|
Name |
Accession |
Description |
Interval |
E-value |
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
5-393 |
0e+00 |
|
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: 568.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 5 LHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLAGGRGKGtfegglkGGVKIVFSPEEAKAVSSR 84
Cdd:COG0045 3 LHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKA-------GGVKLAKSPEEAREAAEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 85 MIGKKLFTKQTGEKGRICNQVFVCERRYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPDAIIKEPIDIVEGI 164
Cdd:COG0045 76 ILGMTLVTHQTGPKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 165 KKEQAVRLAQKMGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVEDASGVVMCMDAKINFDSNSAYRQKKIFDMQDW 244
Cdd:COG0045 156 QPYQARELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 245 TQEDERDRQAAKADLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAIL 324
Cdd:COG0045 236 SEEDPLEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAIL 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3821927 325 VNIFGGIMRCDVIAQGIVVAVKDLDLKIPVVVRLQGTRVDDAKALITASGLKILACDDLDEAAKMVVKL 393
Cdd:COG0045 316 VNIFGGITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAESGLNIIAADTLEEAAKKAVEL 384
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
5-395 |
0e+00 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 535.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 5 LHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLAGGRGKGtfegglkGGVKIVFSPEEAKAVSSR 84
Cdd:PRK00696 3 LHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKA-------GGVKLAKSPEEAREFAKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 85 MIGKKLFTKQTGEKGRICNQVFVCERRYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPDAIIKEPIDIVEGI 164
Cdd:PRK00696 76 ILGMTLVTHQTGPKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 165 KKEQAVRLAQKMGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVEDASGVVMCMDAKINFDSNSAYRQKKIFDMQDW 244
Cdd:PRK00696 156 QPFQAREIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 245 TQEDERDRQAAKADLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAIL 324
Cdd:PRK00696 236 SEEDPLEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAIL 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3821927 325 VNIFGGIMRCDVIAQGIVVAVKDLDLKIPVVVRLQGTRVDDAKALITASGLKILACDDLDEAAKMVVKLSE 395
Cdd:PRK00696 316 VNIFGGITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAESGLNIIAADTLDDAAQKAVEAAK 386
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
5-395 |
2.48e-159 |
|
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases model (pfam00549). The C-terminal half is described by the ATP-grasp model (pfam02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G [Energy metabolism, TCA cycle]
Pssm-ID: 273396 [Multi-domain] Cd Length: 386 Bit Score: 453.76 E-value: 2.48e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 5 LHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLAGGRGKGtfegglkGGVKIVFSPEEAKAVSSR 84
Cdd:TIGR01016 3 LHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAGPVVVKAQVHAGGRGKA-------GGVKVAKSKEEARAAAEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 85 MIGKKLFTKQTGEKGRICNQVFVCERRYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPDAIIKEPIDIVEGI 164
Cdd:TIGR01016 76 LLGKELVTNQTDPLGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 165 KKEQAVRLAQKMGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVEDASGVVMCMDAKINFDSNSAYRQKKIFDMQDW 244
Cdd:TIGR01016 156 LPYQAREIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 245 TQEDERDRQAAKADLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAIL 324
Cdd:TIGR01016 236 SQEDPREVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVF 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3821927 325 VNIFGGIMRCDVIAQGIVVAVKDLDLKIPVVVRLQGTRVDDAKALITASGLKILACDDLDEAAKMVVKLSE 395
Cdd:TIGR01016 316 INIFGGITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAESGLNIIFATSMEEAAEKAVEAAE 386
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
4-212 |
3.74e-91 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 273.37 E-value: 3.74e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 4 SLHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLAGGRGKGtfegglkGGVKIVFSPEEAKAVSS 83
Cdd:pfam08442 1 NLHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRGKA-------GGVKLAKSPEEAKEVAK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 84 RMIGKKLFTKQTGEKGRICNQVFVCERRYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPDAIIKEPIDIVEG 163
Cdd:pfam08442 74 EMLGKNLVTKQTGPDGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPVIIASTEGGVDIEEVAAKNPEKIHKFPIDPLKG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 3821927 164 IKKEQAVRLAQKMGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVE 212
Cdd:pfam08442 154 LTPYQAREIAFKLGLPGELIKQAADIIKKLYKLFVEYDATLVEINPLVE 202
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
5-393 |
0e+00 |
|
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: 568.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 5 LHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLAGGRGKGtfegglkGGVKIVFSPEEAKAVSSR 84
Cdd:COG0045 3 LHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKA-------GGVKLAKSPEEAREAAEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 85 MIGKKLFTKQTGEKGRICNQVFVCERRYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPDAIIKEPIDIVEGI 164
Cdd:COG0045 76 ILGMTLVTHQTGPKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 165 KKEQAVRLAQKMGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVEDASGVVMCMDAKINFDSNSAYRQKKIFDMQDW 244
Cdd:COG0045 156 QPYQARELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 245 TQEDERDRQAAKADLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAIL 324
Cdd:COG0045 236 SEEDPLEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAIL 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3821927 325 VNIFGGIMRCDVIAQGIVVAVKDLDLKIPVVVRLQGTRVDDAKALITASGLKILACDDLDEAAKMVVKL 393
Cdd:COG0045 316 VNIFGGITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAESGLNIIAADTLEEAAKKAVEL 384
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
5-395 |
0e+00 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 535.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 5 LHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLAGGRGKGtfegglkGGVKIVFSPEEAKAVSSR 84
Cdd:PRK00696 3 LHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKA-------GGVKLAKSPEEAREFAKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 85 MIGKKLFTKQTGEKGRICNQVFVCERRYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPDAIIKEPIDIVEGI 164
Cdd:PRK00696 76 ILGMTLVTHQTGPKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 165 KKEQAVRLAQKMGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVEDASGVVMCMDAKINFDSNSAYRQKKIFDMQDW 244
Cdd:PRK00696 156 QPFQAREIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 245 TQEDERDRQAAKADLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAIL 324
Cdd:PRK00696 236 SEEDPLEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAIL 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3821927 325 VNIFGGIMRCDVIAQGIVVAVKDLDLKIPVVVRLQGTRVDDAKALITASGLKILACDDLDEAAKMVVKLSE 395
Cdd:PRK00696 316 VNIFGGITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAESGLNIIAADTLDDAAQKAVEAAK 386
|
|
| PLN00124 |
PLN00124 |
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional |
1-396 |
0e+00 |
|
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional
Pssm-ID: 177736 [Multi-domain] Cd Length: 422 Bit Score: 535.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 1 RRLSLHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEI--GSKDLVIKAQVLAGGRGKGTFEGGLKGGVKIVfSPEEA 78
Cdd:PLN00124 26 RRLNIHEYQGAELMSKYGVNVPKGAAASSLDEVKKALEKMfpDEGEVVVKSQILAGGRGLGTFKNGLKGGVHIV-KKDKA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 79 KAVSSRMIGKKLFTKQTGEKGRICNQVFVCERRYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPDAIIKEPI 158
Cdd:PLN00124 105 EELAGKMLGQILVTKQTGPAGKPVNKVYLCEKMSLVNEMYFAILLDRASAGPLIIACSKGGTSIEDLAEKFPEKIIKVPI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 159 DIVEGIKKEQAVRLAQKMGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVEDASGVVMCMDAKINFDSNSAYRQKKI 238
Cdd:PLN00124 185 DIFKGITDEDAAKVVDGLAPKVADRNDAIEQVKKLYKLFCKCDCTMVEINPLAETADGQLVAADAKLNFDDNAAFRQKEI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 239 FDMQDWTQEDERDRQAAKADLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDK 318
Cdd:PLN00124 265 FALRDTSQEDPREVAAAKADLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGSPANFLDVGGNASEQQVVEAFKILTSDD 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3821927 319 KVLAILVNIFGGIMRCDVIAQGIVVAVKDLDLKIPVVVRLQGTRVDDAKALITASGLKILACDDLDEAAKMVVKLSEI 396
Cdd:PLN00124 345 KVKAILVNIFGGIMKCDVIASGIVNAAKQVGLKVPLVVRLEGTNVDQGKRILKESGMTLITAEDLDDAAEKAVKALAI 422
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
5-395 |
2.48e-159 |
|
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases model (pfam00549). The C-terminal half is described by the ATP-grasp model (pfam02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G [Energy metabolism, TCA cycle]
Pssm-ID: 273396 [Multi-domain] Cd Length: 386 Bit Score: 453.76 E-value: 2.48e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 5 LHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLAGGRGKGtfegglkGGVKIVFSPEEAKAVSSR 84
Cdd:TIGR01016 3 LHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAGPVVVKAQVHAGGRGKA-------GGVKVAKSKEEARAAAEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 85 MIGKKLFTKQTGEKGRICNQVFVCERRYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPDAIIKEPIDIVEGI 164
Cdd:TIGR01016 76 LLGKELVTNQTDPLGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 165 KKEQAVRLAQKMGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVEDASGVVMCMDAKINFDSNSAYRQKKIFDMQDW 244
Cdd:TIGR01016 156 LPYQAREIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 245 TQEDERDRQAAKADLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAIL 324
Cdd:TIGR01016 236 SQEDPREVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVF 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3821927 325 VNIFGGIMRCDVIAQGIVVAVKDLDLKIPVVVRLQGTRVDDAKALITASGLKILACDDLDEAAKMVVKLSE 395
Cdd:TIGR01016 316 INIFGGITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAESGLNIIFATSMEEAAEKAVEAAE 386
|
|
| PRK14046 |
PRK14046 |
malate--CoA ligase subunit beta; Provisional |
3-391 |
3.89e-138 |
|
malate--CoA ligase subunit beta; Provisional
Pssm-ID: 237594 [Multi-domain] Cd Length: 392 Bit Score: 400.24 E-value: 3.89e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 3 LSLHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLAGGRGKGtfegglkGGVKIVFSPEEAKAVS 82
Cdd:PRK14046 1 MDIHEYQAKELLASFGVAVPRGALAYSPEQAVYRARELGGWHWVVKAQIHSGARGKA-------GGIKLCRTYNEVRDAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 83 SRMIGKKLFTKQTGEKGRICNQVFVCERRYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPDAIIKEPIDIVE 162
Cdd:PRK14046 74 EDLLGKKLVTHQTGPEGKPVQRVYVETADPIERELYLGFVLDRKSERVRVIASARGGMEIEEIAAKEPEAIIQVVVEPAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 163 GIKKEQAVRLAQKMGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVEDASGVVMCMDAKINFDSNSAYRQKKIFDMQ 242
Cdd:PRK14046 154 GLQQFQAREIAFGLGLDIKQVSRAVKTIMGCYRAFRDLDATMLEINPLVVTKDDRVLALDAKMSFDDNALFRRPNIAEMR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 243 DWTQEDERDRQAAKADLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLA 322
Cdd:PRK14046 234 DPSQEDPREAQAAEHGLSYVGLDGDIGCIVNGAGLAMATMDMIKLAGGEPANFLDVGGGASPERVAKAFRLVLSDRNVKA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3821927 323 ILVNIFGGIMRCDVIAQGIVVAVKDLDLKIPVVVRLQGTRVDDAKALITASGLKILACDDLDEAAKMVV 391
Cdd:PRK14046 314 ILVNIFAGINRCDWVAEGVVQAAREVGIDVPLVVRLAGTNVEEGRKILAESGLPIITADTLAEAAEKAV 382
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
4-212 |
3.74e-91 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 273.37 E-value: 3.74e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 4 SLHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLAGGRGKGtfegglkGGVKIVFSPEEAKAVSS 83
Cdd:pfam08442 1 NLHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRGKA-------GGVKLAKSPEEAKEVAK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 84 RMIGKKLFTKQTGEKGRICNQVFVCERRYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPDAIIKEPIDIVEG 163
Cdd:pfam08442 74 EMLGKNLVTKQTGPDGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPVIIASTEGGVDIEEVAAKNPEKIHKFPIDPLKG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 3821927 164 IKKEQAVRLAQKMGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVE 212
Cdd:pfam08442 154 LTPYQAREIAFKLGLPGELIKQAADIIKKLYKLFVEYDATLVEINPLVE 202
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
271-391 |
6.09e-35 |
|
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, malate CoA ligase and ATP-citrate lyase. Some members of the family utilize ATP others use GTP.
Pssm-ID: 395434 [Multi-domain] Cd Length: 128 Bit Score: 125.45 E-value: 6.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 271 LVNGAGLAMATMDIIKLHGGTPANFLDVGGGA-TVHQVTEAFKLITSDKKVLAILVNIFGGIMRCDVIAQGIVVAVKDL- 348
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAfTPTTRIDALKLEAADPEVKVILLDIVLGYGACEDPAGGLLKAIKEAr 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 3821927 349 DLKIPVVVRLQGTRVD-----DAKALITASGLKILACDDLDEAAKMVV 391
Cdd:pfam00549 81 ARELPVVARVCGTEADpqgrsGQAKALAESGVLIASSNNQALRAAGAV 128
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
13-117 |
1.01e-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: 46.79 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 13 LLQEAGISVPHGVVARTPDEAYKIAKEIGSkDLVIKAQVLAGGRgkgtfegglkgGVKIVFSPEEAKAVSSRMIGKKlft 92
Cdd:COG0439 61 ALAAAGVPVPGFALVDSPEEALAFAEEIGY-PVVVKPADGAGSR-----------GVRVVRDEEELEAALAEARAEA--- 125
|
90 100
....*....|....*....|....*
gi 3821927 93 kqtgeKGRICNQVFVCERRYPRREY 117
Cdd:COG0439 126 -----KAGSPNGEVLVEEFLEGREY 145
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
1-80 |
5.53e-05 |
|
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: 44.00 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 1 RRLSLHEYLSMGLLQEAGISVPHGVVARTPDEAYKIAKEIG--------SKDLVIKAQVlaggrgkgtfegglkGGVKI- 71
Cdd:pfam13549 6 GRTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGypvvlkivSPDILHKSDV---------------GGVRLn 70
|
....*....
gi 3821927 72 VFSPEEAKA 80
Cdd:pfam13549 71 LRSAEAVRA 79
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
13-61 |
3.84e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 42.84 E-value: 3.84e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 3821927 13 LLQEAGISVPHGVVARTPDEAYKIAKEIGSKdLVIKAQvlAGGRGKGTF 61
Cdd:PRK14016 221 LLAAAGVPVPEGRVVTSAEDAWEAAEEIGYP-VVVKPL--DGNHGRGVT 266
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
13-77 |
4.48e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 42.78 E-value: 4.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3821927 13 LLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLaGGRgkgtfegglkgGVKIVFSPEE 77
Cdd:PRK05294 676 LLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVL-GGR-----------AMEIVYDEEE 728
|
|
| PLN02235 |
PLN02235 |
ATP citrate (pro-S)-lyase |
2-237 |
1.20e-03 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 177879 [Multi-domain] Cd Length: 423 Bit Score: 40.91 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 2 RLSLHEYLSMGLLQE-----AGISVPHGV--VARTPDEAYKIAKE--IGSKDLVIKAQVLAGGRGKgtfeGGLKgGVKIV 72
Cdd:PLN02235 3 RKKIREYDSKRLLKEhlkrlAGIDLPIRSaqVTESTDFNELANKEpwLSSTKLVVKPDMLFGKRGK----SGLV-ALNLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 73 FSpEEAKAVSSRMiGKKLftKQTGEKGRIcnQVFVCERRYP-RREYYFAITMER-----SFqgpvligSSQGGVNIEdva 146
Cdd:PLN02235 78 LA-QVATFVKERL-GKEV--EMGGCKGPI--TTFIVEPFVPhDQEFYLSIVSDRlgcsiSF-------SECGGIEIE--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 147 aENPDAIIKEPIDIVEGIKKEQAVRLAQkmGFPSNLVDEAAENMIKLYNLFLKYDATMIEINPMVEdASGVVMCMDAKIN 226
Cdd:PLN02235 142 -ENWDKVKTIFLPTEAPLTSEICAPLIA--TLPLEIRGKIEEFIKGVFAVFQDLDFTFLEMNPFTL-VDGEPYPLDMRGE 217
|
250
....*....|.
gi 3821927 227 FDSNSAYRQKK 237
Cdd:PLN02235 218 LDDTAAFKNFK 228
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
13-91 |
1.77e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 40.35 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 13 LLQEAGISV----PHGVvaRTPDEAYKIAKEIGSKdLVIKAQvlAGGrgkgtfeGGLkgGVKIVFSPEE-AKAV-SSRMI 86
Cdd:PRK08654 122 LMKKAGVPVlpgtEEGI--EDIEEAKEIAEEIGYP-VIIKAS--AGG-------GGI--GMRVVYSEEElEDAIeSTQSI 187
|
....*
gi 3821927 87 GKKLF 91
Cdd:PRK08654 188 AQSAF 192
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
13-91 |
2.01e-03 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 40.00 E-value: 2.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3821927 13 LLQEAGISVPHGVVARTPDEAYKIAKEIGsKDLVIKAQVLAGGRGkgtfegglkggVKIVFSPEEAKAVSSRMIGKKLF 91
Cdd:COG0151 109 FMARYGIPTAAYRVFTDLEEALAYLEEQG-APIVVKADGLAAGKG-----------VVVAETLEEALAAVDDMLADGKF 175
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
13-41 |
2.19e-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: 40.25 E-value: 2.19e-03
10 20
....*....|....*....|....*....
gi 3821927 13 LLQEAGISVPHGVVARTPDEAYKIAKEIG 41
Cdd:COG0458 121 LLDKLGIPQPKSGTATSVEEALAIAEEIG 149
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
13-110 |
9.32e-03 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 37.26 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3821927 13 LLQEAGISVPHGVVARTPDEAYKIAKEIGSKDLVIKAQVLAGGRgkgtfegglkgGVKIVFSPEEAKAVSSRMIGKKLFt 92
Cdd:pfam01071 9 FMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGK-----------GVIVASSNEEAIKAVDEILEQKKF- 76
|
90
....*....|....*...
gi 3821927 93 kqtGEKGricNQVFVCER 110
Cdd:pfam01071 77 ---GEAG---ETVVIEEF 88
|
|
|