:PRK09282 527 SPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
565-1024 |
1.96e-121 |
|
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: 385.79 E-value: 1.96e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 565 LLLMDTTFRDAHQSLLATRVRTHDLKKIAPY-VSHNFsnlFSLENWGGATFDVAMRFLSECPWKRLQELRALIPNVPFQM 643
Cdd:COG5016 4 VKITDTTLRDGHQSLFATRMRTEDMLPIAEKlDEAGF---WSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 644 LLRGANAVGYTNYPDNAVFKFCEVAKENGMDIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISYTgdVSDPmrqkYSLD 723
Cdd:COG5016 81 LLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYT--ISPV----HTVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 724 YYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFpDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVDSM 803
Cdd:COG5016 155 YYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEAL-DIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 804 AGMTSQPSMGAIVACTKGTKLDTGISLDKVFDYSEYWEVARGLYAPFDCTATMKsgNADVYENEIPGGQYTNLHFQAHSM 883
Cdd:COG5016 234 AGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGV--DPRVLVHQVPGGMLSNLVSQLKEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 884 GLGNKFKEVKKAYTEANKLLGDLIKVTPSSKIVGDLAqfmVQNSLSLAEVEKRADElsfplsVVEFLQGHIGIPHGGFPE 963
Cdd:COG5016 312 GALDRLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQA---VLNVLTGERYKMITKE------VKDYVLGYYGKTPAPIDP 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922960042 964 PFRSKVLKSLPRIEGRPGASLPPMdFEALESGLRAAhgdeiTPEDVMSAAMYPKVFQEFKE 1024
Cdd:COG5016 383 EVRKKALGDEEPITCRPADLLEPE-LEKLRKEGLAK-----SDEDVLTYALFPQVAIKFLK 437
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
569-1170 |
1.96e-116 |
|
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate decarboxylase alpha subunit and its equivalents in archaea. The oxaloacetate decarboxylase Na+ pump is the paradigm of the family of Na+ transport decarboxylases that present in bacteria and archaea. It a multi subunit enzyme consisting of a peripheral alpha-subunit and integral membrane subunits beta and gamma. The energy released by the decarboxylation reaction of oxaloacetate is coupled to Na+ ion pumping across the membrane. [Transport and binding proteins, Cations and iron carrying compounds, Energy metabolism, Other]
Pssm-ID: 273447 [Multi-domain] Cd Length: 582 Bit Score: 373.74 E-value: 1.96e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 569 DTTFRDAHQSLLATRVRTHDLKKIAPYVSHnfSNLFSLENWGGATFDVAMRFLSECPWKRLQELRALIPNVPFQMLLRGA 648
Cdd:TIGR01108 3 DVVLRDAHQSLFATRMRTEDMLPIAEKLDD--VGYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLRGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 649 NAVGYTNYPDNAVFKFCEVAKENGMDIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISYTgdvSDPMrqkYSLDYYLKL 728
Cdd:TIGR01108 81 NLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT---TSPV---HTLETYLDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 729 ADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFpDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVDSMAGMTS 808
Cdd:TIGR01108 155 AEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRF-GLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGGTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 809 QPSMGAIVACTKGTKLDTGISLDKVFDYSEYWEVARGLYAPFDctATMKSGNADVYENEIPGGQYTNLHFQAHSMGLGNK 888
Cdd:TIGR01108 234 HPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFE--GQLKGPDSRILVAQVPGGMLSNLESQLKEQNALDK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 889 FKEVKKAYTEANKLLGDLIKVTPSSKIVGDLAqfmVQNSLSLAEVEKRADElsfplsVVEFLQGHIGIPHGGFPEPFRSK 968
Cdd:TIGR01108 312 LDEVLEEIPRVREDLGYPPLVTPTSQIVGTQA---VLNVLTGERYKTITKE------TKGYLKGEYGRTPAPINAELQRK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 969 VLKSL-PRIEGRPGASLPPmDFEALESGLRAAHGDEITPEDVMSAAMYPKV---FQEFKEFTSTFGPVdclntrlfLDGP 1044
Cdd:TIGR01108 383 ILGDEkPIVDCRPADLLEP-ELDKLRAEVREAGAEKNSIEDVLTYALFPQVglkFLENRHNPAAFEPK--------PEEK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 1045 KIAEEfqvelergkilHIKALALGdLNKSGQREVFFELNGQLRSVLVKD-------TAAMKEMHFHPKALKDVR--GQVG 1115
Cdd:TIGR01108 454 VIEQE-----------HAQVVGKY-EETHASGSYTVEVEGKAFVVKVSPggdvsqiTASAPANTSGGTVAAKAGagTPVT 521
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922960042 1116 APMPGKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKV------HVNADSSL 1170
Cdd:TIGR01108 522 APIAGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREIlvkvgdAVSVGQVL 582
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
565-1176 |
4.01e-97 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 321.88 E-value: 4.01e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 565 LLLMDTTFRDAHQSLLATRVRTHDLKKIAP------YvshnfsnlFSLENWGGATFDVAMRFLSECPWKRLQELRALIPN 638
Cdd:PRK14040 5 LAITDVVLRDAHQSLFATRLRLDDMLPIAAkldkvgY--------WSLESWGGATFDACIRFLGEDPWERLRELKKAMPN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 639 VPFQMLLRGANAVGYTNYPDNAVFKFCEVAKENGMDIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISYTgdVSdPMrq 718
Cdd:PRK14040 77 TPQQMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT--TS-PV-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 719 kYSLDYYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFpDIPIHVHTHDTAGAGVAAMLACAQAGADIVDV 798
Cdd:PRK14040 152 -HTLQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRV-DVPLHLHCHATTGLSTATLLKAIEAGIDGVDT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 799 AVDSMAGMTSQPSMGAIVACTKGTKLDTGISLDKVFDYSEYWEVARGLYAPFDctATMKSGNADVYENEIPGGQYTNLHF 878
Cdd:PRK14040 230 AISSMSMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFE--GQLKGVDSRILVAQVPGGMLTNMES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 879 QAHSMGLGNKFKEVKKAYTEANKLLGDLIKVTPSSKIVGDLAqfmVQNSLSLAEVEKRADELSfplsvvEFLQGHigipH 958
Cdd:PRK14040 308 QLKEQGAADKLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQA---VLNVLTGERYKTITKETA------GVLKGE----Y 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 959 GGFPEPF----RSKVLKSLPRIEGRPGASLPP-MDF-------EALESGLRAAhGDEItpEDVMSAAMYPKV---FQEFK 1023
Cdd:PRK14040 375 GATPAPVnaelQARVLEGAEPITCRPADLLAPeLDKleaelrrQAQEKGITLA-ENAI--DDVLTYALFPQIglkFLENR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 1024 EFTSTFGPVDCLNTRLFLDGPKI--AEEFQVELErGKILHIKALALGDLnksgqrevffelngqlrSVLVKDTAAMKEMH 1101
Cdd:PRK14040 452 HNPAAFEPVPQAEAAQPAAKAEPagSETYTVEVE-GKAYVVKVSEGGDI-----------------SQITPAAPAAAPAA 513
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922960042 1102 FHPKALKDVRGQ-VGAPMPGKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNA-DSSLEGEDLI 1176
Cdd:PRK14040 514 AAAAAPAAAAGEpVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEgDAVAVGDTLL 590
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
863-1063 |
7.35e-97 |
|
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: 306.69 E-value: 7.35e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 863 VYENEIPGGQYTNLHFQAHSMGLGNKFKEVKKAYTEANKLLGDLIKVTPSSKIVGDLAQFMVQNSLSLAEVEKRADELSF 942
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 943 PLSVVEFLQGHIGIPHGGFPEPFRSKVLKSLPRIEGRPGASLPPMDFEALESGLRAAHGDEITPEDVMSAAMYPKVFQEF 1022
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 922960042 1023 KEFTSTFGPVDCLNTRLFLDGPKIAEEFQVELERGKILHIK 1063
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
567-1022 |
9.50e-92 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 302.39 E-value: 9.50e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 567 LMDTTFRDAHQSLLATRVRTHDLKKIAPYVSHnfSNLFSLENWGGATFDVAMRFLSECPWKRLQELRALIPNVPFQMLLR 646
Cdd:PRK12331 6 ITETVLRDGQQSLIATRMTTEEMLPILEKLDN--AGYHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKLQMLLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 647 GANAVGYTNYPDNAVFKFCEVAKENGMDIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISYTgdvSDPMrqkYSLDYYL 726
Cdd:PRK12331 84 GQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT---TSPV---HTIDYFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 727 KLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFpDIPIHVHTHDTagAGVAAM--LACAQAGADIVDVAVDSMA 804
Cdd:PRK12331 158 KLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAV-TVPLEVHTHAT--SGIAEMtyLKAIEAGADIIDTAISPFA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 805 GMTSQPSMGAIVACTKGTKLDTGISLDKVFDYSEYWEVARGLY-APFDCTATMKSGNADVYENEIPGGQYTNLHFQAHSM 883
Cdd:PRK12331 235 GGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYrEEGILNPKVKDVEPKTLIYQVPGGMLSNLLSQLKEQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 884 GLGNKFKEVKKAYTEANKLLGDLIKVTPSSKIVGDLAqfmVQNSLSlAEVEKradelSFPLSVVEFLQGHIGIPHGGFPE 963
Cdd:PRK12331 315 GAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQA---LMNVIS-GERYK-----MVPNEIKDYVRGLYGRPPAPIAE 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 964 PFRSKVLKSLPRIEGRPGASLPPmDFEALESGLRA-AHGDeitpEDVMSAAMYPKVFQEF 1022
Cdd:PRK12331 386 EIKKKIIGDEEVITCRPADLIEP-QLEKLREEIAEyAESE----EDVLSYALFPQQAKDF 440
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
566-1162 |
2.17e-87 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 295.48 E-value: 2.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 566 LLMDTTFRDAHQSLLATRVRTHDLKKIAPYVSHnfSNLFSLENWGGATFDVAMRFLSECPWKRLQELRALIPNVPFQMLL 645
Cdd:PRK14042 5 FITDVTLRDAHQCLIATRMRTEDMLPICNKMDD--VGFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSMLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 646 RGANAVGYTNYPDNAVFKFCEVAKENGMDIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISYTgdvSDPMrqkYSLDYY 725
Cdd:PRK14042 83 RGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYT---TSPV---HTLDNF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 726 LKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRdRFPDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVDSMAG 805
Cdd:PRK14042 157 LELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLK-QATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFSG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 806 MTSQPSMGAIVACTKGTKLDTGISLDKVFDYSEYWEVARGLYAPFDCTATMKSGNADVYenEIPGGQYTNLHFQAHSMGL 885
Cdd:PRK14042 236 GASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLY--QVPGGMISNLYNQLKEQNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 886 GNKFKEVKKAYTEANKLLGDLIKVTPSSKIVGDLAqfmVQNSLSLAEVEKRADELSFplsvveFLQGHIGIPHGGFPEPF 965
Cdd:PRK14042 314 LDKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQA---VINVLTGERYKTITNEVKL------YCQGKYGTPPGKISSAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 966 RSKVLKSLPRIEGRPGaSLPPMDFEALESGLRAAhgdEITPEDVMSAAMYPKVFQEFKEFTSTFGPV-DCLNTRLFLDGP 1044
Cdd:PRK14042 385 RKKAIGRTEVIEVRPG-DLLPNELDQLQNEISDL---ALSDEDVLLYAMFPEIGRQFLEQRKNNQLIpEPLLTQSSAPDN 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 1045 KIAEEFQVELErGKILHIKALALGdLNKSGQREVFFELNGQLRSVLVKDTAAMKEMHFHPKALKDVRGQVGAPMPGKVVE 1124
Cdd:PRK14042 461 SVMSEFDIILH-GESYHVKVAGYG-MIEHGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIPGSIIA 538
|
570 580 590
....*....|....*....|....*....|....*...
gi 922960042 1125 VKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKV 1162
Cdd:PRK14042 539 IHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEI 576
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
566-1022 |
3.06e-86 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 287.84 E-value: 3.06e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 566 LLMDTTFRDAHQSLLATRVRTHDLKKIAPYVSHnfSNLFSLENWGGATFDVAMRFLSECPWKRLQELRALIPNVPFQMLL 645
Cdd:PRK14041 4 MFVDTTLRDGHQSLIATRMRTEDMLPALEAFDR--MGFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQMLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 646 RGANAVGYTNYPDNAVFKFCEVAKENGMDIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISYTgdVSdPMrqkYSLDYY 725
Cdd:PRK14041 82 RGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT--VS-PV---HTLEYY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 726 LKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFpDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVDSMAG 805
Cdd:PRK14041 156 LEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKF-GVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPFSM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 806 MTSQPSMGAIVACTKGTKLDTGISLDKVFDYSEYWEVARGLYAPFDctATMKSGNADVYENEIPGGQYTNLHFQAHSMGL 885
Cdd:PRK14041 235 GTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYD--VGMKSPDSRILVSQIPGGMYSNLVKQLKEQKM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 886 GNKFKEVKKAYTEANKLLGDLIKVTPSSKIVGDLAqfmVQNSLSLAEVEKRADElsfplsVVEFLQGHIGIPHGGFPEPF 965
Cdd:PRK14041 313 LHKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQA---VLNVLTGERYKRVTNE------TKNYVKGLYGRPPAPIDEEL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 922960042 966 RSKVLKSLPRIEGRPGASLPPmDFEAL--ESGLRAAhgdeiTPEDVMSAAMYPKVFQEF 1022
Cdd:PRK14041 384 MKKILGDEKPIDCRPADLLEP-ELEKArkELGILAE-----TDEDLLIYVILGEVGKKF 436
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
573-1022 |
3.96e-78 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 266.24 E-value: 3.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 573 RDAHQSLLATRVRTHDLkkIAPYVSHNFSNLFSLENWGGATFDVAMRFLSECPWKRLQELRALIPNVPFQMLLRGANAVG 652
Cdd:PRK12330 13 RDAHQSLMATRMAMEDM--VGACEDIDNAGYWSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQMLLRGQNLLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 653 YTNYPDNAVFKFCEVAKENGMDIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISYTgdVSdPMrqkYSLDYYLKLADEL 732
Cdd:PRK12330 91 YRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYT--VS-PI---HTVEGFVEQAKRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 733 VKAGTHILSIKDMAGLLKPQASRLLIEALRDRF-PDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVDSMA-GMTSQP 810
Cdd:PRK12330 165 LDMGADSICIKDMAALLKPQPAYDIVKGIKEACgEDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAISSMSlGPGHNP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 811 SMgAIVACTKGTKLDTGISLDKVFDYSEYWEVARGLYAPFDCTATmkSGNADVYENEIPGGQYTNLHFQAHSMGLGNKFK 890
Cdd:PRK12330 245 TE-SLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTT--GVETEIFKSQIPGGMLSNMESQLKQQGAGDRMD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 891 EVKKAYTEANKLLGDLIKVTPSSKIVGDLAQFMVqnslslaevekradeLSFPLSVV--EFLQGHIGIpHGGFPEPFRSK 968
Cdd:PRK12330 322 EVLEEVPRVRKDAGYPPLVTPSSQIVGTQAVFNV---------------LMGRYKVLtgEFADLMLGY-YGETPGERNPE 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 969 VLKSLPR------IEGRPGASLPPmDFEALESGLRAAHGDEITPEDVMSAAMYPKVFQEF 1022
Cdd:PRK12330 386 VVEQAKKqakkepITCRPADLLEP-EWDKLRAEALALEGCDGSDEDVLTYALFPQVAPKF 444
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
153-360 |
3.33e-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: 247.60 E-value: 3.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 153 DKVEARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPIIFKAAYGGGGRGMRVVRNYEELEENYQRAYSEALAAFGN 232
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 233 GALFVEKFIEKPRHIEVQILGDKYGNVIHLYERDCSIQRRHQKVVEIAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTV 312
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 922960042 313 EFLVD-KHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRVCEGRSLP 360
Cdd:pfam02786 161 EFALDpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
568-841 |
3.30e-69 |
|
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: 232.73 E-value: 3.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 568 MDTTFRDAHQSLLATRvRTHDLKKIAPYVSHnfSNLFSLENWGGATFDVAmrFLSECPWKRLQELRALIPNVPFQMLLRG 647
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDE--AGVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 648 anavgytnypdnaVFKFCEVAKENGMDIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISY--------TGDVSDPMRQK 719
Cdd:cd03174 76 -------------REKGIERALEAGVDEVRIFDSASETHSRKNLNKSREEDLENAEEAIEAakeaglevEGSLEDAFGCK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 720 YSLDYYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFPDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVA 799
Cdd:cd03174 143 TDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEAGADRVDGS 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 922960042 800 VDSMAGMTSQPSMGAIVACTKGTKLDTGISLDKVFDYSEYWE 841
Cdd:cd03174 223 VNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVE 264
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
562-1041 |
7.95e-64 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 225.00 E-value: 7.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 562 HQGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVSHnfSNLFSLENWGGATFDVAMRFLSECPWKRLQELRALIPNVPF 641
Cdd:PRK12581 10 QQQVAITETVLRDGHQSLMATRLSIEDMLPVLTILDK--IGYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 642 QMLLRGANAVGYTNYPDNAVFKFCEVAKENGMDIFRVFDSLNYIPNMLLGMEAAGAAGGVVEAAISYTgdvSDPMrqkYS 721
Cdd:PRK12581 88 QMLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYT---TSPV---HT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 722 LDYYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRdRFPDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVD 801
Cdd:PRK12581 162 LNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIK-AMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 802 SMAGMTSQPSMGAIVACTKGTKLDtgISLDKVF--DYSEYWEVARGLY-APFDCTATMKSGNADVYENEIPGGQYTNLHF 878
Cdd:PRK12581 241 PFSEGTSQPATESMYLALKEAGYD--ITLDETLleQAANHLRQARQKYlADGILDPSLLFPDPRTLQYQVPGGMLSNMLS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 879 QAHSMGLGNKFKEVKKAYTEANKLLGDLIKVTPSSKIVGDLAQFMVQNSLSLAEVEKRadelsfplsVVEFLQGHIGIPH 958
Cdd:PRK12581 319 QLKQANAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNVILGKPYQMVSKE---------IKQYLAGDYGKTP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 959 GGFPEPFRSKVLKSLPRIEGRPGASLPPmDFEALESGLRAAHGdeiTPEDVMSAAMYPKVFQEFkeFTSTFGPVDCLNTR 1038
Cdd:PRK12581 390 APVNEDLKRSQIGSAPVTTNRPADQLSP-EFEVLKAEVADLAQ---TDEDVLTYALFPSVAKPF--LTTKYQTDDVIKVT 463
|
...
gi 922960042 1039 LFL 1041
Cdd:PRK12581 464 AFI 466
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
39-147 |
2.75e-58 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 195.78 E-value: 2.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 39 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlSPVAAYLHIPDIIKVAKENNVDAIHP 118
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPG-PASESYLNIDAIIDAAKETGADAIHP 79
|
90 100
....*....|....*....|....*....
gi 922960042 119 GYGFLSERADFAQACAEAGVRFIGPSPEV 147
Cdd:pfam00289 80 GYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
100-357 |
3.24e-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: 178.53 E-value: 3.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 100 HIPDIIKVAKE----NNVDAIHPGYGFLSERAdfAQACAEAGVRfiGPSPEVVRKMGDKVEARALAIKAGVPVvPGTDaP 175
Cdd:COG0439 1 DIDAIIAAAAElareTGIDAVLSESEFAVETA--AELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFA-L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 176 ISCLQEAQEFAKTYDFPIIFKAAYGGGGRGMRVVRNYEELEENYQRAYSEALAAFGNGALFVEKFIEKpRHIEVQILGDK 255
Cdd:COG0439 75 VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVRD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 256 yGNVIHlyerdCSIQRRHQK---VVE---IAPAAhLDSHLRDRLTLDSVNLAKQVGYEN-AGTVEFLVDKHGKHYFIEVN 328
Cdd:COG0439 154 -GEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGEPYLIEIN 226
|
250 260 270
....*....|....*....|....*....|.
gi 922960042 329 SRLQVEH--TVTEEITDVDLVHAQLRVCEGR 357
Cdd:COG0439 227 ARLGGEHipPLTELATGVDLVREQIRLALGE 257
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
377-484 |
6.54e-47 |
|
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: 162.97 E-value: 6.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 377 QCRVTTEDPSRGFQPDTGRIEVFRSGEGMGIRLDSAsAFQGAIISPHYDSLLVKVIASGKDLPTAATKMHRALTEFRVRG 456
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSG-VYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 922960042 457 VKTNIPFLQNVLSNSQFLYATVDTQFID 484
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
377-485 |
1.36e-40 |
|
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: 144.94 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 377 QCRVTTEDPSRGFQPDTGRIEVFRSGEGMGIRLDSAsAFQGAIISPHYDSLLVKVIASGKDLPTAATKMHRALTEFRVRG 456
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSG-VYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 922960042 457 VKTNIPFLQNVLSNSQFLYATVDTQFIDE 485
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
567-839 |
4.58e-30 |
|
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase.
Pssm-ID: 459902 [Multi-domain] Cd Length: 264 Bit Score: 120.52 E-value: 4.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 567 LMDTTFRDAHQSLlATRVRTHDLKKIAPyvshnfsnlfSLENWGGATFDVAMRFLSECPWKRLQELRALIPNVPFQMLLR 646
Cdd:pfam00682 4 ICDTTLRDGEQAL-GVAFSIDEKLAIAR----------ALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVLCR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 647 GAnavgytnypDNAVFKFCEVAKENGMDIFRVFDSLNYIP-NMLLGMEAAGAAGGVVE---AAISYTGDV--SDPMRQKY 720
Cdd:pfam00682 73 AR---------EHDIKAAVEALKGAGAVRVHVFIATSDLHrKYKLGKDREEVAKRAVAavkAARSRGIDVefSPEDASRT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 721 SLDYYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFPD-IPIHVHTHDTAGAGVAAMLACAQAGADIVDVA 799
Cdd:pfam00682 144 DPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRVDGT 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 922960042 800 VDSMAGMTSQPSMGAIVACTKGTKLDTGISLDKVFDYSEY 839
Cdd:pfam00682 224 VNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANL 263
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1113-1179 |
1.46e-26 |
|
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: 103.65 E-value: 1.46e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922960042 1113 QVGAPMPGKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1113-1179 |
1.17e-19 |
|
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: 84.19 E-value: 1.17e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922960042 1113 QVGAPMPGK-----VVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:pfam00364 2 EIKSPMIGEsvregVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1112-1177 |
5.59e-15 |
|
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: 73.01 E-value: 5.59e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922960042 1112 GQVGAPMPGKV-------VEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHV-NADSSLEGEDLIL 1177
Cdd:COG0511 61 GAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVeNGQPVEYGQPLFV 134
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
38-331 |
1.53e-14 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 78.89 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 38 PIKKVMVANRGEIAI-----------RVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIgrglsPVAAYlHIPDIIK 106
Cdd:TIGR01369 5 DIKKILVIGSGPIVIgqaaefdysgsQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIE-----PLTPE-AVEKIIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 107 vaKENnVDAIHPGYG---------FLSERAdfaqACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGtdAPIS 177
Cdd:TIGR01369 79 --KER-PDAILPTFGgqtalnlavELEESG----VLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIAH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 178 CLQEAQEFAKTYDFPIIFKAAYGGGGRGMRVVRNYEELEENYQRayseALAAFGNGALFVEKFIEKPRHIEVQILGDKYG 257
Cdd:TIGR01369 150 SVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAER----ALSASPINQVLVEKSLAGWKEIEYEVMRDSND 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 258 NVIHLyerdCSIQR-----RH--QKVVeIAPAAHLDS----HLRDRltldSVNLAKQVGYENAGTVEFLVD-KHGKHYFI 325
Cdd:TIGR01369 226 NCITV----CNMENfdpmgVHtgDSIV-VAPSQTLTDkeyqMLRDA----SIKIIRELGIEGGCNVQFALNpDSGRYYVI 296
|
....*.
gi 922960042 326 EVNSRL 331
Cdd:TIGR01369 297 EVNPRV 302
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1112-1179 |
3.14e-12 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 65.65 E-value: 3.14e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922960042 1112 GQVGAPMPGKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:PRK05641 85 NVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1114-1176 |
3.95e-11 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 61.75 E-value: 3.95e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922960042 1114 VGAPMPGKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLE-GEDLI 1176
Cdd:PRK06549 64 MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNpGDGLI 127
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
130-421 |
4.94e-11 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 67.33 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 130 AQACAEAGVRFIGPSPEVVrkmgDKVEAR----ALAIKAGVPVVPGTDApiSCLQEAQEFAKTYDFPIIFKAAYGGGGRG 205
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESI----DRAEDRekfsELLDELGIPQPKWKTA--TSVEEAVEFASEIGYPVLVRPSYVLGGRA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 206 MRVVRNYEELEenyqRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKyGNVI------HLyER------DCSIqrrh 273
Cdd:TIGR01369 720 MEIVYNEEELR----RYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDG-EEVLipgimeHI-EEagvhsgDSTC---- 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 274 qkvveIAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVdKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQLRV 353
Cdd:TIGR01369 790 -----VLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV-KDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRV 863
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922960042 354 CEGRSLPELGLEQDKIQiNGCAIQCRVTTEDPSRGFQPDTGrIEVFRSGEGMGIRLDSASAFQGAIIS 421
Cdd:TIGR01369 864 MLGKKLEELGVGKEKEP-KYVAVKEPVFSFSKLAGVDPVLG-PEMKSTGEVMGIGRDLAEAFLKAQLS 929
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
726-835 |
2.89e-10 |
|
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: 62.41 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 726 LKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFPDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVdsmAG 805
Cdd:cd07938 152 AEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERFPDEKLALHFHDTRGQALANILAALEAGVRRFDSSV---GG 228
|
90 100 110
....*....|....*....|....*....|....*....
gi 922960042 806 MTSQP-SMGA--------IVACTKGTKLDTGISLDKVFD 835
Cdd:cd07938 229 LGGCPfAPGAtgnvatedLVYMLEGMGIETGIDLDKLLA 267
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1113-1179 |
5.00e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 56.72 E-value: 5.00e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922960042 1113 QVGAPMPGKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNadsslEGE-----DLILEI 1179
Cdd:PRK08225 3 KVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQ-----EGDfvnegDVLLEI 69
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1113-1179 |
6.03e-10 |
|
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: 56.68 E-value: 6.03e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922960042 1113 QVGAPMP------GKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:cd06663 1 TILIPDLaqhlgdGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
722-839 |
3.57e-09 |
|
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; Isopropylmalate/homocitrate/citramalate synthases is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439889 [Multi-domain] Cd Length: 452 Bit Score: 60.57 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 722 LDYYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFPDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVD 801
Cdd:COG0119 147 PDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHNDLGLAVANSLAAVEAGADQVEGTIN 226
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 922960042 802 SM---AGMTSQPSMGAIVACTKGtkLDTGISLDKVFDYSEY 839
Cdd:COG0119 227 GIgerAGNAALEEVVMNLKLKYG--VDTGIDLSKLTELSRL 265
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
103-415 |
1.28e-08 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 59.60 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 103 DIIKVAKENNVDAIHPGYGflSERA-DFAQACAEAGVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDApiSCLQE 181
Cdd:PRK12815 621 DVLNVAEAENIKGVIVQFG--GQTAiNLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTA--TDEEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 182 AQEFAKTYDFPIIFKAAYGGGGRGMRVVRNYEELEENYQRAYSealaafGNGALFVEKFIEKpRHIEVQILGDKYGNVI- 260
Cdd:PRK12815 697 AFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENAS------QLYPILIDQFIDG-KEYEVDAISDGEDVTIp 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 261 ----HLYER-----DcSIQrrhqkvveIAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVdKHGKHYFIEVNSRl 331
Cdd:PRK12815 770 giieHIEQAgvhsgD-SIA--------VLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL-ANDEIYVLEVNPR- 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 332 qVEHTV--TEEITDVDLVHAQLRVCEGRSLPELGLEQDKIQINGcaiqcRVTTEDPSRGFQ--PDTGRI---EVFRSGEG 404
Cdd:PRK12815 839 -ASRTVpfVSKATGVPLAKLATKVLLGKSLAELGYPNGLWPGSP-----FIHVKMPVFSYLkyPGVDNTlgpEMKSTGEV 912
|
330
....*....|.
gi 922960042 405 MGIRLDSASAF 415
Cdd:PRK12815 913 MGIDKDLEEAL 923
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
80-330 |
2.61e-08 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 57.20 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 80 QKADEAYLIGRGLSPvaAYlhIPDIIKVAKENNVDAIHPGY----GFLSE-RADFAqacaEAGVRFIGPSPEVVRKMGDK 154
Cdd:PRK12767 41 YFADKFYVVPKVTDP--NY--IDRLLDICKKEKIDLLIPLIdpelPLLAQnRDRFE----EIGVKVLVSSKEVIEICNDK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 155 VEARALAIKAGVPVvpgtdaPISCLQE------AQEFAKTYDFPIIFKAAYGGGGRGMRVVRNYEELEenyqRAYSEala 228
Cdd:PRK12767 113 WLTYEFLKENGIPT------PKSYLPEsledfkAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEY--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 229 afgNGALFVEKFIEkprHIE--VQILGDKYGNVIHlyerdcSIQRRHQKV----VEIAPAAHlDSHLRDrLTLDSVNLAK 302
Cdd:PRK12767 180 ---VPNLIIQEFIE---GQEytVDVLCDLNGEVIS------IVPRKRIEVrageTSKGVTVK-DPELFK-LAERLAEALG 245
|
250 260
....*....|....*....|....*...
gi 922960042 303 QVGYENagtVEFLVDKhGKHYFIEVNSR 330
Cdd:PRK12767 246 ARGPLN---IQCFVTD-GEPYLFEINPR 269
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
102-349 |
5.51e-08 |
|
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: 55.72 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 102 PDIIKVAKENNVDAIHPGYGFLSERADFAQACAEAGVRFIgPSPEVVRKMGDKVEARALAIKAGVPVVPgTdAPISCLQE 181
Cdd:COG0189 46 PELYRGEDLSEFDAVLPRIDPPFYGLALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPP-T-LVTRDPDD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 182 AQEFAKTYDFPIIFKAAYGGGGRGMRVVRNYEELEenyqrAYSEALAAFGNGALFVEKFIEKPRHIEVQI--LGDKygnV 259
Cdd:COG0189 123 LRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALE-----SILEALTELGSEPVLVQEFIPEEDGRDIRVlvVGGE---P 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 260 IHLYER-----DCSIQRRHQKVVEiapAAHLDSHLRDRLtldsVNLAKQVGYENAGtVEFLVDKHGkHYFIEVNSRLQVE 334
Cdd:COG0189 195 VAAIRRipaegEFRTNLARGGRAE---PVELTDEERELA----LRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVTPGFR 265
|
250
....*....|....*
gi 922960042 335 HtvTEEITDVDLVHA 349
Cdd:COG0189 266 G--LERATGVDIAEA 278
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1120-1179 |
5.92e-08 |
|
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: 50.84 E-value: 5.92e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 1120 GKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
722-800 |
7.15e-08 |
|
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate synthase (IPMS) catalyzes an aldol-type condensation of acetyl-CoA and 2-oxoisovalerate yielding 2-isopropylmalate and CoA, the first committed step in leucine biosynthesis. This family includes the Arabidopsis thaliana IPMS1 and IPMS2 proteins, the Glycine max GmN56 protein, and the Brassica insularis BatIMS protein. This family also includes a group of archeal IPMS-like proteins represented by the Methanocaldococcus jannaschii AksA protein. AksA catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form trans-homoaconitate, one of 13 steps in the conversion of alpha-ketoglutarate and acetylCoA to alpha-ketosuberate, a precursor to coenzyme B and biotin. AksA also catalyzes the condensation of alpha-ketoadipate or alpha-ketopimelate with acetylCoA to form, respectively, the (R)-homocitrate homologs (R)-2-hydroxy-1,2,5-pentanetricarboxylic acid and (R)-2-hydroxy-1,2,6- hexanetricarboxylic acid. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163678 Cd Length: 268 Bit Score: 55.15 E-value: 7.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 722 LDYYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFPDI--PIHVHTHDTAGAGVAAMLACAQAGADIVDVA 799
Cdd:cd07940 142 LDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVPNIkvPISVHCHNDLGLAVANSLAAVEAGARQVECT 221
|
.
gi 922960042 800 V 800
Cdd:cd07940 222 I 222
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
727-838 |
7.61e-08 |
|
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: 54.81 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 727 KLADE---LVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFPDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVavdSM 803
Cdd:cd07943 142 ELAEQaklMESYGADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATRIDG---SL 218
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 922960042 804 AGM-----TSQPSMGAIVACTKGtkLDTGISLDKVFDYSE 838
Cdd:cd07943 219 AGLgagagNTPLEVLVAVLERMG--IETGIDLYKLMDAAE 256
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
722-849 |
2.05e-07 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 54.94 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 722 LDYYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRfPDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVD 801
Cdd:PRK09389 142 LDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSEL-VKGPVSIHCHNDFGLAVANTLAALAAGADQVHVTIN 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 922960042 802 SM---AGMTSQPSMgaIVACTKGTKLDTGISLDKVFDYSEYWEVARGLYAP 849
Cdd:PRK09389 221 GIgerAGNASLEEV--VMALKHLYDVETGIKLEELYELSRLVSRLTGIPVP 269
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
130-330 |
3.13e-07 |
|
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: 54.50 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 130 AQACAEA----GVRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDApiSCLQEAQEFAKTYDFPIIFKAAYGGGGRG 205
Cdd:COG0458 87 AVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTA--TSVEEALAIAEEIGYPVIVRPSYVLGGRG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 206 MRVVRNYEELEENYQRayseALAAFGNGALFVEKFIEKPRHIEVQILGDKYGNVI------HLyER------DcSIqrrh 273
Cdd:COG0458 165 MGIVYNEEELEEYLER----ALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIivgimeHI-EPagvhsgD-SI---- 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 922960042 274 qkVVeiAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKhGKHYFIEVNSR 330
Cdd:COG0458 235 --CV--APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDD-GRVYVIEVNPR 286
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1114-1180 |
7.35e-07 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 47.88 E-value: 7.35e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922960042 1114 VGAPMPGKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEIT 1180
Cdd:PRK05889 5 VRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVIS 71
|
|
| PLN02746 |
PLN02746 |
hydroxymethylglutaryl-CoA lyase |
728-839 |
7.83e-07 |
|
hydroxymethylglutaryl-CoA lyase
Pssm-ID: 178347 Cd Length: 347 Bit Score: 52.48 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 728 LADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFPDIPIHVHTHDTAGAGVAAMLACAQAGADIVDvavDSMAGMT 807
Cdd:PLN02746 202 VAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDKLAVHFHDTYGQALANILVSLQMGISTVD---SSVAGLG 278
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 922960042 808 SQP-SMGA--------IVACTKGTKLDTGISLDKVFDYSEY 839
Cdd:PLN02746 279 GCPyAKGAsgnvatedVVYMLNGLGVSTNVDLGKLMAAGDF 319
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
722-800 |
1.44e-06 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 52.10 E-value: 1.44e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922960042 722 LDYYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFpDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAV 800
Cdd:PRK11858 144 LDFLIEFAKAAEEAGADRVRFCDTVGILDPFTMYELVKELVEAV-DIPIEVHCHNDFGMATANALAGIEAGAKQVHTTV 221
|
|
| DRE_TIM_CMS |
cd07945 |
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ... |
708-849 |
4.16e-06 |
|
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: 50.07 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 708 YTGDVSDPMRQkySLDYYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFPDIPIHVHTHDTAGAGVAAMLA 787
Cdd:cd07945 134 YLEDWSNGMRD--SPDYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFHAHNDYDLAVANVLA 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922960042 788 CAQAGADIVDVAVDSMAGMTSQPSMGAIVACTKG-TKLDTGISLDKVFDYSEYWEVARGLYAP 849
Cdd:cd07945 212 AVKAGIKGLHTTVNGLGERAGNAPLASVIAVLKDkLKVKTNIDEKRLNRASRLVETFSGKRIP 274
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
722-844 |
5.03e-06 |
|
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) of Streptomyces rubellomurinus catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate and CoA, a reaction similar to one catalyzed by homocitrate synthase. The gene encoding FrbC is one of several genes required for the biosynthesis of FR900098, a potent antimalarial antibiotic. This protein is also required for assembly of the nitrogenase MoFe complex but its exact role is unknown. This family also includes the NifV proteins of Heliobacterium chlorum and Gluconacetobacter diazotrophicus, which appear to be orthologous to FrbC. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163677 [Multi-domain] Cd Length: 259 Bit Score: 49.43 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 722 LDYYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFpDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVD 801
Cdd:cd07939 138 PDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAAT-DLPLEFHAHNDLGLATANTLAAVRAGATHVSVTVN 216
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 922960042 802 SM---AGMTS--QPSMGAIVACtkgtKLDTGISLDKVFDYSEYweVAR 844
Cdd:cd07939 217 GLgerAGNAAleEVVMALKHLY----GRDTGIDTTRLPELSQL--VAR 258
|
|
| PRK08195 |
PRK08195 |
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated |
735-864 |
6.61e-06 |
|
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
Pssm-ID: 181282 [Multi-domain] Cd Length: 337 Bit Score: 49.83 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 735 AGTHILSIKDMAGLLKPQASRLLIEALRDRF-PDIPIHVHTHDTAGAGVAAMLACAQAGADIVDVAVDSM-AGMTSQPsM 812
Cdd:PRK08195 156 YGAQCVYVVDSAGALLPEDVRDRVRALRAALkPDTQVGFHGHNNLGLGVANSLAAVEAGATRIDGSLAGLgAGAGNTP-L 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 922960042 813 GAIVACTKGTKLDTGISLDKVFDYSEywEVARGLyAPFDCT---ATMKSGNADVY 864
Cdd:PRK08195 235 EVLVAVLDRMGWETGVDLYKLMDAAE--DLVRPL-MDRPVRvdrEALTLGYAGVY 286
|
|
| PRK05692 |
PRK05692 |
hydroxymethylglutaryl-CoA lyase; Provisional |
708-845 |
9.08e-06 |
|
hydroxymethylglutaryl-CoA lyase; Provisional
Pssm-ID: 180206 Cd Length: 287 Bit Score: 48.73 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 708 YTGDVsdPMRQkysldyYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFPDIPIHVHTHDTAGAGVAAMLA 787
Cdd:PRK05692 148 YEGEV--PPEA------VADVAERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAEFPAERLAGHFHDTYGQALANIYA 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922960042 788 CAQAGADIVDVAVDSMAGMTSQPsmGA--------IVACTKGTKLDTGISLDKVFDYSEYWEVARG 845
Cdd:PRK05692 220 SLEEGITVFDASVGGLGGCPYAP--GAsgnvatedVLYMLHGLGIETGIDLDKLVRAGQFIQSKLG 283
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1107-1177 |
1.26e-05 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 49.49 E-value: 1.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922960042 1107 LKDVR-GQVGAPMPGKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLIL 1177
Cdd:TIGR01348 116 VQEVTvPDIGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLIL 187
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1120-1179 |
2.02e-05 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 48.85 E-value: 2.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 1120 GKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIF 74
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1114-1179 |
2.10e-05 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 48.72 E-value: 2.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922960042 1114 VGAPMPGKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:TIGR01348 8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATL 73
|
|
| PRK00915 |
PRK00915 |
2-isopropylmalate synthase; Validated |
722-800 |
3.46e-05 |
|
2-isopropylmalate synthase; Validated
Pssm-ID: 234864 [Multi-domain] Cd Length: 513 Bit Score: 47.80 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 722 LDYYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFPDI---PIHVHTHDTAGAGVAAMLACAQAGADIVDV 798
Cdd:PRK00915 148 LDFLCRVVEAAIDAGATTINIPDTVGYTTPEEFGELIKTLRERVPNIdkaIISVHCHNDLGLAVANSLAAVEAGARQVEC 227
|
..
gi 922960042 799 AV 800
Cdd:PRK00915 228 TI 229
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
39-331 |
9.32e-05 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 46.70 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 39 IKKVMVANRGEIAI-----------RVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLigrglSPVAaylhiPDII-K 106
Cdd:PLN02735 23 LKKIMILGAGPIVIgqacefdysgtQACKALKEEGYEVVLINSNPATIMTDPETADRTYI-----APMT-----PELVeQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 107 VAKENNVDAIHPGYGflSERA-DFAQACAEAG------VRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTDApiSCL 179
Cdd:PLN02735 93 VIAKERPDALLPTMG--GQTAlNLAVALAESGilekygVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIA--TTL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 180 QEAQEFAKTY-DFPIIFKAAYGGGGRGMRVVRNYEELEEnyqrAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDKYGN 258
Cdd:PLN02735 169 DECFEIAEDIgEFPLIIRPAFTLGGTGGGIAYNKEEFET----ICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 259 VIHLyerdCSIQRRHQKVVE------IAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGT-VEFLVD-KHGKHYFIEVNSR 330
Cdd:PLN02735 245 VVII----CSIENIDPMGVHtgdsitVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSnVQFAVNpVDGEVMIIEMNPR 320
|
.
gi 922960042 331 L 331
Cdd:PLN02735 321 V 321
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
39-330 |
1.02e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 46.63 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 39 IKKVMVANRGEI--------------AIRVFRactELGIRTVAVYSEQDTGQMHRQKADEAYLIgrglsPvaayLHIPDI 104
Cdd:PRK05294 7 IKKILIIGSGPIvigqacefdysgtqACKALR---EEGYRVVLVNSNPATIMTDPEMADATYIE-----P----ITPEFV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 105 IKVAKENNVDAIHPGYG---FLSeradFAQACAEAG------VRFIGPSPEVVRKMGDKVEARALAIKAGVPVVPGTdaP 175
Cdd:PRK05294 75 EKIIEKERPDAILPTMGgqtALN----LAVELAESGvlekygVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSG--I 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 176 ISCLQEAQEFAKTYDFPIIFKAAYGGGGRGMRVVRNYEELEENYQRayseALAAFGNGALFVEKFIEKPRHIEVQILGDK 255
Cdd:PRK05294 149 AHSMEEALEVAEEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVER----GLDLSPVTEVLIEESLLGWKEYEYEVMRDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 256 YGNVIHLyerdCSIqrrhqkvvE--------------IAPAAHLDS----HLRDrltlDSVNLAKQVGYENAGT-VEFLV 316
Cdd:PRK05294 225 NDNCIIV----CSI--------EnidpmgvhtgdsitVAPAQTLTDkeyqMLRD----ASIAIIREIGVETGGCnVQFAL 288
|
330
....*....|....*
gi 922960042 317 D-KHGKHYFIEVNSR 330
Cdd:PRK05294 289 NpKDGRYIVIEMNPR 303
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
87-328 |
1.11e-04 |
|
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: 45.48 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 87 LIGRGLSPVAAYLHIPDIIKVAKENNVD----AIHPGYGflsEraD-FAQACAE-AGVRFIGPSPevvrkMG-----DKV 155
Cdd:COG1181 28 LDKAGYDVVPIGIDVEDLPAALKELKPDvvfpALHGRGG---E--DgTIQGLLElLGIPYTGSGV-----LAsalamDKA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 156 EARALAIKAGVPVVPGTDAPISCLQEAQEFAKTYDFPIIFKAA-----------YggggrgmrvvrNYEELEEnyqrAYS 224
Cdd:COG1181 98 LTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAregssvgvskvK-----------NAEELAA----ALE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 225 EALaAFGNGALfVEKFIEkPRHIEVQILGDKYGNVIhlyerdcsiqrrhqKVVEIAPA--------------------AH 284
Cdd:COG1181 163 EAF-KYDDKVL-VEEFID-GREVTVGVLGNGGPRAL--------------PPIEIVPEngfydyeakytdggteyicpAR 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 922960042 285 LDSHLRDRLTldsvNLAKQV-------GYenaGTVEFLVDKHGKHYFIEVN 328
Cdd:COG1181 226 LPEELEERIQ----ELALKAfralgcrGY---ARVDFRLDEDGEPYLLEVN 269
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
39-331 |
2.07e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 45.73 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 39 IKKVMVANRGEIAI-----------RVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLigrglSPVAaylhiPDIIK- 106
Cdd:PRK12815 7 IQKILVIGSGPIVIgqaaefdysgtQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYF-----EPLT-----VEFVKr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 107 -VAKENNvDAIHPGYGflSERA-DFAQACAEAG------VRFIGPSPEVVRKMGDKVEARALAIKAGVPVvPGTDApISC 178
Cdd:PRK12815 77 iIAREKP-DALLATLG--GQTAlNLAVKLHEDGileqygVELLGTNIEAIQKGEDRERFRALMKELGEPV-PESEI-VTS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 179 LQEAQEFAKTYDFPIIFKAAYGGGGRGMRVVRNYEELEENYQRAysEALAAFGNgaLFVEKFIEKPRHIEVQILGDKYGN 258
Cdd:PRK12815 152 VEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQG--LQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 259 VIHLyerdCSIQRrhqkvVE-----------IAPAAHLDSHLRDRLTLDSVNLAKQVGYENAGTVEFLVDKHGKHYF-IE 326
Cdd:PRK12815 228 CITV----CNMEN-----IDpvgihtgdsivVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYlIE 298
|
....*
gi 922960042 327 VNSRL 331
Cdd:PRK12815 299 VNPRV 303
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1120-1179 |
2.17e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 45.20 E-value: 2.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 1120 GKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:PRK11855 16 VEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVI 75
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1106-1179 |
3.52e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 44.61 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 1106 ALKDVRgqvgapMP------GKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:PRK11854 205 GVKDVN------VPdiggdeVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRF 278
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1106-1179 |
3.86e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 44.61 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 1106 ALKDVRgqvgapMP------GKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:PRK11854 104 AAKDVH------VPdigsdeVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVF 177
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
1113-1152 |
4.31e-04 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 38.96 E-value: 4.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 922960042 1113 QVGAPMPGKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVN 1152
Cdd:pfam13533 4 KIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQ 43
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1113-1143 |
4.99e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.88 E-value: 4.99e-04
10 20 30
....*....|....*....|....*....|.
gi 922960042 1113 QVGAPMPGKVVEVKVKAGQKVEKGQPLCVLS 1143
Cdd:COG1566 47 TVAAKVSGRVTEVLVKEGDRVKKGQVLARLD 77
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
140-254 |
5.75e-04 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 44.04 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 140 FIGPSPEVVRKMGDKVEARALAIKAGVPVVP--------GTDAPISCLQEAQEfakTYDFPIIFKAAYGGGGRGMRVVRN 211
Cdd:PRK14573 555 YTGPSLAFSAIAMDKVLTKRFASDVGVPVVPyqpltlagWKREPELCLAHIVE---AFSFPMFVKTAHLGSSIGVFEVHN 631
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 922960042 212 YEELEEnyqrAYSEALAAfgNGALFVEKFIEKPRHIEVQILGD 254
Cdd:PRK14573 632 VEELRD----KISEAFLY--DTDVFVEESRLGSREIEVSCLGD 668
|
|
| FolP |
COG0294 |
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ... |
755-817 |
6.45e-04 |
|
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440063 Cd Length: 274 Bit Score: 43.12 E-value: 6.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922960042 755 RLL--IEALRDRFpDIPIHVhthDTAGAGVAAmlACAQAGADIV-DVavdsmAGMTSQPSMGAIVA 817
Cdd:COG0294 74 RVVpvIEALRAEF-DVPISV---DTYKAEVAR--AALEAGADIInDV-----SGLRFDPEMAEVAA 128
|
|
| PLN03228 |
PLN03228 |
methylthioalkylmalate synthase; Provisional |
723-820 |
7.02e-04 |
|
methylthioalkylmalate synthase; Provisional
Pssm-ID: 178767 [Multi-domain] Cd Length: 503 Bit Score: 43.76 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 723 DYYLKLADELVKAGTHILSIKDMAGLLKPQASRLLIEALRDRFP---DIPIHVHTHDTAGAGVAAMLACAQAGADIVDVA 799
Cdd:PLN03228 239 EFLCKILGEAIKAGATSVGIADTVGINMPHEFGELVTYVKANTPgidDIVFSVHCHNDLGLATANTIAGICAGARQVEVT 318
|
90 100
....*....|....*....|.
gi 922960042 800 VDSMAGMTSQPSMGAIVACTK 820
Cdd:PLN03228 319 INGIGERSGNASLEEVVMALK 339
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
143-326 |
8.76e-04 |
|
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: 43.14 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 143 PSPEVVRKMGDKVEARALAIKAGVPVVPGtdAPISCLQEAQEFAKTYDFPIIFKAAyggggrgmrvVRNY---------- 212
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAPF--AAVDSLEDLEAAIAELGLPAVLKTR----------RGGYdgkgqvviks 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 213 -EELEenyqraysEALAAFGNGALFVEKFI--EKprhiEVQILG--DKYGNVIHlY---ErdcSIQRRHQKVVEIAPaAH 284
Cdd:COG0026 147 aADLE--------AAWAALGGGPCILEEFVpfER----ELSVIVarSPDGEVAT-YpvvE---NVHRNGILDESIAP-AR 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 922960042 285 LDSHLRDRLTLDSVNLAKQVGYenAGT--VEFLVDKHGK--------------HYFIE 326
Cdd:COG0026 210 ISEALAAEAEEIAKRIAEALDY--VGVlaVEFFVTKDGEllvneiaprphnsgHWTIE 265
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
1113-1142 |
1.07e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 42.62 E-value: 1.07e-03
10 20 30
....*....|....*....|....*....|
gi 922960042 1113 QVGAPMPGKVVEVKVKAGQKVEKGQPLCVL 1142
Cdd:COG0845 25 EVRARVSGRVEEVLVDEGDRVKKGQVLARL 54
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
1120-1176 |
1.08e-03 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 42.75 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 922960042 1120 GKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLE-GEDLI 1176
Cdd:PTZ00144 59 GTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEvGAPLS 116
|
|
| HIS2 |
COG1387 |
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and ... |
104-187 |
1.22e-03 |
|
Histidinol phosphatase or related hydrolase of the PHP family [Amino acid transport and metabolism, General function prediction only]; Histidinol phosphatase or related hydrolase of the PHP family is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 440997 [Multi-domain] Cd Length: 232 Bit Score: 41.68 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 104 IIKVAKENNVDAI-HPGYGFLSERADF-------AQACAEAGVrFI---------GPSPEVVRkmgdkvearaLAIKAGV 166
Cdd:COG1387 118 LLKAIENPLVDILgHPDGRLLGGRPGYevdieevLEAAAENGV-ALeintrplrlDPSDELLK----------LAKELGV 186
|
90 100
....*....|....*....|....*
gi 922960042 167 PVVPGTDA--P--ISCLQEAQEFAK 187
Cdd:COG1387 187 KITIGSDAhsPedLGDLEYGVALAR 211
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
51-176 |
1.66e-03 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 42.26 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 51 AIRVFRACTELGIRTVAVYSEQDTGQMHRQ--KA--DEAYLIGRglsPVAAYLHIPDIIKVAKENNVDAIHPGYGFLSER 126
Cdd:COG1228 163 ARAALRELLAEGADYIKVFAEGGAPDFSLEelRAilEAAHALGL---PVAAHAHQADDIRLAVEAGVDSIEHGTYLDDEV 239
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922960042 127 ADFAqacAEAGVRFIGP------------SPEVVRKMGDKVEAR----ALAIKAGVPVVPGTDAPI 176
Cdd:COG1228 240 ADLL---AEAGTVVLVPtlslflallegaAAPVAAKARKVREAAlanaRRLHDAGVPVALGTDAGV 302
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1120-1179 |
4.15e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 41.35 E-value: 4.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 1120 GKVVEVKVKAGQKVEKGQPLCVLSAMKMETVVNSPISGIISKVHVNADSSLEGEDLILEI 1179
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVI 192
|
|
| DRE_TIM_LeuA3 |
cd07941 |
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel ... |
758-796 |
5.35e-03 |
|
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel domain; Desulfobacterium autotrophicum LeuA3 is sequence-similar to alpha-isopropylmalate synthase (LeuA) but its exact function is unknown. Members of this family have an N-terminal TIM barrel domain that 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: 163679 Cd Length: 273 Bit Score: 40.13 E-value: 5.35e-03
10 20 30
....*....|....*....|....*....|....*....
gi 922960042 758 IEALRDRFPDIPIHVHTHDTAGAGVAAMLACAQAGADIV 796
Cdd:cd07941 186 VKEVRERLPGVPLGIHAHNDSGLAVANSLAAVEAGATQV 224
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
68-358 |
6.91e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 40.60 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 68 VYSEQDT---GQMHRQKA----DEAYLI--GRGLSPVAAYLHIPDIikVAKENNVDAIHpgyGFLSERAD---------- 128
Cdd:PRK02186 6 VFIESNTtgtGELLLRKAllrgFTPYFLtaNRGKYPFLDAIRVVTI--SADTSDPDRIH---RFVSSLDGvagimsssey 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 129 FAQACAEAGVRFIGPS--PEVVRKMGDKVE-ARALAiKAGVPVvPGTDApISCLQEAQEFAKTYDFPIIFKAAYGGGGRG 205
Cdd:PRK02186 81 FIEVASEVARRLGLPAanTEAIRTCRDKKRlARTLR-DHGIDV-PRTHA-LALRAVALDALDGLTYPVVVKPRMGSGSVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 206 MRVVRNYEELEenyqrAYSEALAAFGNGALFVEKFIEKPRHiEVQILGDKYGNVIhlyerdCSIQRRHQ----KVVEIA- 280
Cdd:PRK02186 158 VRLCASVAEAA-----AHCAALRRAGTRAALVQAYVEGDEY-SVETLTVARGHQV------LGITRKHLgpppHFVEIGh 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922960042 281 --PAAhLDSHLRDRLTLDSVNLAKQVGYE-NAGTVEFLVdKHGKHYFIEVNSRLQ--VEHTVTEEITDVDLVHAQLRVCE 355
Cdd:PRK02186 226 dfPAP-LSAPQRERIVRTVLRALDAVGYAfGPAHTELRV-RGDTVVIIEINPRLAggMIPVLLEEAFGVDLLDHVIDLHL 303
|
...
gi 922960042 356 GRS 358
Cdd:PRK02186 304 GVA 306
|
|
| |
