|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-448 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 742.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 1 MKKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLQGERPTDTYLNIEKLLAVAARAGADAVHPG 80
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 81 YGFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAAF 160
Cdd:COG4770 82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 161 GGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIEE 240
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 241 APAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLPL 320
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 321 SFDGTPV-PRGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAIS 399
Cdd:COG4770 322 PFTQEDIkLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2414954838 400 RARRALAEFKVEGVATVLPFHRAVMDHDDFTAANtfaVHTRWIETDFAE 448
Cdd:COG4770 402 RMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGD---VDTGFIERELAE 447
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-448 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 582.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 1 MKKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLQGERPTDTYLNIEKLLAVAARAGADAVHPG 80
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 81 YGFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAAF 160
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 161 GGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIEE 240
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 241 APAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLPL 320
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 321 SFDGTPVP-RGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAIS 399
Cdd:PRK08591 322 SIKQEDIVfRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2414954838 400 RARRALAEFKVEGVATVLPFHRAVMDHDDFTAANtfaVHTRWIETDFAE 448
Cdd:PRK08591 402 RMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGD---YNIHYLEKKLAL 447
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-434 |
5.49e-172 |
|
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: 495.05 E-value: 5.49e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 1 MKKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLqGERPT-DTYLNIEKLLAVAARAGADAVHP 79
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCI-GPAPSaKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 80 GYGFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAA 159
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 160 FGGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIE 239
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 240 EAPAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLP 319
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 320 LSFDGTPVP-RGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAI 398
Cdd:TIGR00514 321 LSLKQEDVVvRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 2414954838 399 SRARRALAEFKVEGVATVLPFHRAVMDHDDFTAANT 434
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGT 436
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
114-321 |
6.91e-88 |
|
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: 270.72 E-value: 6.91e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 114 DKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAAFGGGGRGLKVAWKLDEVSELYESAVREAVTAFGR 193
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 194 GECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIEEAPAPYLTDELRQRIHESARAVCAEAGYVGAGTV 273
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2414954838 274 EFLL-SGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLPLS 321
Cdd:pfam02786 161 EFALdPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
334-443 |
1.32e-54 |
|
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: 180.30 E-value: 1.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 334 EFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAISRARRALAEFKVEGV 413
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100 110
....*....|....*....|....*....|
gi 2414954838 414 ATVLPFHRAVMDHDDFTAANtfaVHTRWIE 443
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGD---VDTGFLE 107
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
510-575 |
8.56e-19 |
|
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: 80.54 E-value: 8.56e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2414954838 510 AVLTPVAGNLHAWAVEDGATVEKGQVIAIMEAMKMETSILAPCAGTV-QISKEPGGYLEAKMVIGRV 575
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVkEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
492-556 |
3.77e-14 |
|
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: 69.54 E-value: 3.77e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2414954838 492 AAAPADASQPTAEAPDPHAVLTPVAGNLHAWA-------VEDGATVEKGQVIAIMEAMKMETSILAPCAGTV 556
Cdd:COG0511 44 AAAAPAAAAAAAAASGGGAVKSPMVGTFYRAPspgakpfVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTV 115
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
453-557 |
5.22e-13 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 71.50 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 453 APRNAEPADPGVLRtfVEIDGKRHELGL-PAALLAGM--SLNAAAPADASQPTAEAPDPHAVLTPVAGNLHAWAVEDGAT 529
Cdd:PRK14040 468 PAAKAEPAGSETYT--VEVEGKAYVVKVsEGGDISQItpAAPAAAPAAAAAAAPAAAAGEPVTAPLAGNIFKVIVTEGQT 545
|
90 100
....*....|....*....|....*...
gi 2414954838 530 VEKGQVIAIMEAMKMETSILAPCAGTVQ 557
Cdd:PRK14040 546 VAEGDVLLILEAMKMETEIRAAQAGTVR 573
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
467-569 |
1.05e-12 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 71.32 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 467 TFVEID-GKRHELGLPA---ALLAGMS-----LN-----------AAAPADASQPTAEAPDPHAVLTPVAGNLHAWAVED 526
Cdd:PRK12999 1015 IEVEIEpGKTLIIKLEAigePDEDGMRtvyfeLNgqprevqvrdrSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKE 1094
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2414954838 527 GATVEKGQVIAIMEAMKMETSILAPCAGTV-QISKEPGGYLEAK 569
Cdd:PRK12999 1095 GDEVKAGDPLAVIEAMKMETTITAPVDGTVkRVLVKAGDQVEAG 1138
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
522-575 |
6.27e-09 |
|
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: 52.60 E-value: 6.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2414954838 522 WAVEDGATVEKGQVIAIMEAMKMETSILAPCAGTVQ-ISKEPGGYLEAKMVIGRV 575
Cdd:pfam00364 19 WLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKeILVPEGDTVEVGDPLAKI 73
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-448 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 742.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 1 MKKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLQGERPTDTYLNIEKLLAVAARAGADAVHPG 80
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 81 YGFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAAF 160
Cdd:COG4770 82 YGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 161 GGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIEE 240
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 241 APAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLPL 320
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 321 SFDGTPV-PRGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAIS 399
Cdd:COG4770 322 PFTQEDIkLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2414954838 400 RARRALAEFKVEGVATVLPFHRAVMDHDDFTAANtfaVHTRWIETDFAE 448
Cdd:COG4770 402 RMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGD---VDTGFIERELAE 447
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-448 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 582.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 1 MKKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLQGERPTDTYLNIEKLLAVAARAGADAVHPG 80
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 81 YGFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAAF 160
Cdd:PRK08591 82 YGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 161 GGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIEE 240
Cdd:PRK08591 162 GGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 241 APAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLPL 320
Cdd:PRK08591 242 APSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 321 SFDGTPVP-RGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAIS 399
Cdd:PRK08591 322 SIKQEDIVfRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2414954838 400 RARRALAEFKVEGVATVLPFHRAVMDHDDFTAANtfaVHTRWIETDFAE 448
Cdd:PRK08591 402 RMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGD---YNIHYLEKKLAL 447
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-444 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 562.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 1 MKKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGL-QGERPTDTYLNIEKLLAVAARAGADAVHP 79
Cdd:PRK12999 5 IKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIgEGKHPVRAYLDIDEIIRVAKQAGVDAIHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 80 GYGFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAA 159
Cdd:PRK12999 85 GYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKAS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 160 FGGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIE 239
Cdd:PRK12999 165 AGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 240 EAPAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLP 319
Cdd:PRK12999 245 IAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGAT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 320 LSFDGTPVP-------RGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVT-EGSRVSPNFDSMIAKLIVTG 391
Cdd:PRK12999 325 LHDLEIGIPsqedirlRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAfAGAEITPYYDSLLVKLTAWG 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2414954838 392 ATREQAISRARRALAEFKVEGVATVLPFHRAVMDHDDFTAANtfaVHTRWIET 444
Cdd:PRK12999 405 RTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGD---YTTSFIDE 454
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
2-453 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 550.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 2 KKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLQGERPTDTYLNIEKLLAVAARAGADAVHPGY 81
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 82 GFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAAFG 161
Cdd:PRK08654 83 GFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 162 GGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIEEA 241
Cdd:PRK08654 163 GGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 242 PAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSgDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLPLS 321
Cdd:PRK08654 243 PSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 322 FDGTPVP-RGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAISR 400
Cdd:PRK08654 322 FKQEDITiRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIAR 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2414954838 401 ARRALAEFKVEGVATVLPFHRAVMDHDDFTAANTfavHTRWIEtdfaEHVTIA 453
Cdd:PRK08654 402 MRRALYEYVIVGVKTNIPFHKAVMENENFVRGNL---HTHFIE----EETTIL 447
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-444 |
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: 550.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 1 MKKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYgLQGER--PTDTYLNIEKLLAVAARAGADAVH 78
Cdd:COG1038 4 IKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAY-LIGEGkgPVDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 79 PGYGFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKA 158
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 159 AFGGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLI 238
Cdd:COG1038 163 AAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 239 EEAPAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGL 318
Cdd:COG1038 243 EIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 319 PLSFDGTPVP-------RGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTG-VTEGSRVSPNFDSMIAKLIVT 390
Cdd:COG1038 323 SLDDPEIGIPsqedirlNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGnAYTGAVITPYYDSLLVKVTAW 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2414954838 391 GATREQAISRARRALAEFKVEGVATVLPFHRAVMDHDDFTAANtfaVHTRWIET 444
Cdd:COG1038 403 GRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGE---CTTSFIDE 453
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
2-447 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 550.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 2 KKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLQGERPTDTYLNIEKLLAVAARAGADAVHPGY 81
Cdd:PRK06111 3 QKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 82 GFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAAFG 161
Cdd:PRK06111 83 GLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 162 GGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIEEA 241
Cdd:PRK06111 163 GGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 242 PAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLPLS 321
Cdd:PRK06111 243 PSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 322 FDGTPVPR-GHSFEFRINAEDAgNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAISR 400
Cdd:PRK06111 323 FTQDDIKRsGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISR 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2414954838 401 ARRALAEFKVEGVATVLPFHRAVMDHDDFTAANTFAVH-TRWIETDFA 447
Cdd:PRK06111 402 LHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFlTKQLVKKST 449
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
2-429 |
6.30e-174 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 500.01 E-value: 6.30e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 2 KKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLQGERPTDTYLNIEKLLAVAARAGADAVHPGY 81
Cdd:PRK05586 3 KKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 82 GFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAAFG 161
Cdd:PRK05586 83 GFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKASAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 162 GGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIEEA 241
Cdd:PRK05586 163 GGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 242 PAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLPLS 321
Cdd:PRK05586 243 PSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 322 FDGTPVP-RGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAISR 400
Cdd:PRK05586 323 IKQEDIKiNGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQK 402
|
410 420
....*....|....*....|....*....
gi 2414954838 401 ARRALAEFKVEGVATVLPFHRAVMDHDDF 429
Cdd:PRK05586 403 MKRALGEFIIEGVNTNIDFQFIILEDEEF 431
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-434 |
5.49e-172 |
|
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: 495.05 E-value: 5.49e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 1 MKKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLqGERPT-DTYLNIEKLLAVAARAGADAVHP 79
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCI-GPAPSaKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 80 GYGFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAA 159
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 160 FGGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIE 239
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 240 EAPAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLP 319
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 320 LSFDGTPVP-RGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAI 398
Cdd:TIGR00514 321 LSLKQEDVVvRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAI 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 2414954838 399 SRARRALAEFKVEGVATVLPFHRAVMDHDDFTAANT 434
Cdd:TIGR00514 401 ARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGT 436
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-433 |
2.64e-170 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 491.54 E-value: 2.64e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 1 MKKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLqGERPTDTYLNIEKLLAVAARAGADAVHPG 80
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSI-GADPLAGYLNPRRLVNLAVETGCDALHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 81 YGFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAAF 160
Cdd:PRK07178 81 YGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKATS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 161 GGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIEE 240
Cdd:PRK07178 161 GGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 241 APAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLPL 320
Cdd:PRK07178 241 APSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 321 SFDGTPVP-RGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAIS 399
Cdd:PRK07178 321 SYKQEDIQhRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALD 400
|
410 420 430
....*....|....*....|....*....|....
gi 2414954838 400 RARRALAEFKVEGVATVLPFHRAVMDHDDFTAAN 433
Cdd:PRK07178 401 RGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQ 434
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
3-429 |
6.98e-156 |
|
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: 475.86 E-value: 6.98e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 3 KVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYgLQGE----RPTDTYLNIEKLLAVAARAGADAVH 78
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESY-QVGEgpdlGPIEAYLSIDEIIRVAKLNGVDAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 79 PGYGFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKA 158
Cdd:TIGR01235 80 PGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 159 AFGGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLI 238
Cdd:TIGR01235 160 SWGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 239 EEAPAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGL 318
Cdd:TIGR01235 240 EVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 319 PLSFDGTPVP-------RGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVT-EGSRVSPNFDSMIAKLIVT 390
Cdd:TIGR01235 320 SLPTPQLGVPnqedirtNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSyAGAIITPYYDSLLVKVSAW 399
|
410 420 430
....*....|....*....|....*....|....*....
gi 2414954838 391 GATREQAISRARRALAEFKVEGVATVLPFHRAVMDHDDF 429
Cdd:TIGR01235 400 ASTPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKF 438
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-448 |
9.68e-151 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 441.94 E-value: 9.68e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 1 MKKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLqGERPTDTYLNIEKLLAVAARAGADAVHPG 80
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRI-GTDPIKGYLDVKRIVEIAKACGADAIHPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 81 YGFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEdPVNDAS--EVVAFAEQHGLPIAIKA 158
Cdd:PRK08463 81 YGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTE-KLNSESmeEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 159 AFGGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLI 238
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 239 EEAPAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGL 318
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 319 PLSFDGTPV-PRGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQA 397
Cdd:PRK08463 320 ILDLEQSDIkPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2414954838 398 ISRARRALAEFKVEGVATVLPFHRAVMDHDDFTAANtfaVHTRWIETDFAE 448
Cdd:PRK08463 400 VNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGY---FDTSYIETHMQE 447
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-460 |
1.54e-150 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 441.12 E-value: 1.54e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 1 MKKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLQGERPTDTYLNIEKLLAVAARAGADAVHPG 80
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 81 YGFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAAF 160
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 161 GGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHgRVVVVGTRDCSLQRRNQKLIEE 240
Cdd:PRK12833 165 GGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 241 APAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGD-GTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLP 319
Cdd:PRK12833 244 APSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDArGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 320 LSF-DGTPVPRGHSFEFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAI 398
Cdd:PRK12833 324 LRFaQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAAL 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2414954838 399 SRARRALAEFKVEGVATVLPFHRAVMDHDDFTAANTfavHTRWIETDFAEHVTIAPRNAEPA 460
Cdd:PRK12833 404 ARAARALRELRIDGMKTTAPLHRALLADADVRAGRF---HTNFLEAWLAEWRAALDAAASAA 462
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-446 |
4.58e-148 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 433.79 E-value: 4.58e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 1 MKKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLQGERPTDTYLNIEKLLAVAARAGADAVHPG 80
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 81 YGFLSERAEFARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAAF 160
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 161 GGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIEE 240
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 241 APAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLPL 320
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 321 SFDGTPVPRGHSFEFRINAEDAgNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAISR 400
Cdd:PRK08462 324 PSQESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIAK 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2414954838 401 ARRALAEFKVEGVATVLPFHRAVMDHDDFTAANtfaVHTRWIETDF 446
Cdd:PRK08462 403 MKRALKEFKVEGIKTTIPFHLEMMENADFINNK---YDTKYLEEHF 445
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
114-321 |
6.91e-88 |
|
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: 270.72 E-value: 6.91e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 114 DKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAAFGGGGRGLKVAWKLDEVSELYESAVREAVTAFGR 193
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 194 GECFVERFLDRPRHIEAQIIADRHGRVVVVGTRDCSLQRRNQKLIEEAPAPYLTDELRQRIHESARAVCAEAGYVGAGTV 273
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2414954838 274 EFLL-SGDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLPLS 321
Cdd:pfam02786 161 EFALdPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
334-443 |
1.32e-54 |
|
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: 180.30 E-value: 1.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 334 EFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAISRARRALAEFKVEGV 413
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100 110
....*....|....*....|....*....|
gi 2414954838 414 ATVLPFHRAVMDHDDFTAANtfaVHTRWIE 443
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGD---VDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
334-444 |
4.45e-53 |
|
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: 176.14 E-value: 4.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 334 EFRINAEDAGNGFLPTPGSIAVFQPPSGPGVRLDTGVTEGSRVSPNFDSMIAKLIVTGATREQAISRARRALAEFKVEGV 413
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100 110
....*....|....*....|....*....|.
gi 2414954838 414 ATVLPFHRAVMDHDDFTAANtfaVHTRWIET 444
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGE---VDTGFLEE 108
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
2-108 |
6.44e-48 |
|
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: 162.27 E-value: 6.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 2 KKVLIANRGEIAVRIARACRDYGVASVAVYADADIDALHVRQADEAYGLQGERPTDTYLNIEKLLAVAARAGADAVHPGY 81
Cdd:pfam00289 2 KKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPGY 81
|
90 100
....*....|....*....|....*..
gi 2414954838 82 GFLSERAEFARAVIDAGLIWIGPDPAT 108
Cdd:pfam00289 82 GFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
103-319 |
1.64e-47 |
|
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: 166.97 E-value: 1.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 103 GPDPATIDALGDKVQARRIALKVGAPLVAGteDPVNDASEVVAFAEQHGLPIAIKAAFGGGGRGLKVAWKLDEVSELYES 182
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGF--ALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 183 AVREAVTAFGRGECFVERFLDRpRHIEAQIIAdRHGRVVVvgtrdCSLQRRNQK------LIEEAPAPyLTDELRQRIHE 256
Cdd:COG0439 121 ARAEAKAGSPNGEVLVEEFLEG-REYSVEGLV-RDGEVVV-----CSITRKHQKppyfveLGHEAPSP-LPEELRAEIGE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2414954838 257 SARAVCAEAGYV-GAGTVEFLLSGDGTLSFLEVNTRLQVEH--PVTEETSGVDLVIEQLRVADGLP 319
Cdd:COG0439 193 LVARALRALGYRrGAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
510-575 |
8.56e-19 |
|
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: 80.54 E-value: 8.56e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2414954838 510 AVLTPVAGNLHAWAVEDGATVEKGQVIAIMEAMKMETSILAPCAGTV-QISKEPGGYLEAKMVIGRV 575
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVkEILVKEGDQVEAGQLLVVI 67
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
492-556 |
3.77e-14 |
|
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: 69.54 E-value: 3.77e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2414954838 492 AAAPADASQPTAEAPDPHAVLTPVAGNLHAWA-------VEDGATVEKGQVIAIMEAMKMETSILAPCAGTV 556
Cdd:COG0511 44 AAAAPAAAAAAAAASGGGAVKSPMVGTFYRAPspgakpfVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTV 115
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
91-291 |
2.58e-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: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 91 ARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEdpVNDASEVVAFAEQHGLPIAIKAAFGGGGRGLKVA 170
Cdd:COG0458 91 EEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGT--ATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 171 WKLDEvselYESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADRHGRVVVVgtrdCSLQrrNqklIEEA--------- 241
Cdd:COG0458 169 YNEEE----LEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgvhsgdsic 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2414954838 242 --PAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSgDGTLSFLEVNTR 291
Cdd:COG0458 236 vaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD-DGRVYVIEVNPR 286
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
453-557 |
5.22e-13 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 71.50 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 453 APRNAEPADPGVLRtfVEIDGKRHELGL-PAALLAGM--SLNAAAPADASQPTAEAPDPHAVLTPVAGNLHAWAVEDGAT 529
Cdd:PRK14040 468 PAAKAEPAGSETYT--VEVEGKAYVVKVsEGGDISQItpAAPAAAPAAAAAAAPAAAAGEPVTAPLAGNIFKVIVTEGQT 545
|
90 100
....*....|....*....|....*...
gi 2414954838 530 VEKGQVIAIMEAMKMETSILAPCAGTVQ 557
Cdd:PRK14040 546 VAEGDVLLILEAMKMETEIRAAQAGTVR 573
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
96-335 |
9.67e-13 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 71.15 E-value: 9.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 96 DAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGteDPVNDASEVVAFAEQHGLPIAIKAAFGGGGRGLKVAWKLDE 175
Cdd:PRK12815 652 EAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPA 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 176 VSELYESAVR--EAVTafgrgecfVERFLDrPRHIEAQIIADrhGRVVVVGTRdcslqrrnQKLIEEA-----------P 242
Cdd:PRK12815 730 LEAYLAENASqlYPIL--------IDQFID-GKEYEVDAISD--GEDVTIPGI--------IEHIEQAgvhsgdsiavlP 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 243 APYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDgTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLPLSF 322
Cdd:PRK12815 791 PQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLAND-EIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAE 869
|
250
....*....|...
gi 2414954838 323 DGTPVPRGHSFEF 335
Cdd:PRK12815 870 LGYPNGLWPGSPF 882
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
467-569 |
1.05e-12 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 71.32 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 467 TFVEID-GKRHELGLPA---ALLAGMS-----LN-----------AAAPADASQPTAEAPDPHAVLTPVAGNLHAWAVED 526
Cdd:PRK12999 1015 IEVEIEpGKTLIIKLEAigePDEDGMRtvyfeLNgqprevqvrdrSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKE 1094
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2414954838 527 GATVEKGQVIAIMEAMKMETSILAPCAGTV-QISKEPGGYLEAK 569
Cdd:PRK12999 1095 GDEVKAGDPLAVIEAMKMETTITAPVDGTVkRVLVKAGDQVEAG 1138
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
91-320 |
2.52e-12 |
|
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: 70.03 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 91 ARAVIDAGLIWIGPDPATIDALGDKVQARRIALKVGAPLVAGTEdpVNDASEVVAFAEQHGLPIAIKAAFGGGGRGLKVA 170
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKT--ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 171 WKLDEVSELyesaVREAVTAFGRGECFVERFLDRPRHIEAQIIADrHGRVVVVGTrdcslqrrnQKLIEEA--------- 241
Cdd:TIGR01369 724 YNEEELRRY----LEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD-GEEVLIPGI---------MEHIEEAgvhsgdstc 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 242 --PAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSgDGTLSFLEVNTRLQVEHPVTEETSGVDLVIEQLRVADGLP 319
Cdd:TIGR01369 790 vlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKK 868
|
.
gi 2414954838 320 L 320
Cdd:TIGR01369 869 L 869
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
491-569 |
9.15e-12 |
|
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: 68.18 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 491 NAAAPADASQPTAEAPDPHAVLTPVAGNLHAWAVEDGATVEKGQVIAIMEAMKMETSILAPCAGTV-QISKEPGGYLEAK 569
Cdd:COG1038 1059 RSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVkEVLVKEGDQVEAG 1138
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
449-576 |
1.73e-11 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 66.79 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 449 HVTIAPRNAEPADPGVLRtfveIDGKRHELGLPAAllagmslnaAAPADASQPTAEAPDphAVLTPVAGNLHAWAVEDGA 528
Cdd:PRK09282 478 EVKIEGVKAEGKRPFYLR----VDGMPEEVVVEPL---------KEIVVGGRPRASAPG--AVTSPMPGTVVKVKVKEGD 542
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2414954838 529 TVEKGQVIAIMEAMKMETSILAPCAGTV-QISKEPGGYLEAKMVIGRVE 576
Cdd:PRK09282 543 KVKAGDTVLVLEAMKMENEIQAPVDGTVkEILVKEGDRVNPGDVLMEIE 591
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
136-283 |
2.71e-10 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 62.01 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 136 PVNDASEVVAFAEQHGLPIAIKAAFGG-GGRGLkvaWKLDEVSELyesavREAVTAFGRGECFVERFLDRPRHIeAQIIA 214
Cdd:COG0026 109 AVDSLEDLEAAIAELGLPAVLKTRRGGyDGKGQ---VVIKSAADL-----EAAWAALGGGPCILEEFVPFEREL-SVIVA 179
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2414954838 215 -DRHGRVV---VVGTRdcslQRRNQkLIE-EAPAPyLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTL 283
Cdd:COG0026 180 rSPDGEVAtypVVENV----HRNGI-LDEsIAPAR-ISEALAAEAEEIAKRIAEALDYVGVLAVEFFVTKDGEL 247
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
136-291 |
2.89e-10 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 59.19 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 136 PVNDASEVVAFAEQHGLPIAIKAAFGG-GGRGLKVAWKLDEVselyesavREAVTAFGRGECFVERFLDRPRHIEAQIIA 214
Cdd:pfam02222 12 AAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADL--------PQAWEELGDGPVIVEEFVPFDRELSVLVVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 215 DRHGRVV---VVGTRdcslQRRNQKLIEEAPAPyLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNTR 291
Cdd:pfam02222 84 SVDGETAfypVVETI----QEDGICRLSVAPAR-VPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLINELAPR 158
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
1-409 |
9.05e-10 |
|
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: 60.70 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 1 MKKVLIANrgeIAVR-IARACRDYG--VASVAVYADADIDALHVRQADEAYGLQGERPTDTYlniEKLLAVAARAGADAV 77
Cdd:COG2232 4 PPDLLIAG---FSARaLAQSARRAGyrVYAVDLFADLDTRALAERWVRLDAESCGFDLEDLP---AALLELAAADDPDGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 78 HPGYGFLSERAEFARavIDAGLIWIGPDPATIDALGDKVQ-ARRIA-LKVGAPLVAGTEDPvnDASEVVafaeqhglpia 155
Cdd:COG2232 78 VYGSGFENFPELLER--LARRLPLLGNPPEVVRRVKDPLRfFALLDeLGIPHPETRFEPPP--DPGPWL----------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 156 IKAAFGGGGRGLKVAwkldevselyesavreAVTAFGRGECFVERFLDrPRHIEAQIIADRHgRVVVVGTrdcslqrrNQ 235
Cdd:COG2232 143 VKPIGGAGGWHIRPA----------------DSEAPPAPGRYFQRYVE-GTPASVLFLADGS-DARVLGF--------NR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 236 KLIEEAPA-PY----------LTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGtLSFLEVNTRLQVEHPVTEETSG 304
Cdd:COG2232 197 QLIGPAGErPFryggnigplaLPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDG-PYVLEVNPRPQASLDLYEDATG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 305 VDLVIEQLRVADG-LPlsfDGTPVPRGHSFEFRI-NAEDAgngfLPTPGSIAvfQPP-----SGPGVRLDTGvtegsrvS 377
Cdd:COG2232 276 GNLFDAHLRACRGeLP---EVPRPKPRRVAAKAIlYAPRD----LTIPDDLS--WPPwvadiPAPGTRIEKG-------E 339
|
410 420 430
....*....|....*....|....*....|..
gi 2414954838 378 PnfdsmIAKLIVTGATREQAISRARRALAEFK 409
Cdd:COG2232 340 P-----VCTVLAEGPTAEAARALLERRAEEVR 366
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
465-563 |
1.10e-09 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 56.74 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 465 LRTF-VEIDGKRH-----ELGLP---AALLAGMSLNAAAPAD-ASQPTAEAPDP------HAVLTPVAGNLHAWAVEDGA 528
Cdd:PRK06549 2 LRKFkITIDGKEYlvemeEIGAPaqaAAPAQPASTPVPVPTEaSPQVEAQAPQPaaaagaDAMPSPMPGTILKVLVAVGD 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 2414954838 529 TVEKGQVIAIMEAMKMETSILAPCAGTV-QISKEPG 563
Cdd:PRK06549 82 QVTENQPLLILEAMKMENEIVASSAGTVtAIHVTPG 117
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
137-292 |
2.31e-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: 60.40 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 137 VNDASEVVAFAEQHGLPIAIKAAFGGGGRGLKVAWKLDEVSELYESAVREAVTafgrGECFVERFLDRPRHIEAQIIADR 216
Cdd:TIGR01369 148 AHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPI----NQVLVEKSLAGWKEIEYEVMRDS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 217 HGRVVVVgtrdCSLQR------RNQKLIEEAPAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGD-GTLSFLEVN 289
Cdd:TIGR01369 224 NDNCITV----CNMENfdpmgvHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDsGRYYVIEVN 299
|
...
gi 2414954838 290 TRL 292
Cdd:TIGR01369 300 PRV 302
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
103-290 |
2.39e-09 |
|
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: 58.96 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 103 GPDPATIdALG-DKVQARRIALKVGAPLVAGTEDPVNDASEVVAFAEQHGLPIAIKAAFGGGGRGLKVAWKLDEvselYE 181
Cdd:COG1181 84 GSGVLAS-ALAmDKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEE----LA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 182 SAVREAvTAFGRgECFVERFLDrPRHIEAQIIADRHGRV-----VVVGTRDCSLQ--RRNQKLIEEAPAPyLTDELRQRI 254
Cdd:COG1181 159 AALEEA-FKYDD-KVLVEEFID-GREVTVGVLGNGGPRAlppieIVPENGFYDYEakYTDGGTEYICPAR-LPEELEERI 234
|
170 180 190
....*....|....*....|....*....|....*.
gi 2414954838 255 HESARAVCAEAGYVGAGTVEFLLSGDGTLSFLEVNT 290
Cdd:COG1181 235 QELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNT 270
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
136-283 |
4.43e-09 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 58.63 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 136 PVNDASEVVAFAEQHGLPIAIKAAFGG-GGRGlkvAWKLDEVSELyesavREAVTAFGRGECFVERFLDRPRhiEAQIIA 214
Cdd:PRK06019 120 VVDSAEDLEAALADLGLPAVLKTRRGGyDGKG---QWVIRSAEDL-----EAAWALLGSVPCILEEFVPFER--EVSVIV 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2414954838 215 --DRHGRVV---VVGTrdcslQRRNQKLIE-EAPAPyLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTL 283
Cdd:PRK06019 190 arGRDGEVVfypLVEN-----VHRNGILRTsIAPAR-ISAELQAQAEEIASRIAEELDYVGVLAVEFFVTGDGEL 258
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
509-564 |
5.81e-09 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 52.87 E-value: 5.81e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2414954838 509 HAVLTPVAGNLHAWAVEDGATVEKGQVIAIMEAMKMETSILAPCAGTVQISKEPGG 564
Cdd:PRK08225 2 TKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEG 57
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
522-575 |
6.27e-09 |
|
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: 52.60 E-value: 6.27e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2414954838 522 WAVEDGATVEKGQVIAIMEAMKMETSILAPCAGTVQ-ISKEPGGYLEAKMVIGRV 575
Cdd:pfam00364 19 WLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKeILVPEGDTVEVGDPLAKI 73
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
90-289 |
2.36e-08 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 55.72 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 90 FARAVIDAGLIWIgPDPATIDALGDKVQARRIALKVGAP----LVAgtedpvNDASEVVAFAEQHGLPIAIKAAFGGGGR 165
Cdd:COG0189 73 LLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPvpptLVT------RDPDDLRAFLEELGGPVVLKPLDGSGGR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 166 GLkvaWKLDEVSELyeSAVREAVTAFGRGECFVERFldrprhieaqiIADRHG---RVVVVGTRD-CSLQRRNQK----- 236
Cdd:COG0189 146 GV---FLVEDEDAL--ESILEALTELGSEPVLVQEF-----------IPEEDGrdiRVLVVGGEPvAAIRRIPAEgefrt 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2414954838 237 ------LIEEAPapyLTDELRQRIHESARAVcaEAGYVGagtVEFLLSGDGTLsFLEVN 289
Cdd:COG0189 210 nlarggRAEPVE---LTDEERELALRAAPAL--GLDFAG---VDLIEDDDGPL-VLEVN 259
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
137-292 |
2.68e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 53.82 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 137 VNDASEVVAFAEQHGLPIAIKAAFGGGGRGLKVAWKLDEVSELYESAVREAVTAfgrgECFVERFLDRPRHIEAQIIADR 216
Cdd:PRK12815 149 VTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIH----QCLLEESIAGWKEIEYEVMRDR 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 217 HGRVVVVG-----------TRDCslqrrnqklIEEAPAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSF 285
Cdd:PRK12815 225 NGNCITVCnmenidpvgihTGDS---------IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYY 295
|
....*...
gi 2414954838 286 L-EVNTRL 292
Cdd:PRK12815 296 LiEVNPRV 303
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
481-557 |
2.99e-06 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 47.16 E-value: 2.99e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2414954838 481 PAALLAGMSLNAAAPADASQPTAEapdpHAVLTPVAGNLHAWAVEDGATVEKGQVIAIMEAMKMETSILAPCAGTVQ 557
Cdd:PRK05641 61 PAVPSAPTPVAPAAPAPAPASAGE----NVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVK 133
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
83-292 |
3.10e-06 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 49.54 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 83 FLSE-RAEFARAVIdagLIWigPDPATIDALGDKVQARRIALKVGAPlVAGTEDpVNDASEVVAFAEQHGLPIAIKAAFG 161
Cdd:COG3919 90 LLSRhRDELEEHYR---LPY--PDADLLDRLLDKERFYELAEELGVP-VPKTVV-LDSADDLDALAEDLGFPVVVKPADS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 162 GG-----GRGLKVAWKLDEVSELyESAVREAVTAFGrgECFVERFLDRPRHIEAQIIA--DRHGRVVVVGTRdcslQRRN 234
Cdd:COG3919 163 VGydelsFPGKKKVFYVDDREEL-LALLRRIAAAGY--ELIVQEYIPGDDGEMRGLTAyvDRDGEVVATFTG----RKLR 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2414954838 235 QK--------LIEEAPAPyltdelrqRIHESARAVCAEAGYVGAGTVEFLL-SGDGTLSFLEVNTRL 292
Cdd:COG3919 236 HYppaggnsaARESVDDP--------ELEEAARRLLEALGYHGFANVEFKRdPRDGEYKLIEINPRF 294
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
479-563 |
8.27e-05 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 44.83 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 479 GLPAALLAgmslnAAAPADASQPTAEAPDP-------HAVL-TPVAGNLHAWA-------VEDGATVEKGQVIAIMEAMK 543
Cdd:PLN02983 165 SPPAAQPA-----PSAPASSPPPTPASPPPakapkssHPPLkSPMAGTFYRSPapgeppfVKVGDKVQKGQVVCIIEAMK 239
|
90 100
....*....|....*....|.
gi 2414954838 544 METSILAPCAGT-VQISKEPG 563
Cdd:PLN02983 240 LMNEIEADQSGTiVEILAEDG 260
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
120-292 |
1.02e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 45.54 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 120 RIALKVGAPLVAGTEDpvndasEVVAFAEQHG-LPIAIKAAFGGGGRGLKVAWKLDEvselYESAVREAVTAFGRGECFV 198
Cdd:PLN02735 154 KIGLKTPPSGIATTLD------ECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEE----FETICKAGLAASITSQVLV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 199 ERFLDRPRHIEAQIIADRHGRVVVVgtrdCSLQR------RNQKLIEEAPAPYLTDELRQRIHESARAVCAEAGY-VGAG 271
Cdd:PLN02735 224 EKSLLGWKEYELEVMRDLADNVVII----CSIENidpmgvHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVeCGGS 299
|
170 180
....*....|....*....|..
gi 2414954838 272 TVEFLLS-GDGTLSFLEVNTRL 292
Cdd:PLN02735 300 NVQFAVNpVDGEVMIIEMNPRV 321
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
152-410 |
1.14e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 45.22 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 152 LPIAIKAAFGGGGRGLKVAWKLDEVSELYESAVREAVTAFgrgecFVERFLDRPRHiEAQIIADRHGRVVVVGTRdcSLQ 231
Cdd:PRK02186 143 YPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAGTRAA-----LVQAYVEGDEY-SVETLTVARGHQVLGITR--KHL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 232 RRNQKLIEEA---PAPyLTDELRQRIHESARAVCAEAGY-VGAGTVEFLLSGDgTLSFLEVNTRLQVEH-PVT-EETSGV 305
Cdd:PRK02186 215 GPPPHFVEIGhdfPAP-LSAPQRERIVRTVLRALDAVGYaFGPAHTELRVRGD-TVVIIEINPRLAGGMiPVLlEEAFGV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 306 DLVIEQLRVADGLPlsFDGTPVPRGHS-FEFRINAEDA---GNGFLPTPgsiavfqPPSGPGVRLDTGVTEGSRVSP--N 379
Cdd:PRK02186 293 DLLDHVIDLHLGVA--AFADPTAKRYGaIRFVLPARSGvlrGLLFLPDD-------IAARPELRFHPLKQPGDALRLegD 363
|
250 260 270
....*....|....*....|....*....|.
gi 2414954838 380 FDSMIAKLIVTGATREQAISRARRALAEFKV 410
Cdd:PRK02186 364 FRDRIAAVVCAGDHRDSVAAAAERAVAGLSI 394
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
134-290 |
1.34e-04 |
|
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: 43.46 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 134 EDPVNDASEVVAFAEQHGLPIAIKAAFGGGGRGLKVAWKLDEvselYESAVREAvtaFGR-GECFVERFLDrPRHIEAQI 212
Cdd:pfam07478 19 DWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREE----LQAAIEEA---FQYdEKVLVEEGIE-GREIECAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 213 IADRHGRVVVVGTR--DCSLQRRNQKLIEEA-----PAPyLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSGDGTLSF 285
Cdd:pfam07478 91 LGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSaqivvPAD-LEEEQEEQIQELALKAYKALGCRGLARVDFFLTEDGEIVL 169
|
....*
gi 2414954838 286 LEVNT 290
Cdd:pfam07478 170 NEVNT 174
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
516-556 |
1.51e-04 |
|
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: 40.12 E-value: 1.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2414954838 516 AGNLHAWAVEDGATVEKGQVIAIMEAMKMETSILAPCAGTV 556
Cdd:cd06663 13 DGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTV 53
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
139-291 |
6.38e-04 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 42.42 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 139 DASEVVAFAEQHGLPIAIKAAFGGGGRGLKVAWKLDEVSELYESAVREAVTAFGRGECFVERFLDRPrhiEAQIIA--DR 216
Cdd:PLN02257 125 DPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLEEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGE---EASFFAlvDG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 217 HGRVVVVGTRDcslqrrnQKLIEE-------------APAPYLTDELRQR-----IHESARAVCAE-AGYVG---AGTVe 274
Cdd:PLN02257 202 ENAIPLESAQD-------HKRVGDgdtgpntggmgaySPAPVLTPELESKvmetiIYPTVKGMAAEgCKFVGvlyAGLM- 273
|
170
....*....|....*..
gi 2414954838 275 fLLSGDGTLSFLEVNTR 291
Cdd:PLN02257 274 -IEKKSGLPKLLEYNVR 289
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
508-576 |
7.30e-04 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 42.40 E-value: 7.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 508 PHAVLTPVAGNLHAWAVEDGATVEKGQVIAIMEAMKMETSILAPCAGTV-QISKEPGGYLEAKMVIGRVE 576
Cdd:PRK14042 525 PGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVaEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
524-577 |
1.06e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 38.07 E-value: 1.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2414954838 524 VEDGATVEKGQVIAIMEAMKMETSILAPCAGTV-QISKEPGGYLEAKMVIGRVEA 577
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVvEFLVEDGEPVEAGQVLARIEE 80
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
91-291 |
1.40e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 41.62 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 91 ARAVIDAGLIWIGPDPATIDALGDKVQARRI--ALKVGAPLvAGTedpVNDASEVVAFAEQHGLPIAIKAAFGGGGRGLK 168
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAIDLAEDRERFSKLleKLGIPQPP-NGT---ATSVEEALEVAEEIGYPVLVRPSYVLGGRAME 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 169 VAWklDEvSELyESAVREAVTAFGRGECFVERFLDRPRHIEAQIIADrhGRVVVVGTrdcSLQRrnqklIEEA------- 241
Cdd:PRK05294 722 IVY--DE-EEL-ERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD--GEDVLIGG---IMEH-----IEEAgvhsgds 787
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2414954838 242 ----PAPYLTDELRQRIHESARAVCAEAGYVGAGTVEFLLSgDGTLSFLEVNTR 291
Cdd:PRK05294 788 acslPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVK-DDEVYVIEVNPR 840
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
514-543 |
1.93e-03 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 36.27 E-value: 1.93e-03
10 20 30
....*....|....*....|....*....|
gi 2414954838 514 PVAGNLHAWAVEDGATVEKGQVIAIMEAMK 543
Cdd:pfam13533 8 PVSGKVVAVNVKEGQQVKKGDVLATLDSPE 37
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
524-572 |
3.75e-03 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 36.33 E-value: 3.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2414954838 524 VEDGATVEKGQVIAIMEAMKMETSILAPCAGTV-QISKEPGGYLEAKMVI 572
Cdd:PRK05889 18 VNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVsKVSVSVGDVIQAGDLI 67
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
102-291 |
5.72e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 39.70 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 102 IGPDPATIDALGDKVQARRIALKVGAPLVAGTedPVNDASEVVAFAEQHGLPIAIKAAFGGGGRGLKVAWKLDEVSELYE 181
Cdd:PRK05294 116 IGAKLEAIDKAEDRELFKEAMKKIGLPVPRSG--IAHSMEEALEVAEEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2414954838 182 SAVREAVTafgrGECFVERFLDRPRHIEAQIIADRHGRVVVVgtrdCSlqrrnqklIEE--------------APAPYLT 247
Cdd:PRK05294 194 RGLDLSPV----TEVLIEESLLGWKEYEYEVMRDKNDNCIIV----CS--------IENidpmgvhtgdsitvAPAQTLT 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2414954838 248 DELRQRIHESARAVCAEAGYV-GAGTVEFLLS-GDGTLSFLEVNTR 291
Cdd:PRK05294 258 DKEYQMLRDASIAIIREIGVEtGGCNVQFALNpKDGRYIVIEMNPR 303
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
517-556 |
7.96e-03 |
|
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: 35.43 E-value: 7.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2414954838 517 GNLHAWAVEDGATVEKGQVIAIMEAMKMETSILAPCAGTV 556
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVL 56
|
|
| |
