|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
7-463 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 806.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 7 KKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSKDSYLVADKIIDVAKQAGVDCIHPGY 86
Cdd:COG4770 3 KKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 87 GFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAAFG 166
Cdd:COG4770 83 GFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 167 GGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIEEA 246
Cdd:COG4770 163 GGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 247 PAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGD-EFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESLP 325
Cdd:COG4770 243 PSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADgNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 326 LSQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDALFTPnESEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREAALG 405
Cdd:COG4770 323 FTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPP-GGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1675085468 406 RLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIEDQGERLVAKNEQQSVIA 463
Cdd:COG4770 402 RMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEELAL 459
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
6-458 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 642.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 6 LKKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSKDSYLVADKIIDVAKQAGVDCIHPG 85
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 86 YGFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAAF 165
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 166 GGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIEE 245
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 246 APAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGD-EFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESL 324
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNgEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 325 PLSQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDALFTPnESEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREAAL 404
Cdd:PRK08591 322 SIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPP-GGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1675085468 405 GRLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIEdqgERLVAKNEQ 458
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLE---KKLALQEEK 451
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
6-446 |
0e+00 |
|
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: 549.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 6 LKKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSKDSYLVADKIIDVAKQAGVDCIHPG 85
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 86 YGFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAAF 165
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 166 GGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIEE 245
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 246 APAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLL-CGDEFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESL 324
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLdKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 325 PLSQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDALFTPNeSEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREAAL 404
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPG-GPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1675085468 405 GRLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIE 446
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLE 442
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
120-325 |
4.99e-86 |
|
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: 268.02 E-value: 4.99e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 120 KTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAAFGGGGKGMRVVEHAKDFISALEGAKREAKAGFGND 199
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 200 LVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIEEAPAPGLSDALRKEMGEAAVRCAQAINYRGAGTVE 279
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1675085468 280 FLL--CGDEFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESLP 325
Cdd:pfam02786 162 FALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
339-446 |
9.00e-50 |
|
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: 168.36 E-value: 9.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 339 EARIYAEDPSNDFIPCSGHIDALFTPnESEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREAALGRLSKALEQFHLAG 418
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFP-GGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 1675085468 419 FSCNVNFLHNLAKHPTFQAGAPDTHFIE 446
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
584-649 |
4.97e-23 |
|
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: 92.86 E-value: 4.97e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1675085468 584 LAAPLNGTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIV 649
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
536-650 |
5.07e-16 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 81.43 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 536 NLVVNGEKV------VAHINQTNSHITVMYKAQQTVLELIDKHYISE--HESDALPLAAPLNGTVVKHLVEVGSTVAKGD 607
Cdd:PRK09282 469 KVEVDGEKYevkiegVKAEGKRPFYLRVDGMPEEVVVEPLKEIVVGGrpRASAPGAVTSPMPGTVVKVKVKEGDKVKAGD 548
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1675085468 608 AVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIVE 650
Cdd:PRK09282 549 TVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
579-649 |
5.23e-16 |
|
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: 82.05 E-value: 5.23e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1675085468 579 SDALPLAAPLNGTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIV 649
Cdd:COG1038 1074 GNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
592-649 |
2.99e-12 |
|
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: 62.23 E-value: 2.99e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1675085468 592 VVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIV 649
Cdd:pfam00364 16 VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
590-651 |
1.10e-07 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 54.35 E-value: 1.10e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1675085468 590 GTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIVEE 651
Cdd:TIGR01347 15 GTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEE 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
7-463 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 806.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 7 KKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSKDSYLVADKIIDVAKQAGVDCIHPGY 86
Cdd:COG4770 3 KKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 87 GFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAAFG 166
Cdd:COG4770 83 GFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 167 GGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIEEA 246
Cdd:COG4770 163 GGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 247 PAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGD-EFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESLP 325
Cdd:COG4770 243 PSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADgNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 326 LSQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDALFTPnESEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREAALG 405
Cdd:COG4770 323 FTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPP-GGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1675085468 406 RLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIEDQGERLVAKNEQQSVIA 463
Cdd:COG4770 402 RMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEELAL 459
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
6-458 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 642.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 6 LKKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSKDSYLVADKIIDVAKQAGVDCIHPG 85
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 86 YGFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAAF 165
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 166 GGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIEE 245
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 246 APAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGD-EFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESL 324
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNgEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 325 PLSQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDALFTPnESEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREAAL 404
Cdd:PRK08591 322 SIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPP-GGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1675085468 405 GRLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIEdqgERLVAKNEQ 458
Cdd:PRK08591 401 ARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLE---KKLALQEEK 451
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
7-455 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 619.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 7 KKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSKDSYLVADKIIDVAKQAGVDCIHPGY 86
Cdd:PRK06111 3 QKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 87 GFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAAFG 166
Cdd:PRK06111 83 GLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 167 GGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIEEA 246
Cdd:PRK06111 163 GGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 247 PAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGDE-FFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESLP 325
Cdd:PRK06111 243 PSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 326 LSQADIQLQGHSFEARIYAEDPsNDFIPCSGHIDALFTPnESEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREAALG 405
Cdd:PRK06111 323 FTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLP-GGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAIS 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1675085468 406 RLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIEDQGERLVAK 455
Cdd:PRK06111 401 RLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQLVKKSTK 450
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
6-469 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 618.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 6 LKKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSKDSYLVADKIIDVAKQAGVDCIHPG 85
Cdd:PRK08654 2 FKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 86 YGFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAAF 165
Cdd:PRK08654 82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 166 GGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIEE 245
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 246 APAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGDEFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESLP 325
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 326 LSQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDALFTPNeSEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREAALG 405
Cdd:PRK08654 322 FKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPG-GPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 406 RLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIEDQ---------------------GERLVAKNEQQSVIAT 464
Cdd:PRK08654 401 RMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEEttileemkryaleeeerektlSEKFFPGNKKVAAIAA 480
|
....*
gi 1675085468 465 VVAAY 469
Cdd:PRK08654 481 AVNAY 485
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
3-447 |
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: 588.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 3 TKSLKKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSK-DSYLVADKIIDVAKQAGVDC 81
Cdd:COG1038 1 MKKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPvDAYLDIEEIIRVAKEKGVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 82 IHPGYGFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLI 161
Cdd:COG1038 81 IHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 162 KAAFGGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQK 241
Cdd:COG1038 161 KAAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 242 VIEEAPAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLC-GDEFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAA 320
Cdd:COG1038 241 VVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDdDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 321 GESL-------PlSQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDALFTPneSEF-VRIDTGIA-AGDEISPFYDPMIA 391
Cdd:COG1038 321 GYSLddpeigiP-SQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSA--GGFgIRLDGGNAyTGAVITPYYDSLLV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1675085468 392 KLIVHDDNREAALGRLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIED 447
Cdd:COG1038 398 KVTAWGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDE 453
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
2-455 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 586.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 2 TTKSLKKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSK-DSYLVADKIIDVAKQAGVD 80
Cdd:PRK12999 1 EMKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPvRAYLDIDEIIRVAKQAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 81 CIHPGYGFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVL 160
Cdd:PRK12999 81 AIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 161 IKAAFGGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQ 240
Cdd:PRK12999 161 LKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 241 KVIEEAPAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGD-EFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIA 319
Cdd:PRK12999 241 KVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADgNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 320 AGESL------PLSQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDALFTPneSEF-VRIDTGIA-AGDEISPFYDPMIA 391
Cdd:PRK12999 321 EGATLhdleigIPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSP--GGFgVRLDGGNAfAGAEITPYYDSLLV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1675085468 392 KLIVHDDNREAALGRLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIEDQGERLVAK 455
Cdd:PRK12999 399 KLTAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFP 462
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
6-448 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 565.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 6 LKKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSKDSYLVADKIIDVAKQAGVDCIHPG 85
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 86 YGFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAAF 165
Cdd:PRK05586 82 FGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 166 GGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIEE 245
Cdd:PRK05586 162 GGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 246 APAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGD-EFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESL 324
Cdd:PRK05586 242 APSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDgNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 325 PLSQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDALFTPNESEfVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREAAL 404
Cdd:PRK05586 322 SIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLG-VRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1675085468 405 GRLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIEDQ 448
Cdd:PRK05586 401 QKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKK 444
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
6-446 |
0e+00 |
|
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: 549.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 6 LKKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSKDSYLVADKIIDVAKQAGVDCIHPG 85
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 86 YGFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAAF 165
Cdd:TIGR00514 82 YGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 166 GGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIEE 245
Cdd:TIGR00514 162 GGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 246 APAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLL-CGDEFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESL 324
Cdd:TIGR00514 242 APSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLdKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 325 PLSQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDALFTPNeSEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREAAL 404
Cdd:TIGR00514 322 SLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPG-GPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1675085468 405 GRLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIE 446
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLE 442
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
6-474 |
1.27e-177 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 513.11 E-value: 1.27e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 6 LKKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSkDSYLVADKIIDVAKQAGVDCIHPG 85
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGADPL-AGYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 86 YGFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAAF 165
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 166 GGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIEE 245
Cdd:PRK07178 161 GGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 246 APAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGD-EFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESL 324
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADgEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 325 PLSQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDALFTPNeSEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREAAL 404
Cdd:PRK07178 321 SYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPG-GPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEAL 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1675085468 405 GRLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIEDQGERLVAKNEQQ-SVIATVVAAYTYAHQ 474
Cdd:PRK07178 400 DRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTNYSIKRKpEELAAAIAAAIAAHA 470
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
3-446 |
1.10e-174 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 505.44 E-value: 1.10e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 3 TKSLKKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSKDSYLVADKIIDVAKQAGVDCI 82
Cdd:PRK12833 2 PSRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 83 HPGYGFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIK 162
Cdd:PRK12833 82 HPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 163 AAFGGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHgNCVYLGDRDCSLQRRHQKV 242
Cdd:PRK12833 162 AAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 243 IEEAPAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLL--CGDEFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAA 320
Cdd:PRK12833 241 LEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFddARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 321 GESLPLSQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDALFTPnESEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNR 400
Cdd:PRK12833 321 GEPLRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWP-QGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDR 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1675085468 401 EAALGRLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIE 446
Cdd:PRK12833 400 AAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
4-446 |
1.79e-165 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 481.17 E-value: 1.79e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 4 KSLKKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSKDSYLVADKIIDVAKQAGVDCIH 83
Cdd:PRK08462 2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 84 PGYGFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKA 163
Cdd:PRK08462 82 PGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 164 AFGGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVI 243
Cdd:PRK08462 162 AAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 244 EEAPAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLL-CGDEFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGE 322
Cdd:PRK08462 242 EESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLdSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 323 SLPlSQADIQLQGHSFEARIYAEDPsNDFIPCSGHIDALFTPNESEfVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREA 402
Cdd:PRK08462 322 ELP-SQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRN-VRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1675085468 403 ALGRLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIE 446
Cdd:PRK08462 399 AIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLE 442
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
6-468 |
2.48e-161 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 471.99 E-value: 2.48e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 6 LKKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSKdSYLVADKIIDVAKQAGVDCIHPG 85
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPIK-GYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 86 YGFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDT-DFLQAEAEKIGYPVLIKAA 164
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSESmEEIKIFARKIGYPVILKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 165 FGGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIE 244
Cdd:PRK08463 161 GGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 245 EAPAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLcgDE---FFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAG 321
Cdd:PRK08463 241 IAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLL--DDynrFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 322 ESLPLSQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDALFtPNESEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNRE 401
Cdd:PRK08463 319 EILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYY-PALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYD 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1675085468 402 AALGRLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIEDQGERLVAKNE------QQSVIATVVAA 468
Cdd:PRK08463 398 LAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKTEdrhqenKEEVIAAIAAA 470
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
8-450 |
8.09e-160 |
|
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: 489.34 E-value: 8.09e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 8 KILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSK---DSYLVADKIIDVAKQAGVDCIHP 84
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGPDLgpiEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 85 GYGFLSENCDFALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAA 164
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 165 FGGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIE 244
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 245 EAPAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGD-EFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGES 323
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDgKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 324 LPL------SQADIQLQGHSFEARIYAEDPSNDFIPCSGHIDAlFTPNESEFVRIDTGIA-AGDEISPFYDPMIAKLIVH 396
Cdd:TIGR01235 321 LPTpqlgvpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEA-YRSAGGFGIRLDGGNSyAGAIITPYYDSLLVKVSAW 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1675085468 397 DDNREAALGRLSKALEQFHLAGFSCNVNFLHNLAKHPTFQAGAPDTHFIEDQGE 450
Cdd:TIGR01235 400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPE 453
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
120-325 |
4.99e-86 |
|
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: 268.02 E-value: 4.99e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 120 KTRAKEIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAAFGGGGKGMRVVEHAKDFISALEGAKREAKAGFGND 199
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 200 LVLLERYVTKPRHVEVQVFADSHGNCVYLGDRDCSLQRRHQKVIEEAPAPGLSDALRKEMGEAAVRCAQAINYRGAGTVE 279
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1675085468 280 FLL--CGDEFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESLP 325
Cdd:pfam02786 162 FALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
6-113 |
8.51e-60 |
|
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: 195.40 E-value: 8.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 6 LKKILVANRGEIACRVMRTAKQMGLTTVAVYSDADKHAQHVKHADEAYHIGPAPSKDSYLVADKIIDVAKQAGVDCIHPG 85
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 1675085468 86 YGFLSENCDFALACEKNDIAFIGPPASS 113
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
66-322 |
3.37e-56 |
|
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: 191.62 E-value: 3.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 66 VADKIIDVAKQAGVDCIhpgygfLSENCD----FALACEKNDIAfiGPPASSIEAMGSKTRAKEIMHQANVPlVPGYYGD 141
Cdd:COG0439 5 IIAAAAELARETGIDAV------LSESEFavetAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVP-VPGFALV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 142 NQDTDFLQAeAEKIGYPVLIKAAFGGGGKGMRVVEHAKDFISALEGAKREAKAGFGNDLVLLERYVTKpRHVEVQVFADs 221
Cdd:COG0439 76 DSPEEALAF-AEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVR- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 222 HGNCVYlgdrdCSLQRRHQK---VIE---EAPAPgLSDALRKEMGEAAVRCAQAINY-RGAGTVEFLLCGD-EFFFMEMN 293
Cdd:COG0439 153 DGEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLTPDgEPYLIEIN 226
|
250 260 270
....*....|....*....|....*....|.
gi 1675085468 294 TRLQVEH--PVTEMVTGVDLVNWQINIAAGE 322
Cdd:COG0439 227 ARLGGEHipPLTELATGVDLVREQIRLALGE 257
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
339-446 |
9.00e-50 |
|
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: 168.36 E-value: 9.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 339 EARIYAEDPSNDFIPCSGHIDALFTPnESEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREAALGRLSKALEQFHLAG 418
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFP-GGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 1675085468 419 FSCNVNFLHNLAKHPTFQAGAPDTHFIE 446
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
339-447 |
6.83e-46 |
|
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: 158.04 E-value: 6.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 339 EARIYAEDPSNDFIPCSGHIDALFTPnESEFVRIDTGIAAGDEISPFYDPMIAKLIVHDDNREAALGRLSKALEQFHLAG 418
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 1675085468 419 FSCNVNFLHNLAKHPTFQAGAPDTHFIED 447
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
584-649 |
4.97e-23 |
|
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: 92.86 E-value: 4.97e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1675085468 584 LAAPLNGTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIV 649
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
536-650 |
5.07e-16 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 81.43 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 536 NLVVNGEKV------VAHINQTNSHITVMYKAQQTVLELIDKHYISE--HESDALPLAAPLNGTVVKHLVEVGSTVAKGD 607
Cdd:PRK09282 469 KVEVDGEKYevkiegVKAEGKRPFYLRVDGMPEEVVVEPLKEIVVGGrpRASAPGAVTSPMPGTVVKVKVKEGDKVKAGD 548
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1675085468 608 AVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIVE 650
Cdd:PRK09282 549 TVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
579-649 |
5.23e-16 |
|
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: 82.05 E-value: 5.23e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1675085468 579 SDALPLAAPLNGTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIV 649
Cdd:COG1038 1074 GNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
575-650 |
1.91e-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: 73.39 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 575 SEHESDALPLAAPLNGTV-------VKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLA 647
Cdd:COG0511 54 AAAASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLF 133
|
...
gi 1675085468 648 IVE 650
Cdd:COG0511 134 VIE 136
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
579-651 |
2.86e-15 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 79.80 E-value: 2.86e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1675085468 579 SDALPLAAPLNGTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIVEE 651
Cdd:PRK12999 1074 GNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
27-325 |
3.63e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 74.58 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 27 QMGLTTVAVYSDADKHAQHVKHADEaYHIGPAPSKDSYLVADKIIDVAKQAGVDCIHPGygflSENCDFALACEKNDIA- 105
Cdd:COG3919 26 EAGVRVIVVDRDPLGPAARSRYVDE-VVVVPDPGDDPEAFVDALLELAERHGPDVLIPT----GDEYVELLSRHRDELEe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 106 ---FIGPPASSIEAMGSKTRAKEIMHQANVPlVPGYYGDNQDTDfLQAEAEKIGYPVLIKAA----FGGGGKGMRV-VEH 177
Cdd:COG3919 101 hyrLPYPDADLLDRLLDKERFYELAEELGVP-VPKTVVLDSADD-LDALAEDLGFPVVVKPAdsvgYDELSFPGKKkVFY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 178 AKDFISALEGAKREAKAGFGndlVLLERYVTKPRHVEVQVFA--DSHGNCVYLGDrdcslqrrHQKVIEEAPAPGLSDAL 255
Cdd:COG3919 179 VDDREELLALLRRIAAAGYE---LIVQEYIPGDDGEMRGLTAyvDRDGEVVATFT--------GRKLRHYPPAGGNSAAR 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1675085468 256 R----KEMGEAAVRCAQAINYRGAGTVEFLLC--GDEFFFMEMNTRLQVEHPvteMVT--GVDLVNWQINIAAGESLP 325
Cdd:COG3919 248 EsvddPELEEAARRLLEALGYHGFANVEFKRDprDGEYKLIEINPRFWRSLY---LATaaGVNFPYLLYDDAVGRPLE 322
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
579-646 |
1.34e-13 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 73.81 E-value: 1.34e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1675085468 579 SDALPLAAPLNGTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDML 646
Cdd:PRK14040 522 AAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTL 589
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
96-324 |
3.45e-13 |
|
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: 72.60 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 96 ALACEKNDIA----FIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTdfLQAEAEKIGYPVLIKAAFGGGGKG 171
Cdd:COG0458 87 AVELEEAGILegvkILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEE--ALAIAEEIGYPVIVRPSYVLGGRG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 172 MRVVEHAKDFISALEGAKREAkagfGNDLVLLERYVTKPRHVEVQVFADSHGNCVYLgdrdCSLQrrHqkvIEEA----- 246
Cdd:COG0458 165 MGIVYNEEELEEYLERALKVS----PDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgvhsg 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 247 ------PAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGDEFFFMEMNTRlqvehpVTEMV------TGVDLVNW 314
Cdd:COG0458 232 dsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPR------ASRSSpfaskaTGYPIAKI 305
|
250
....*....|
gi 1675085468 315 QINIAAGESL 324
Cdd:COG0458 306 AAKLALGYTL 315
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
67-294 |
3.96e-13 |
|
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: 70.52 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 67 ADKIIDVAKQAGVDCIHPG-YGFLSENCDFALACEKNDIAFIGPP--ASSIeAMgSKTRAKEIMHQANVPLVPGYYGDNQ 143
Cdd:COG1181 42 VEDLPAALKELKPDVVFPAlHGRGGEDGTIQGLLELLGIPYTGSGvlASAL-AM-DKALTKRVLAAAGLPTPPYVVLRRG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 144 DTDFLQAEAEKIGYPVLIKAAFGGGGKGMRVVEHAKDFISALEGAKREakagfgNDLVLLERYVtKPRHVEVQVfadshg 223
Cdd:COG1181 120 ELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DDKVLVEEFI-DGREVTVGV------ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 224 ncvyLGDRD---------------CSLQRRHQ--KVIEEAPAPgLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGD- 285
Cdd:COG1181 187 ----LGNGGpralppieivpengfYDYEAKYTdgGTEYICPAR-LPEELEERIQELALKAFRALGCRGYARVDFRLDEDg 261
|
....*....
gi 1675085468 286 EFFFMEMNT 294
Cdd:COG1181 262 EPYLLEVNT 270
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
96-324 |
1.53e-12 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 71.15 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 96 ALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFlqAEAEKIGYPVLIKAAFGGGGKGMRVV 175
Cdd:PRK12815 647 AKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAF--AFAKRIGYPVLIRPSYVIGGQGMAVV 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 176 EHAKDFISALEGAKReakagfGNDLVLLERYVTKprhVEVQVFADSHGNCVYLGDrdcslQRRHqkvIEEA--------- 246
Cdd:PRK12815 725 YDEPALEAYLAENAS------QLYPILIDQFIDG---KEYEVDAISDGEDVTIPG-----IIEH---IEQAgvhsgdsia 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 247 --PAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGDEFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESL 324
Cdd:PRK12815 788 vlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSL 867
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
592-649 |
2.99e-12 |
|
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: 62.23 E-value: 2.99e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1675085468 592 VVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIV 649
Cdd:pfam00364 16 VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
108-294 |
1.10e-11 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 66.29 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 108 GPPASSIeAMgSKTRAKEIMHQANVPlVPGYYGDNQDtDFLQAEAEKIGYPVLIKAAFGGGGKGMRVVEHAKDFISALEG 187
Cdd:PRK01372 89 GVLASAL-AM-DKLRTKLVWQAAGLP-TPPWIVLTRE-EDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALEL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 188 AkreakAGFGnDLVLLERYVTKPrhvEVQVfadshgnCVyLGDRD---CSLQRRHQ------KVIEEA-----PApGLSD 253
Cdd:PRK01372 165 A-----FKYD-DEVLVEKYIKGR---ELTV-------AV-LGGKAlpvIEIVPAGEfydyeaKYLAGGtqyicPA-GLPA 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1675085468 254 ALRKEMGEAAVRCAQAINYRGAGTVEFLLCGD-EFFFMEMNT 294
Cdd:PRK01372 227 EIEAELQELALKAYRALGCRGWGRVDFMLDEDgKPYLLEVNT 268
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
586-650 |
1.19e-10 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 57.49 E-value: 1.19e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1675085468 586 APLNGTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIVE 650
Cdd:PRK08225 6 ASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
96-324 |
5.42e-10 |
|
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: 62.71 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 96 ALACEKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGyyGDNQDTDFLQAEAEKIGYPVLIKAAFGGGGKGMRVV 175
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 176 EHAKDfisaLEGAKREAKAGFGNDLVLLERYVTKPrhVEVQVFADSHGNCVYL--------------GDRDCSLqrrhqk 241
Cdd:TIGR01369 724 YNEEE----LRRYLEEAVAVSPEHPVLIDKYLEDA--VEVDVDAVSDGEEVLIpgimehieeagvhsGDSTCVL------ 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 242 vieeaPAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGDEFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAG 321
Cdd:TIGR01369 792 -----PPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLG 866
|
...
gi 1675085468 322 ESL 324
Cdd:TIGR01369 867 KKL 869
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
586-646 |
1.52e-09 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 57.18 E-value: 1.52e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1675085468 586 APLNGTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDML 646
Cdd:PRK05641 89 APMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPL 149
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
100-296 |
2.51e-09 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 60.78 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 100 EKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDflQAEAEKIGYPVLIKAAFGGGGKGMRVVEHAK 179
Cdd:TIGR01369 108 EKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEA--LAAAKEIGYPVIVRPAFTLGGTGGGIAYNRE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 180 DFISALEGAKREAKAGFgndlVLLERYVTKPRHVEVQVFADSHGNC-------------VYLGDRdcslqrrhqkvIEEA 246
Cdd:TIGR01369 186 ELKEIAERALSASPINQ----VLVEKSLAGWKEIEYEVMRDSNDNCitvcnmenfdpmgVHTGDS-----------IVVA 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1675085468 247 PAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGD--EFFFMEMNTRL 296
Cdd:TIGR01369 251 PSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDsgRYYVIEVNPRV 302
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
107-323 |
4.37e-09 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 59.86 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 107 IGPPASSIEAMG---SKTRAKEIMHQANVPlVPGYYGDNQDTDFLQAeAEKIGYPVLIKAAFGGGGKGMRVVEHAKDFIS 183
Cdd:PRK02186 92 LGLPAANTEAIRtcrDKKRLARTLRDHGID-VPRTHALALRAVALDA-LDGLTYPVVVKPRMGSGSVGVRLCASVAEAAA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 184 ALEGAKREakagfGNDLVLLERYVTKPRHvEVQVFADSHGNCV------YLGDRDCSLQRRHqkvieEAPAPgLSDALRK 257
Cdd:PRK02186 170 HCAALRRA-----GTRAALVQAYVEGDEY-SVETLTVARGHQVlgitrkHLGPPPHFVEIGH-----DFPAP-LSAPQRE 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1675085468 258 EMGEAAVRCAQAINYR-GAGTVEFLLCGDEFFFMEMNTRLQVEH-PVT-EMVTGVDLVNWQINIAAGES 323
Cdd:PRK02186 238 RIVRTVLRALDAVGYAfGPAHTELRVRGDTVVIIEINPRLAGGMiPVLlEEAFGVDLLDHVIDLHLGVA 306
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
578-646 |
7.14e-09 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 54.43 E-value: 7.14e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1675085468 578 ESDALPlaAPLNGTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDML 646
Cdd:PRK06549 60 GADAMP--SPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGL 126
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
590-649 |
8.84e-09 |
|
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: 52.38 E-value: 8.84e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1675085468 590 GTVVKHLVEVGSTVAKGDAVVIIEAMK--MEytLNAPHDGVLTSYCFAEGELVSHGDMLAIV 649
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKatME--VPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
590-629 |
1.05e-08 |
|
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: 52.06 E-value: 1.05e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1675085468 590 GTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVL 629
Cdd:cd06663 14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTV 53
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
590-649 |
1.06e-08 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 52.02 E-value: 1.06e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 590 GTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIV 649
Cdd:cd06849 15 GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
100-296 |
4.72e-08 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 56.52 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 100 EKNDIAFIGPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTdfLQAEAEKIGYPVLIKAAFGGGGKGMRVVEHAK 179
Cdd:PRK12815 109 EQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEE--ALAFAEKIGFPIIVRPAYTLGGTGGGIAENLE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 180 DFISALEGAKREAKagFGNdlVLLERYVTKPRHVEVQVFADSHGNCVYL-------------GDRdcslqrrhqkvIEEA 246
Cdd:PRK12815 187 ELEQLFKQGLQASP--IHQ--CLLEESIAGWKEIEYEVMRDRNGNCITVcnmenidpvgihtGDS-----------IVVA 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1675085468 247 PAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLL--CGDEFFFMEMNTRL 296
Cdd:PRK12815 252 PSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALdpKSKQYYLIEVNPRV 303
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
590-651 |
1.10e-07 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 54.35 E-value: 1.10e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1675085468 590 GTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIVEE 651
Cdd:TIGR01347 15 GTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEE 76
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
49-322 |
2.43e-07 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 52.96 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 49 ADEAYhIGPAPSKDSYLvaDKIIDVAKQAGVDCIHPGY----GFLSENCDfalACEKNDIAFIGPPASSIEAMGSKTRAK 124
Cdd:PRK12767 43 ADKFY-VVPKVTDPNYI--DRLLDICKKEKIDLLIPLIdpelPLLAQNRD---RFEEIGVKVLVSSKEVIEICNDKWLTY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 125 EIMHQANVPLVPGYYGDNQDTDFLQAEAEKIGYPVLIKAAFGGGGKGMRVVEHAKDFISALEGAKreakagfgnDLVLLE 204
Cdd:PRK12767 117 EFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVP---------NLIIQE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 205 rYVtkpRHVE--VQVFADSHGNCVylgdrdCSLQRRHQKVIEEAPAPGLSDAlRKEMGEAAVRCAQAINYRGAGTVEFLL 282
Cdd:PRK12767 188 -FI---EGQEytVDVLCDLNGEVI------SIVPRKRIEVRAGETSKGVTVK-DPELFKLAERLAEALGARGPLNIQCFV 256
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1675085468 283 CGDEFFFMEMNTRLQVEHPVTEMVtGVDLVNWQINIAAGE 322
Cdd:PRK12767 257 TDGEPYLFEINPRFGGGYPLSYMA-GANEPDWIIRNLLGG 295
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
103-294 |
1.66e-06 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 50.50 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 103 DIAFIGPP--ASSIeAMgSKTRAKEIMHQANVPLVPGYY--GDNQDTDFLQAEAEKIGYPVLIKAAfggggkgmR----- 173
Cdd:PRK01966 107 GIPYVGCGvlASAL-SM-DKILTKRLLAAAGIPVAPYVVltRGDWEEASLAEIEAKLGLPVFVKPA--------Nlgssv 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 174 ---VVEHAKDFISALEGAkreakagFGND-LVLLERYVtKPRHVEVQVFadshGNCV--------------------YLG 229
Cdd:PRK01966 177 gisKVKNEEELAAALDLA-------FEYDrKVLVEQGI-KGREIECAVL----GNDPkasvpgeivkpddfydyeakYLD 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1675085468 230 DrdcslqrrhqKVIEEAPAPgLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGD-EFFFMEMNT 294
Cdd:PRK01966 245 G----------SAELIIPAD-LSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDgEIYLNEINT 299
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
597-651 |
7.88e-06 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 44.23 E-value: 7.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1675085468 597 VEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIVEE 651
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIEE 80
|
|
| BCCP |
TIGR00531 |
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify ... |
597-650 |
7.89e-06 |
|
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify biotin carboxyl carrier protein as a peptide of acetyl-CoA carboxylase. Scoring below the trusted cutoff is a related protein encoded in a region associated with polyketide synthesis in the prokaryote Saccharopolyspora hirsuta, and a reported chloroplast-encoded biotin carboxyl carrier protein that may be highly derived from the last common ancestral sequence. Scoring below the noise cutoff are biotin carboxyl carrier domains of other enzymes such as pyruvate carboxylase.The gene name is accB or fabE. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273123 [Multi-domain] Cd Length: 155 Bit Score: 46.37 E-value: 7.89e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1675085468 597 VEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIVE 650
Cdd:TIGR00531 102 VEVGDKVNKGQTVCIVEAMKMMNEIEAEKAGTVVAILVENGQPVEYGEPLIVIE 155
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
590-650 |
1.43e-05 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 48.18 E-value: 1.43e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1675085468 590 GTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIVE 650
Cdd:PRK14042 534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
586-649 |
1.89e-05 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 42.87 E-value: 1.89e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1675085468 586 APLNGTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIV 649
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
132-294 |
2.23e-05 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 45.77 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 132 VPLVPGYYGDNQDtDFLQAEAEKIGYPVLIKAAFGGGGKGMRVVEHAKDFISALEGA-KREAKagfgndlVLLERYVtKP 210
Cdd:pfam07478 13 VTFTRADWKLNPK-EWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAfQYDEK-------VLVEEGI-EG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 211 RHVEVQVFADSHGNCVYLGDR--DCSLQRRHQKVIEEA-----PApGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLC 283
Cdd:pfam07478 84 REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPA-DLEEEQEEQIQELALKAYKALGCRGLARVDFFLT 162
|
170
....*....|..
gi 1675085468 284 GD-EFFFMEMNT 294
Cdd:pfam07478 163 EDgEIVLNEVNT 174
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
108-325 |
2.85e-05 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 47.47 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 108 GPPASSIEAMGSKTRAKEIMHQANVPLVPGYYGDNQDTDFlqAEAEKIGYPVLIKAAFGGGGKGMRVVEHAKDFISALEG 187
Cdd:PLN02735 691 GTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADAL--AIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLET 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 188 A-----KREakagfgndlVLLERYVTKPRHVEVQVFADSHGNCV-------------YLGDRDCSLqrrhqkvieeaPAP 249
Cdd:PLN02735 769 AvevdpERP---------VLVDKYLSDATEIDVDALADSEGNVViggimehieqagvHSGDSACSL-----------PTQ 828
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1675085468 250 GLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLC-GDEFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGESLP 325
Cdd:PLN02735 829 TIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITpSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVMSGKSLK 905
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
251-325 |
3.71e-05 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 46.45 E-value: 3.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1675085468 251 LSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGDEFFFMEMNTRLQVEHPVTEMVTGVDLVNWQINIAAGEsLP 325
Cdd:COG2232 218 LPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRGE-LP 291
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
590-654 |
6.98e-05 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 45.71 E-value: 6.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1675085468 590 GTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIVEEPEA 654
Cdd:PRK14875 17 GKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAEV 81
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
583-641 |
1.56e-04 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 44.06 E-value: 1.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1675085468 583 PLAAPLNGTVVK-------HLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVS 641
Cdd:PLN02983 199 PLKSPMAGTFYRspapgepPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVS 264
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
590-651 |
2.15e-04 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 44.05 E-value: 2.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1675085468 590 GTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIVEE 651
Cdd:PRK05704 17 ATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDE 78
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
589-654 |
2.87e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 44.04 E-value: 2.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1675085468 589 NGTVVKHLVEVGSTVAKGDAVVIIEAMK--MEYTlnAPHDGVLTSYCFAEGELVSHGDMLAIVEEPEA 654
Cdd:PRK11855 15 EVEVIEWLVKEGDTVEEDQPLVTVETDKatMEIP--SPAAGVVKEIKVKVGDTVSVGGLLAVIEAAGA 80
|
|
| PTZ00144 |
PTZ00144 |
dihydrolipoamide succinyltransferase; Provisional |
590-654 |
4.03e-04 |
|
dihydrolipoamide succinyltransferase; Provisional
Pssm-ID: 240289 [Multi-domain] Cd Length: 418 Bit Score: 43.13 E-value: 4.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1675085468 590 GTVVKHLVEVGSTVAKGDAVVIIEAMKMEYTLNAPHDGVLTSYCFAEGELVSHGDMLAIVEEPEA 654
Cdd:PTZ00144 59 GTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGA 123
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
590-650 |
1.02e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 42.12 E-value: 1.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1675085468 590 GTVVKHLVEVGSTVAKGDAVVIIEAMK--MEYTlnAPHDGVLTSYCFAEGELVSHGDMLAIVE 650
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKatMEIP--SPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
150-324 |
1.36e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 42.01 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 150 AEAEKIGYPVLIKAAFGGGGKGMRVVEHAKDfisaLEGAKREAKAGFGNDLVLLERYVTkpRHVEVQVFADSHGNCVYL- 228
Cdd:PRK05294 698 EVAEEIGYPVLVRPSYVLGGRAMEIVYDEEE----LERYMREAVKVSPDHPVLIDKFLE--GAIEVDVDAICDGEDVLIg 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1675085468 229 -------------GDRDCSLqrrhqkvieeaPAPGLSDALRKEMGEAAVRCAQAINYRGAGTVEFLLCGDEFFFMEMNTR 295
Cdd:PRK05294 772 gimehieeagvhsGDSACSL-----------PPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPR 840
|
170 180
....*....|....*....|....*....
gi 1675085468 296 LQVEHPVTEMVTGVDLVNWQINIAAGESL 324
Cdd:PRK05294 841 ASRTVPFVSKATGVPLAKIAARVMLGKKL 869
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
98-163 |
6.18e-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: 39.61 E-value: 6.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1675085468 98 ACEKNDIAFIGPP--ASSIEamGSKTRAKEIMHQANVPlVPGY--YgdnqdTDFLQAEA--EKIGYPVLIKA 163
Cdd:COG0151 81 AFRAAGIPVFGPSkaAAQLE--GSKAFAKEFMARYGIP-TAAYrvF-----TDLEEALAylEEQGAPIVVKA 144
|
|
| |
