|
Name |
Accession |
Description |
Interval |
E-value |
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
15-713 |
0e+00 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 716.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 15 FASLTPLIEPRSVAVIGASSDPTRIGGRPIAYMLRHGYAGQILPVNPNRAEIQGLPAFASVAELPQAPDVAIVAVPAPQV 94
Cdd:COG1042 3 TRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAETV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 95 LETVRALGRQGARSAIVFSSGFSEVGEAGAAMQDAVVAAAREHGMRLLGPNALGAFNSNLGYYAFFSTslerGVPLPGRV 174
Cdd:COG1042 83 PDVVEECGEKGVKAAVVISAGFAETGEEGAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAP----VPPLPGNI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 175 GIATQSGAYGAHLLGMARQRRLGTPICVATGNEADVTLGDSIGWLVESPEIDVVMAYAESIRNVDSFLAALEAAHRaGKP 254
Cdd:COG1042 159 ALVSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAAR-GKP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 255 VILHKVGRSALGSRAALSHTASLAGDDKVLDAVLDDYAVIRARTTEELMDIAYLATRRIYPLGNSLGMITVSGGAGIIVS 334
Cdd:COG1042 238 VVVLKSGRSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 335 DVAEEVGLPMPPMPDMAQERLKARL-SFASPINPVDCTAQALNDLtlVRDFTESMVVDGGYRSLLAFFTQAGTAASigAR 413
Cdd:COG1042 318 DALEDLGLELAELSEETQAALRAVLpPFASVGNPVDITGDADPER--YAAALEALLADPNVDAVLVILTPTAMTDP--EE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 414 LAEQFRRIKeAHPERLFVVSVMGE---GEELAPYEEAGFALFEDPTRAVVAIQAMGRLGEAFARPLR------------- 477
Cdd:COG1042 394 VAEALIEAA-KGSGKPVLASWMGGdsvAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMEtpasedfdpdrer 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 478 -LRRPAGGLQLPASTPGEAEAKRLLARAGIESAAEAVLGSAEEAVAFAEGIGYPVVLKLASADIQHKSEIGGVLLGVSDA 556
Cdd:COG1042 473 aRAIIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 557 DAVRAGFQLLLRRAAEKAPQARLDGVLVARQLQGGVECFMGIQRDPLFGPVALFGLGGIFVEVLQDVVFRRCPFEVDEAE 636
Cdd:COG1042 553 EAVRAAFEEILARVRAARPDARIDGVLVQPMVPGGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALAR 632
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523497446 637 VMIRSIRGAPLLLGARGRPRADVAALARLLSNLSRFAWEAGERLRSvDLNPVIALPEGQGAWAVDAVLEVEEVADGA 713
Cdd:COG1042 633 EMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILEL-DINPLLVVPEGVVAVDARIRLAPPAPPAPR 708
|
|
| AcCoA-syn-alpha |
TIGR02717 |
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ... |
18-467 |
1.38e-106 |
|
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it is believed that this group of ADP-dependent acetyl-CoA synthetases (ACS) act in the direction of acetate and ATP production in the organisms in which it has been characterized. In most species this protein exists as a fused alpha-beta domain polypeptide. In Pyrococcus and related species, however the domains exist as separate polypeptides. This model represents the alpha (N-terminal) domain. In Pyrococcus and related species there appears to have been the development of a paralogous family such that four other proteins are close relatives. In reference, one of these (along with its beta-domain partner) was characterized as ACS-II showing specificity for phenylacetyl-CoA. This model has been constructed to exclude these non-ACS-I paralogs. This may result in new, authentic ACS-I sequences falling below the trusted cutoff.
Pssm-ID: 131764 [Multi-domain] Cd Length: 447 Bit Score: 331.97 E-value: 1.38e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 18 LTPLIEPRSVAVIGASSDPTRIGGRPIAYMLRHGYAGQILPVNPNRAEIQGLPAFASVAELPQAPDVAIVAVPAPQVLET 97
Cdd:TIGR02717 1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 98 VRALGRQGARSAIVFSSGFSEVGEAGAAMQDAVVAAAREHGMRLLGPNALGAFNSNLGYYAFFSTSLergvPLPGRVGIA 177
Cdd:TIGR02717 81 VEECGEKGVKGAVVITAGFKEVGEEGAELEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPTM----PKKGGIAFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 178 TQSGAYGAHLLGMARQRRLGTPICVATGNEADVTLGDSIGWLVESPEIDVVMAYAESIRNVDSFL-AALEAAHRagKPVI 256
Cdd:TIGR02717 157 SQSGALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLkTAREISKK--KPIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 257 LHKVGRSALGSRAALSHTASLAGDDKVLDAVLDDYAVIRARTTEELMDIAYLATRRIYPLGNSLGMITVSGGAGIIVSDV 336
Cdd:TIGR02717 235 VLKSGTSEAGAKAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPKGNRVAIITNAGGPGVIATDA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 337 AEEVGLPMPPMPDMAQERLKARL-SFASPINPVDCTAQALNDL--TLVRDFTESMVVDGgyrsLLAFFTQagtAASIGAR 413
Cdd:TIGR02717 315 CEENGLELAELSEATKNKLRNILpPEASIKNPVDVLGDATPERyaKALKTVAEDENVDG----VVVVLTP---TAMTDPE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 523497446 414 -LAEQFRRIKEAHPERLFVVSVMGEGEELAP---YEEAGFALFEDPTRAVVAIQAMGR 467
Cdd:TIGR02717 388 eVAKGIIEGAKKSNEKPVVAGFMGGKSVDPAkriLEENGIPNYTFPERAVKALSALYR 445
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
493-706 |
1.21e-70 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 463918 [Multi-domain] Cd Length: 221 Bit Score: 229.67 E-value: 1.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 493 GEAEAKRLLARAGIESAAEAVLGSAEEAVAFAEGIGYPVVLKLASADIQHKSEIGGVLLGVSDADAVRAGFQLLLRRAAE 572
Cdd:pfam13549 11 TEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAAYEEILERVRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 573 KAPQARLDGVLVARQLQGGVECFMGIQRDPLFGPVALFGLGGIFVEVLQDVVFRRCPFEVDEAEVMIRSIRGAPLLLGAR 652
Cdd:pfam13549 91 YRPDARIEGVLVQPMAPGGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMIRRTRAYKLLKGYR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523497446 653 GRPRADVAALARLLSNLSRFAWEAGErLRSVDLNPVIAlpEGQGAWAVDAVLEV 706
Cdd:pfam13549 171 GEPPADLDALEDVLVRVSQLVIDFPE-IRELDINPLLA--DEDGVVALDARIRL 221
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
23-116 |
6.16e-19 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 214881 [Multi-domain] Cd Length: 100 Bit Score: 82.17 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 23 EPRSVAVIGASSDPTRIGGRPIAYMLRHG--YAGQILP--VNPnraEIQGLPAFASVAELPQA--PDVAIVAVPAPQVLE 96
Cdd:smart00881 4 PNTSVAVVGASGNLGSFGLAVMRNLLEYGtkFVGGVYPgkVGP---KVDGVPVYDSVAEAPEEtgVDVAVIFVPAEAAPD 80
|
90 100
....*....|....*....|
gi 523497446 97 TVRALGRQGARSAIVFSSGF 116
Cdd:smart00881 81 AIDEAIEAGIKGIVVITEGI 100
|
|
| PRK05678 |
PRK05678 |
succinyl-CoA synthetase subunit alpha; Validated |
59-205 |
9.63e-06 |
|
succinyl-CoA synthetase subunit alpha; Validated
Pssm-ID: 180194 [Multi-domain] Cd Length: 291 Bit Score: 47.86 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 59 VNPNRA--EIQGLPAFASVAELPQA--PDVAIVAVPAP----QVLETVRAlgrqGARSAIVFSSGFsevgeagaAMQD-- 128
Cdd:PRK05678 39 VTPGKGgtTVLGLPVFNTVAEAVEAtgANASVIYVPPPfaadAILEAIDA----GIDLIVCITEGI--------PVLDml 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 129 AVVAAAREHGMRLLGPNALG---AFNSNLGYyaffstslergVP----LPGRVGIATQSGAYGAHLLGMARQRRLGTPIC 201
Cdd:PRK05678 107 EVKAYLERKKTRLIGPNCPGiitPGECKIGI-----------MPghihKKGRVGVVSRSGTLTYEAVAQLTDLGFGQSTC 175
|
....
gi 523497446 202 VATG 205
Cdd:PRK05678 176 VGIG 179
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
15-713 |
0e+00 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 716.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 15 FASLTPLIEPRSVAVIGASSDPTRIGGRPIAYMLRHGYAGQILPVNPNRAEIQGLPAFASVAELPQAPDVAIVAVPAPQV 94
Cdd:COG1042 3 TRSLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEGGFKGKIYPVNPKYDEVLGLPCYPSVADLPEPPDLAVIAVPAETV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 95 LETVRALGRQGARSAIVFSSGFSEVGEAGAAMQDAVVAAAREHGMRLLGPNALGAFNSNLGYYAFFSTslerGVPLPGRV 174
Cdd:COG1042 83 PDVVEECGEKGVKAAVVISAGFAETGEEGAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAP----VPPLPGNI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 175 GIATQSGAYGAHLLGMARQRRLGTPICVATGNEADVTLGDSIGWLVESPEIDVVMAYAESIRNVDSFLAALEAAHRaGKP 254
Cdd:COG1042 159 ALVSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAAR-GKP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 255 VILHKVGRSALGSRAALSHTASLAGDDKVLDAVLDDYAVIRARTTEELMDIAYLATRRIYPLGNSLGMITVSGGAGIIVS 334
Cdd:COG1042 238 VVVLKSGRSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 335 DVAEEVGLPMPPMPDMAQERLKARL-SFASPINPVDCTAQALNDLtlVRDFTESMVVDGGYRSLLAFFTQAGTAASigAR 413
Cdd:COG1042 318 DALEDLGLELAELSEETQAALRAVLpPFASVGNPVDITGDADPER--YAAALEALLADPNVDAVLVILTPTAMTDP--EE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 414 LAEQFRRIKeAHPERLFVVSVMGE---GEELAPYEEAGFALFEDPTRAVVAIQAMGRLGEAFARPLR------------- 477
Cdd:COG1042 394 VAEALIEAA-KGSGKPVLASWMGGdsvAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMEtpasedfdpdrer 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 478 -LRRPAGGLQLPASTPGEAEAKRLLARAGIESAAEAVLGSAEEAVAFAEGIGYPVVLKLASADIQHKSEIGGVLLGVSDA 556
Cdd:COG1042 473 aRAIIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 557 DAVRAGFQLLLRRAAEKAPQARLDGVLVARQLQGGVECFMGIQRDPLFGPVALFGLGGIFVEVLQDVVFRRCPFEVDEAE 636
Cdd:COG1042 553 EAVRAAFEEILARVRAARPDARIDGVLVQPMVPGGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKDVALRLPPLNEALAR 632
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523497446 637 VMIRSIRGAPLLLGARGRPRADVAALARLLSNLSRFAWEAGERLRSvDLNPVIALPEGQGAWAVDAVLEVEEVADGA 713
Cdd:COG1042 633 EMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILEL-DINPLLVVPEGVVAVDARIRLAPPAPPAPR 708
|
|
| AcCoA-syn-alpha |
TIGR02717 |
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ... |
18-467 |
1.38e-106 |
|
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it is believed that this group of ADP-dependent acetyl-CoA synthetases (ACS) act in the direction of acetate and ATP production in the organisms in which it has been characterized. In most species this protein exists as a fused alpha-beta domain polypeptide. In Pyrococcus and related species, however the domains exist as separate polypeptides. This model represents the alpha (N-terminal) domain. In Pyrococcus and related species there appears to have been the development of a paralogous family such that four other proteins are close relatives. In reference, one of these (along with its beta-domain partner) was characterized as ACS-II showing specificity for phenylacetyl-CoA. This model has been constructed to exclude these non-ACS-I paralogs. This may result in new, authentic ACS-I sequences falling below the trusted cutoff.
Pssm-ID: 131764 [Multi-domain] Cd Length: 447 Bit Score: 331.97 E-value: 1.38e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 18 LTPLIEPRSVAVIGASSDPTRIGGRPIAYMLRHGYAGQILPVNPNRAEIQGLPAFASVAELPQAPDVAIVAVPAPQVLET 97
Cdd:TIGR02717 1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEGGYKGKIYPVNPKAGEILGVKAYPSVLEIPDPVDLAVIVVPAKYVPQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 98 VRALGRQGARSAIVFSSGFSEVGEAGAAMQDAVVAAAREHGMRLLGPNALGAFNSNLGYYAFFSTSLergvPLPGRVGIA 177
Cdd:TIGR02717 81 VEECGEKGVKGAVVITAGFKEVGEEGAELEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPTM----PKKGGIAFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 178 TQSGAYGAHLLGMARQRRLGTPICVATGNEADVTLGDSIGWLVESPEIDVVMAYAESIRNVDSFL-AALEAAHRagKPVI 256
Cdd:TIGR02717 157 SQSGALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLkTAREISKK--KPIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 257 LHKVGRSALGSRAALSHTASLAGDDKVLDAVLDDYAVIRARTTEELMDIAYLATRRIYPLGNSLGMITVSGGAGIIVSDV 336
Cdd:TIGR02717 235 VLKSGTSEAGAKAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPKGNRVAIITNAGGPGVIATDA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 337 AEEVGLPMPPMPDMAQERLKARL-SFASPINPVDCTAQALNDL--TLVRDFTESMVVDGgyrsLLAFFTQagtAASIGAR 413
Cdd:TIGR02717 315 CEENGLELAELSEATKNKLRNILpPEASIKNPVDVLGDATPERyaKALKTVAEDENVDG----VVVVLTP---TAMTDPE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 523497446 414 -LAEQFRRIKEAHPERLFVVSVMGEGEELAP---YEEAGFALFEDPTRAVVAIQAMGR 467
Cdd:TIGR02717 388 eVAKGIIEGAKKSNEKPVVAGFMGGKSVDPAkriLEENGIPNYTFPERAVKALSALYR 445
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
493-706 |
1.21e-70 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 463918 [Multi-domain] Cd Length: 221 Bit Score: 229.67 E-value: 1.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 493 GEAEAKRLLARAGIESAAEAVLGSAEEAVAFAEGIGYPVVLKLASADIQHKSEIGGVLLGVSDADAVRAGFQLLLRRAAE 572
Cdd:pfam13549 11 TEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAAYEEILERVRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 573 KAPQARLDGVLVARQLQGGVECFMGIQRDPLFGPVALFGLGGIFVEVLQDVVFRRCPFEVDEAEVMIRSIRGAPLLLGAR 652
Cdd:pfam13549 91 YRPDARIEGVLVQPMAPGGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMIRRTRAYKLLKGYR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523497446 653 GRPRADVAALARLLSNLSRFAWEAGErLRSVDLNPVIAlpEGQGAWAVDAVLEV 706
Cdd:pfam13549 171 GEPPADLDALEDVLVRVSQLVIDFPE-IRELDINPLLA--DEDGVVALDARIRL 221
|
|
| Succ_CoA_lig |
pfam13607 |
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ... |
171-308 |
3.03e-43 |
|
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from Succinyl-CoA ligase alpha subunit and other related enzymes. A conserved histidine is involved in phosphoryl transfer.
Pssm-ID: 433345 [Multi-domain] Cd Length: 138 Bit Score: 152.62 E-value: 3.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 171 PGRVGIATQSGAYGAHLLGMARQRRLGTPICVATGNEADVTLGDSIGWLVESPEIDVVMAYAESIRNVDSFLAALEAAHR 250
Cdd:pfam13607 1 PGNIALVSQSGALGAALLDWARSRGIGFSKFVSLGNEADVDFADLLEYLADDPETRVILLYLEGIRDGRRFLRAARRAAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 523497446 251 AgKPVILHKVGRSALGSRAALSHTASLAGDDKVLDAVLDDYAVIRARTTEELMDIAYL 308
Cdd:pfam13607 81 R-KPVVVLKAGRSEAGARAAASHTGALAGSDAVYDAAFRQAGVIRVDDLEELFDAAEA 137
|
|
| CoA_binding_2 |
pfam13380 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
25-148 |
2.01e-26 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 433162 [Multi-domain] Cd Length: 116 Bit Score: 104.16 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 25 RSVAVIGASSDPTRIGGRPIAYMLRHGYagQILPVNPNRAEIQGLPAFASVAELPQAPDVAIVAVPAPQVLETVRALGRQ 104
Cdd:pfam13380 1 KTIAVVGASPNPGRPGYKVARYLLEHGY--PVIPVNPKAKEILGEPVYPSLADPPEPVDLVDVFRPPEAVPEIVEEALAL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 523497446 105 GARSAIVFSSGFSEvgeagaamqdAVVAAAREHGMRLLGPNALG 148
Cdd:pfam13380 79 GAKAVWLQPGIENE----------EAAAIARAAGIRVVGDRCLG 112
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
23-116 |
6.16e-19 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 214881 [Multi-domain] Cd Length: 100 Bit Score: 82.17 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 23 EPRSVAVIGASSDPTRIGGRPIAYMLRHG--YAGQILP--VNPnraEIQGLPAFASVAELPQA--PDVAIVAVPAPQVLE 96
Cdd:smart00881 4 PNTSVAVVGASGNLGSFGLAVMRNLLEYGtkFVGGVYPgkVGP---KVDGVPVYDSVAEAPEEtgVDVAVIFVPAEAAPD 80
|
90 100
....*....|....*....|
gi 523497446 97 TVRALGRQGARSAIVFSSGF 116
Cdd:smart00881 81 AIDEAIEAGIKGIVVITEGI 100
|
|
| YccU |
COG1832 |
Predicted CoA-binding protein [General function prediction only]; |
21-107 |
7.58e-14 |
|
Predicted CoA-binding protein [General function prediction only];
Pssm-ID: 441437 [Multi-domain] Cd Length: 138 Bit Score: 69.00 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 21 LIEPRSVAVIGASSDPTRIGGRPIAYMLRHGYagQILPVNPNRAEIQGLPAFASVAELPQAPDVAIVAVPAPQVLETVRA 100
Cdd:COG1832 13 LKSAKTIAVVGLSPNPERPSYYVAKYLQRHGY--RVIPVNPGAKEILGEKVYASLADIPEPVDIVDVFRRSEAVPEIVDE 90
|
....*..
gi 523497446 101 LGRQGAR 107
Cdd:COG1832 91 AIAIGAK 97
|
|
| CoA_binding |
pfam02629 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
23-115 |
2.43e-10 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 396961 [Multi-domain] Cd Length: 97 Bit Score: 57.60 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 23 EPRSVAVIGASSDPTRIGGRPIAYMLRHGYAgQILPVNPNRA--EIQGLPAFASVAELPQ--APDVAIVAVPAPQVLETV 98
Cdd:pfam02629 2 KDTKVIVIGAGGLGIQGLNYHFIQMLGYGIK-MVFGVNPGKGgtEILGIPVYNSVDELEEktGVDVAVITVPAPFAQEAI 80
|
90
....*....|....*..
gi 523497446 99 RALGRQGARSAIVFSSG 115
Cdd:pfam02629 81 DELVDAGIKGIVNITPG 97
|
|
| PRK05678 |
PRK05678 |
succinyl-CoA synthetase subunit alpha; Validated |
59-205 |
9.63e-06 |
|
succinyl-CoA synthetase subunit alpha; Validated
Pssm-ID: 180194 [Multi-domain] Cd Length: 291 Bit Score: 47.86 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 59 VNPNRA--EIQGLPAFASVAELPQA--PDVAIVAVPAP----QVLETVRAlgrqGARSAIVFSSGFsevgeagaAMQD-- 128
Cdd:PRK05678 39 VTPGKGgtTVLGLPVFNTVAEAVEAtgANASVIYVPPPfaadAILEAIDA----GIDLIVCITEGI--------PVLDml 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 129 AVVAAAREHGMRLLGPNALG---AFNSNLGYyaffstslergVP----LPGRVGIATQSGAYGAHLLGMARQRRLGTPIC 201
Cdd:PRK05678 107 EVKAYLERKKTRLIGPNCPGiitPGECKIGI-----------MPghihKKGRVGVVSRSGTLTYEAVAQLTDLGFGQSTC 175
|
....
gi 523497446 202 VATG 205
Cdd:PRK05678 176 VGIG 179
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
495-584 |
3.35e-05 |
|
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: 46.02 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 495 AEAKRLLARAGIESAAEAVLGSAEEAVAFAEGIGYPVVLK---LASADiqhkseigGVLLgVSDADAVRAGFQLLLrraA 571
Cdd:COG0439 56 VLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKpadGAGSR--------GVRV-VRDEEELEAALAEAR---A 123
|
90
....*....|...
gi 523497446 572 EKAPQARLDGVLV 584
Cdd:COG0439 124 EAKAGSPNGEVLV 136
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
59-208 |
5.90e-05 |
|
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA synthetase, alpha subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439844 [Multi-domain] Cd Length: 288 Bit Score: 45.44 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 59 VNPNRA--EIQGLPAFASVAELPQA--PDVAIVAVPAPQV----LETVRAlgrqGARSAIVFSSGFSEvgeagaamQDA- 129
Cdd:COG0074 38 VTPGKGgqTVLGVPVFDTVAEAVEEtgADASVIFVPPPFAadaiLEAIDA----GIKLIVCITEGIPV--------LDMv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 130 -VVAAAREHGMRLLGPNALGAFN---SNLG-YYAFFSTslergvplPGRVGIATQSG--AY-GAHLLgmaRQRRLGTPIC 201
Cdd:COG0074 106 rVKRYAKAKGTRLIGPNCPGIITpgeCKLGiMPGHIFK--------PGRVGIVSRSGtlTYeAVWQL---TQAGLGQSTC 174
|
....*..
gi 523497446 202 VATGNEA 208
Cdd:COG0074 175 VGIGGDP 181
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
497-534 |
4.10e-04 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 43.46 E-value: 4.10e-04
10 20 30
....*....|....*....|....*....|....*...
gi 523497446 497 AKRLLARAGIESAAEAVLGSAEEAVAFAEGIGYPVVLK 534
Cdd:COG0151 106 AKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVK 143
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
496-590 |
1.43e-03 |
|
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: 40.75 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 496 EAKRLLARAGIESA--AEAVLGSAEEAVAFAEGIGYPVVLKLASAdiqhkseIGGVLLG-VSDADAVRAGFQLLLRRAAE 572
Cdd:pfam02786 4 LFKAAMKEAGVPTVpgTAGPVETEEEALAAAKEIGYPVIIKAAFG-------GGGLGMGiARNEEELAELFALALAEAPA 76
|
90
....*....|....*...
gi 523497446 573 KAPQarlDGVLVARQLQG 590
Cdd:pfam02786 77 AFGN---PQVLVEKSLKG 91
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
496-571 |
1.64e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 41.55 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 496 EAKRLLARAGIE--SAAEAVLGSAEEAVAFAEGIGYPVVLKlASAdiqhkseiGGVLLG---VSDADAVRAGFQLLLRRA 570
Cdd:PRK06111 118 EARRAMQAAGVPvvPGITTNLEDAEEAIAIARQIGYPVMLK-ASA--------GGGGIGmqlVETEQELTKAFESNKKRA 188
|
.
gi 523497446 571 A 571
Cdd:PRK06111 189 A 189
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
498-532 |
1.92e-03 |
|
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: 41.40 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|....*
gi 523497446 498 KRLLARAGIESAAEAVLGSAEEAVAFAEGIGYPVV 532
Cdd:COG0458 119 KELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVI 153
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
498-536 |
2.64e-03 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 40.83 E-value: 2.64e-03
10 20 30
....*....|....*....|....*....|....*....
gi 523497446 498 KRLLARAGIESAAEAVLGSAEEAVAFAEGIGYPVVLKLA 536
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTR 132
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
498-590 |
5.57e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 40.14 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523497446 498 KRLLARAGIESAAEAVLGSAEEAVAFAEGIGYPVVLKlaSADIQHkseiG-GVLLGVSDADAVRAGFQLllrrAAEKApq 576
Cdd:PRK14016 219 KRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVK--PLDGNH----GrGVTVNITTREEIEAAYAV----ASKES-- 286
|
90
....*....|....
gi 523497446 577 arlDGVLVARQLQG 590
Cdd:PRK14016 287 ---SDVIVERYIPG 297
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
498-534 |
6.53e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 39.37 E-value: 6.53e-03
10 20 30
....*....|....*....|....*....|....*..
gi 523497446 498 KRLLARAGIESAAEAVLGSAEEAVAFAEGIGYPVVLK 534
Cdd:PRK06019 105 KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLK 141
|
|
| |
