|
Name |
Accession |
Description |
Interval |
E-value |
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
3-702 |
0e+00 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 834.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 3 RLSALFDPETVAVVGATDREGAVGRAILENLRD-GFAGEVVPINPSREAVLGLECYEDATSAP-PIDLAVVVVPPDIVIE 80
Cdd:COG1042 5 SLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEgGFKGKIYPVNPKYDEVLGLPCYPSVADLPePPDLAVIAVPAETVPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 81 SMRNLAAAGTENVVVITAGFAETGGEGAQRERQLREIAAEYDLNVVGPNSLGIMATSTGMNATFGPEDALEGSISFMSQS 160
Cdd:COG1042 85 VVEECGEKGVKAAVVISAGFAETGEEGAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAPVPPLPGNIALVSQS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 161 GAFITAVLDWANEQGIGFRDVVSLGNKTVLDETDFVREWGDDPETDVIIGYLEDIDDGRGFIDAAREVTDDTPIVLVKSG 240
Cdd:COG1042 165 GALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPVVVLKSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 241 RTDAGAQAASSHTGAIAGSERAYEAGLEQAGVLRARSVQELFDYARALSGLPEPESDGVAVVTNAGGPGVLTTDAVGDST 320
Cdd:COG1042 245 RSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADALEDLG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 321 LEMADFADETIDRLGEAMPDEANVYNPIDAIGDADVERFGEALEIALADPNVGSAVVVAAPTAVLSYDDLAETVIERLEA 400
Cdd:COG1042 325 LELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALIEAAKG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 401 HDTPVVTCLMGGERARNAEKTLRESGVPNYFDPSRAVSGLDALARYRDIRDRTVKRP--ETFDVDRERAREILARTKRRT 478
Cdd:COG1042 405 SGKPVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPasEDFDPDRERARAIIEAALAEG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 479 DNRL-GVESMDLLEAYGIPTPDGEIVDDPDRAREVAASIAGDVVMKIVSPDISHKSDIGGVKVGVADED-VYDAYEDVVA 556
Cdd:COG1042 485 RGVLtEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAEaVRAAFEEILA 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 557 RARNYQPDATITGVQIQEMLDleSSTETIVGMNRDPQFgplllyglggIFVEILEDTSVRVAPIDEGEAHEMVDEITAAP 636
Cdd:COG1042 565 RVRAARPDARIDGVLVQPMVP--GGVELIVGVKRDPVFgpvimfglggIFVEVLKDVALRLPPLNEALAREMIRELRAAK 642
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493474997 637 LLRGARGREPADVDDVVETIQRLSQLVTDFPSILELDINPLVAGPDGVQAIDLRLTVDADELDTEE 702
Cdd:COG1042 643 LLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAPPAPPAPR 708
|
|
| AcCoA-syn-alpha |
TIGR02717 |
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ... |
4-447 |
0e+00 |
|
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: 538.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 4 LSALFDPETVAVVGATDREGAVGRAILENLRD-GFAGEVVPINPSREAVLGLECYEDATSAP-PIDLAVVVVPPDIVIES 81
Cdd:TIGR02717 1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEgGYKGKIYPVNPKAGEILGVKAYPSVLEIPdPVDLAVIVVPAKYVPQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 82 MRNLAAAGTENVVVITAGFAETGGEGAQRERQLREIAAEYDLNVVGPNSLGIMATSTGMNATFGPEDALEGSISFMSQSG 161
Cdd:TIGR02717 81 VEECGEKGVKGAVVITAGFKEVGEEGAELEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPTMPKKGGIAFISQSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 162 AFITAVLDWANEQGIGFRDVVSLGNKTVLDETDFVREWGDDPETDVIIGYLEDIDDGRGFIDAAREVTDDTPIVLVKSGR 241
Cdd:TIGR02717 161 ALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREISKKKPIVVLKSGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 242 TDAGAQAASSHTGAIAGSERAYEAGLEQAGVLRARSVQELFDYARALSGLPEPESDGVAVVTNAGGPGVLTTDAVGDSTL 321
Cdd:TIGR02717 241 SEAGAKAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPKGNRVAIITNAGGPGVIATDACEENGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 322 EMADFADETIDRLGEAMPDEANVYNPIDAIGDADVERFGEALEIALADPNVGSAVVVAAPTAVLSYDDLAETVIE-RLEA 400
Cdd:TIGR02717 321 ELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGVVVVLTPTAMTDPEEVAKGIIEgAKKS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 493474997 401 HDTPVVTCLMGGERARNAEKTLRESGVPNYFDPSRAVSGLDALARYR 447
Cdd:TIGR02717 401 NEKPVVAGFMGGKSVDPAKRILEENGIPNYTFPERAVKALSALYRYA 447
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
472-693 |
6.91e-79 |
|
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: 250.86 E-value: 6.91e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 472 ARTKRRTdNRLGVESMDLLEAYGIPTPDGEIVDDPDRAREVAASIAGDVVMKIVSPDISHKSDIGGVKVGVAD-EDVYDA 550
Cdd:pfam13549 2 ALAEGRT-VLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSaEAVRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 551 YEDVVARARNYQPDATITGVQIQEMLdlESSTETIVGMNRDPQFGPLLLYGLGGIFVEILEDTSVRVAPIDEGEAHEMVD 630
Cdd:pfam13549 81 YEEILERVRRYRPDARIEGVLVQPMA--PGGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMIR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493474997 631 EITAAPLLRGARGREPADVDDVVETIQRLSQLVTDFPSILELDINPLVAGPDGVQAIDLRLTV 693
Cdd:pfam13549 159 RTRAYKLLKGYRGEPPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADEDGVVALDARIRL 221
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
7-100 |
5.54e-11 |
|
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: 59.45 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 7 LFDPET-VAVVGATDREGAVGRAILENLRDG---FAGEVVP--INPSreaVLGLECYEDATSAP---PIDLAVVVVPPDI 77
Cdd:smart00881 1 LLNPNTsVAVVGASGNLGSFGLAVMRNLLEYgtkFVGGVYPgkVGPK---VDGVPVYDSVAEAPeetGVDVAVIFVPAEA 77
|
90 100
....*....|....*....|...
gi 493474997 78 VIESMRNLAAAGTENVVVITAGF 100
Cdd:smart00881 78 APDAIDEAIEAGIKGIVVITEGI 100
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
488-550 |
6.41e-05 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 45.85 E-value: 6.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493474997 488 DLLEAYGIPTPDGEIVDDPDRAREVAASIAGDVVMkiVspdishKSDI--------GGVKVGVADEDVYDA 550
Cdd:PRK00696 10 ELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWV--V------KAQVhaggrgkaGGVKLAKSPEEAREF 72
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
3-702 |
0e+00 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 834.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 3 RLSALFDPETVAVVGATDREGAVGRAILENLRD-GFAGEVVPINPSREAVLGLECYEDATSAP-PIDLAVVVVPPDIVIE 80
Cdd:COG1042 5 SLDALFRPRSVAVIGASDRPGKVGGRVLRNLLEgGFKGKIYPVNPKYDEVLGLPCYPSVADLPePPDLAVIAVPAETVPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 81 SMRNLAAAGTENVVVITAGFAETGGEGAQRERQLREIAAEYDLNVVGPNSLGIMATSTGMNATFGPEDALEGSISFMSQS 160
Cdd:COG1042 85 VVEECGEKGVKAAVVISAGFAETGEEGAALEQELLEIARRYGMRLLGPNCLGLINPATGLNATFAPVPPLPGNIALVSQS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 161 GAFITAVLDWANEQGIGFRDVVSLGNKTVLDETDFVREWGDDPETDVIIGYLEDIDDGRGFIDAAREVTDDTPIVLVKSG 240
Cdd:COG1042 165 GALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGIRDGRRFLSAARAAARGKPVVVLKSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 241 RTDAGAQAASSHTGAIAGSERAYEAGLEQAGVLRARSVQELFDYARALSGLPEPESDGVAVVTNAGGPGVLTTDAVGDST 320
Cdd:COG1042 245 RSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPRGRRLAIVTNSGGPGVLAADALEDLG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 321 LEMADFADETIDRLGEAMPDEANVYNPIDAIGDADVERFGEALEIALADPNVGSAVVVAAPTAVLSYDDLAETVIERLEA 400
Cdd:COG1042 325 LELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAVLVILTPTAMTDPEEVAEALIEAAKG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 401 HDTPVVTCLMGGERARNAEKTLRESGVPNYFDPSRAVSGLDALARYRDIRDRTVKRP--ETFDVDRERAREILARTKRRT 478
Cdd:COG1042 405 SGKPVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLMETPasEDFDPDRERARAIIEAALAEG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 479 DNRL-GVESMDLLEAYGIPTPDGEIVDDPDRAREVAASIAGDVVMKIVSPDISHKSDIGGVKVGVADED-VYDAYEDVVA 556
Cdd:COG1042 485 RGVLtEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRDAEaVRAAFEEILA 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 557 RARNYQPDATITGVQIQEMLDleSSTETIVGMNRDPQFgplllyglggIFVEILEDTSVRVAPIDEGEAHEMVDEITAAP 636
Cdd:COG1042 565 RVRAARPDARIDGVLVQPMVP--GGVELIVGVKRDPVFgpvimfglggIFVEVLKDVALRLPPLNEALAREMIRELRAAK 642
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493474997 637 LLRGARGREPADVDDVVETIQRLSQLVTDFPSILELDINPLVAGPDGVQAIDLRLTVDADELDTEE 702
Cdd:COG1042 643 LLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIRLAPPAPPAPR 708
|
|
| AcCoA-syn-alpha |
TIGR02717 |
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ... |
4-447 |
0e+00 |
|
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: 538.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 4 LSALFDPETVAVVGATDREGAVGRAILENLRD-GFAGEVVPINPSREAVLGLECYEDATSAP-PIDLAVVVVPPDIVIES 81
Cdd:TIGR02717 1 LEHLFNPKSVAVIGASRDPGKVGYAIMKNLIEgGYKGKIYPVNPKAGEILGVKAYPSVLEIPdPVDLAVIVVPAKYVPQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 82 MRNLAAAGTENVVVITAGFAETGGEGAQRERQLREIAAEYDLNVVGPNSLGIMATSTGMNATFGPEDALEGSISFMSQSG 161
Cdd:TIGR02717 81 VEECGEKGVKGAVVITAGFKEVGEEGAELEQELVEIARKYGMRLLGPNCLGIINTHIKLNATFAPTMPKKGGIAFISQSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 162 AFITAVLDWANEQGIGFRDVVSLGNKTVLDETDFVREWGDDPETDVIIGYLEDIDDGRGFIDAAREVTDDTPIVLVKSGR 241
Cdd:TIGR02717 161 ALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGIKDGRKFLKTAREISKKKPIVVLKSGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 242 TDAGAQAASSHTGAIAGSERAYEAGLEQAGVLRARSVQELFDYARALSGLPEPESDGVAVVTNAGGPGVLTTDAVGDSTL 321
Cdd:TIGR02717 241 SEAGAKAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPKGNRVAIITNAGGPGVIATDACEENGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 322 EMADFADETIDRLGEAMPDEANVYNPIDAIGDADVERFGEALEIALADPNVGSAVVVAAPTAVLSYDDLAETVIE-RLEA 400
Cdd:TIGR02717 321 ELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGVVVVLTPTAMTDPEEVAKGIIEgAKKS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 493474997 401 HDTPVVTCLMGGERARNAEKTLRESGVPNYFDPSRAVSGLDALARYR 447
Cdd:TIGR02717 401 NEKPVVAGFMGGKSVDPAKRILEENGIPNYTFPERAVKALSALYRYA 447
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
472-693 |
6.91e-79 |
|
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: 250.86 E-value: 6.91e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 472 ARTKRRTdNRLGVESMDLLEAYGIPTPDGEIVDDPDRAREVAASIAGDVVMKIVSPDISHKSDIGGVKVGVAD-EDVYDA 550
Cdd:pfam13549 2 ALAEGRT-VLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSaEAVRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 551 YEDVVARARNYQPDATITGVQIQEMLdlESSTETIVGMNRDPQFGPLLLYGLGGIFVEILEDTSVRVAPIDEGEAHEMVD 630
Cdd:pfam13549 81 YEEILERVRRYRPDARIEGVLVQPMA--PGGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMIR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493474997 631 EITAAPLLRGARGREPADVDDVVETIQRLSQLVTDFPSILELDINPLVAGPDGVQAIDLRLTV 693
Cdd:pfam13549 159 RTRAYKLLKGYRGEPPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADEDGVVALDARIRL 221
|
|
| Succ_CoA_lig |
pfam13607 |
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ... |
152-288 |
3.39e-59 |
|
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: 195.76 E-value: 3.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 152 GSISFMSQSGAFITAVLDWANEQGIGFRDVVSLGNKTVLDETDFVREWGDDPETDVIIGYLEDIDDGRGFIDAAREVTDD 231
Cdd:pfam13607 2 GNIALVSQSGALGAALLDWARSRGIGFSKFVSLGNEADVDFADLLEYLADDPETRVILLYLEGIRDGRRFLRAARRAARR 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 493474997 232 TPIVLVKSGRTDAGAQAASSHTGAIAGSERAYEAGLEQAGVLRARSVQELFDYARAL 288
Cdd:pfam13607 82 KPVVVLKAGRSEAGARAAASHTGALAGSDAVYDAAFRQAGVIRVDDLEELFDAAEAL 138
|
|
| CoA_binding_2 |
pfam13380 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
12-134 |
9.60e-14 |
|
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: 67.95 E-value: 9.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 12 TVAVVGATDREGAVGRAILENLRD-GFagEVVPINPSREAVLGLECYED-ATSAPPIDLAVVVVPPDIVIESMRNLAAAG 89
Cdd:pfam13380 2 TIAVVGASPNPGRPGYKVARYLLEhGY--PVIPVNPKAKEILGEPVYPSlADPPEPVDLVDVFRPPEAVPEIVEEALALG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 493474997 90 TENVVVITAGFAEtggegaqrerQLREIAAEYDLNVVGPNSLGIM 134
Cdd:pfam13380 80 AKAVWLQPGIENE----------EAAAIARAAGIRVVGDRCLGVE 114
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
7-100 |
5.54e-11 |
|
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: 59.45 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 7 LFDPET-VAVVGATDREGAVGRAILENLRDG---FAGEVVP--INPSreaVLGLECYEDATSAP---PIDLAVVVVPPDI 77
Cdd:smart00881 1 LLNPNTsVAVVGASGNLGSFGLAVMRNLLEYgtkFVGGVYPgkVGPK---VDGVPVYDSVAEAPeetGVDVAVIFVPAEA 77
|
90 100
....*....|....*....|...
gi 493474997 78 VIESMRNLAAAGTENVVVITAGF 100
Cdd:smart00881 78 APDAIDEAIEAGIKGIVVITEGI 100
|
|
| Ligase_CoA_2 |
pfam19045 |
Ligase-CoA domain; This domain is related to pfam00549 and adopts a flavodoxin fold. |
299-446 |
4.27e-07 |
|
Ligase-CoA domain; This domain is related to pfam00549 and adopts a flavodoxin fold.
Pssm-ID: 408815 Cd Length: 162 Bit Score: 50.34 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 299 VAVVTNAGGPGVLTTDAVGDSTLEMADFADETIDRLGEAMPDEANVYNPIDAIGDADVERFGEALEIALADPNVGSAVVV 378
Cdd:pfam19045 1 VVIITGAGGSGVLLSDACVDNGLTLMAIPPDLDAAFRKFIPPFGAAGNPVDITGGEPPSTYEATIRLGLEDPRIHALILG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493474997 379 ---AAPTAVLSYDDLAETVIE--RLEAHDTPVVTCLMGGERARNAEKTLRESGVPNY-FDPSRAVSGLDALARY 446
Cdd:pfam19045 81 ywhTIVTPPMVFAELMVRVVEemRAKGIDKPVVASLAGDVEVEEAAEYLFQHGIVAYpYTTEKPVAVLGAKYRW 154
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
86-281 |
1.51e-06 |
|
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: 50.44 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 86 AAAGTENVVVITagfaetggEG--AQRERQLREIAAEYDLNVVGPNSLGIMATSTGMNATFGPEDALEGSISFMSQSGAF 163
Cdd:COG0074 85 IDAGIKLIVCIT--------EGipVLDMVRVKRYAKAKGTRLIGPNCPGIITPGECKLGIMPGHIFKPGRVGIVSRSGTL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 164 ITAVLDWANEQGIGFRDVVSLGNKTV--LDETDFVREWGDDPETDVII------GYLEdiddgrgfIDAAREVTD--DTP 233
Cdd:COG0074 157 TYEAVWQLTQAGLGQSTCVGIGGDPIigTSFIDVLELFEEDPETEAIVmigeigGSAE--------EEAAEYIKEnmTKP 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493474997 234 IVLVKSGRT--------DAGAQAASShtgaiAGSERAYEAGLEQAGVLRARSVQEL 281
Cdd:COG0074 229 VVAYIAGRTappgkrmgHAGAIISGG-----KGTAESKIEALEAAGVPVAESPSEI 279
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
485-678 |
6.00e-06 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 47.64 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 485 ESMDLLEAYGIPTPDGEIVDDPDRAREVAASIAGDVVMKivspdishKSDI--------GGVKVGVADEDVYDAYEDVV- 555
Cdd:pfam08442 6 QAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVV--------KAQVlaggrgkaGGVKLAKSPEEAKEVAKEMLg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 556 ARARNYQPDA---TITGVQIQEMLDLESstETIVG--MNRDPQfgplllyGLGGIF-----VEILE------DTSVRVA- 618
Cdd:pfam08442 78 KNLVTKQTGPdgqPVNKVLVEEALDIKK--EYYLSivLDRASK-------GPVIIAsteggVDIEEvaaknpEKIHKFPi 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493474997 619 ----PIDEGEAHEMVDEItaapllrgarGREPADVDDVVETIQRLSQLVTDFPSILeLDINPLV 678
Cdd:pfam08442 149 dplkGLTPYQAREIAFKL----------GLPGELIKQAADIIKKLYKLFVEYDATL-VEINPLV 201
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
488-550 |
6.41e-05 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 45.85 E-value: 6.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493474997 488 DLLEAYGIPTPDGEIVDDPDRAREVAASIAGDVVMkiVspdishKSDI--------GGVKVGVADEDVYDA 550
Cdd:PRK00696 10 ELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWV--V------KAQVhaggrgkaGGVKLAKSPEEAREF 72
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
485-522 |
3.79e-04 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 43.50 E-value: 3.79e-04
10 20 30
....*....|....*....|....*....|....*...
gi 493474997 485 ESMDLLEAYGIPTPDGEIVDDPDRAREVAASIAGDVVM 522
Cdd:COG0045 7 QAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVV 44
|
|
| YccU |
COG1832 |
Predicted CoA-binding protein [General function prediction only]; |
7-68 |
4.87e-04 |
|
Predicted CoA-binding protein [General function prediction only];
Pssm-ID: 441437 [Multi-domain] Cd Length: 138 Bit Score: 40.88 E-value: 4.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493474997 7 LFDPETVAVVGATDREG----AVGRAILENlrdGFagEVVPINPSREAVLGLECYEDATSAP-PIDL 68
Cdd:COG1832 13 LKSAKTIAVVGLSPNPErpsyYVAKYLQRH---GY--RVIPVNPGAKEILGEKVYASLADIPePVDI 74
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
488-586 |
2.09e-03 |
|
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: 40.63 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 488 DLLEAYGIPTPDGEIVDDPDRAREVAASIAGDVVMKivsPDISHKSDigGVKVgVAD-EDVYDAYEDVVARARNYQPDAT 566
Cdd:COG0439 60 EALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVK---PADGAGSR--GVRV-VRDeEELEAALAEARAEAKAGSPNGE 133
|
90 100
....*....|....*....|.
gi 493474997 567 itgVQIQEMLD-LESSTETIV 586
Cdd:COG0439 134 ---VLVEEFLEgREYSVEGLV 151
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
489-523 |
3.55e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 40.52 E-value: 3.55e-03
10 20 30
....*....|....*....|....*....|....*
gi 493474997 489 LLEAYGIPTPDGEIVDDPDRAREVAASIAGDVVMK 523
Cdd:PRK14016 221 LLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVK 255
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
484-593 |
4.72e-03 |
|
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: 39.54 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493474997 484 VESMDLLEAYGIPTPDGEIVDDPDRAREVAASIAGDVVMKivsPDISHksdiGGVKVGVADEDvyDAYEDVVARARNYQP 563
Cdd:COG0189 98 LFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLK---PLDGS----GGRGVFLVEDE--DALESILEALTELGS 168
|
90 100 110
....*....|....*....|....*....|....*....
gi 493474997 564 DATItgvqIQEMLDLESST---------ETIVGMNRDPQ 593
Cdd:COG0189 169 EPVL----VQEFIPEEDGRdirvlvvggEPVAAIRRIPA 203
|
|
|