|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
960-1713 |
0e+00 |
|
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various eukaryotic acetyl-CoA carboxylases, N-terminal to the catalytic domain (pfam01039). This enzyme (EC:6.4.1.2) is involved in the synthesis of long-chain fatty acids, as it catalyzes the rate-limiting step in this process.
Pssm-ID: 462429 Cd Length: 718 Bit Score: 933.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 960 ELDDPSKVHPAEPFTGELPAQQNTADLGKKLHRVFHSVLGSLTNVMSGFCLpepffSIKLKEWVQKLMMTLRHPSL-LLD 1038
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELpYLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1039 VQEIMTSRAGRIPPPVEKSVRKVMAQYASNitsvLCQFPSQQIATILDCHAATLQRKADREVFFINTQSMVQLVQRYRSG 1118
Cdd:pfam08326 76 WQEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1119 IRGHMKTVVIDLLRRYLRVETIFgkardadanSSGMVggvrslsftsvwvvlsppaHYDKCVINLREQFKPDMSQVLDCI 1198
Cdd:pfam08326 152 LKGHEYSVFASLLEEYYDVEKLF---------SGGNV-------------------REEDVILKLRDENKDDLDKVVDIV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1199 FSHAQVTKKNQLVIMLIDELCGP---DPSLSDELISILNELTQLSKSEHCKVALRARQILIAS--PSYELRHNQVESIFL 1273
Cdd:pfam08326 204 LSHSRVSSKNKLILALLDHYRPNcpnVSNVAKELRPVLKKLAELESRETAKVALKAREVLIQCalPSLEERKNQMEHILK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1274 SAIDMYGH--------QFCPENLQKLILSETTIFDVLNTFFYHANKVVCMASLEVYVGGAYIAYVLNSLQHRQLPDGTCV 1345
Cdd:pfam08326 284 SSVVESGYgesgwkhrEPSLEVLKELIDSKYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1346 VEFQFMLPSSHPNRMTVPISITNPDLLRHTTEL------FMDSGFSPLCQRMGAMVAFRRFEDFTRNFDEVISCFANVPK 1419
Cdd:pfam08326 364 VSWQFQLPSSHSSEFGSPLSPSSDSSPPFKRIAsvsdlsYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1420 DPPLfseartslyseddcKSLREEPIHILNVSIQCADHLE-DEALVPILRTFVQSKKNILVDYGLRRIPFLIAQE-KEFP 1497
Cdd:pfam08326 444 ESGE--------------SNSSDEPINVLNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKdGQYP 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1498 KFFTFRARDEFAEDRIYRHLEPALAFQLELNRMRNFDLTAVPCANHKMHLYLGAAKVegryEVTDHRFFIRAIIRHSDLI 1577
Cdd:pfam08326 510 KYFTFRGPDNYEEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKE----NPTDKRFFVRAIIRPGRLR 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1578 TKEASFEYLQNEGERLLLEAMDELEVAfNNTNVRTDCNHIFLNFVPTVIMDPNKIEESVRYMVMRYGSRLWKLRVLQAEV 1657
Cdd:pfam08326 586 DDIPTAEYLISEAERLLNDILDALEVA-SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEI 664
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 2138330 1658 KINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRsGNIMFHSFGnKQGPQH 1713
Cdd:pfam08326 665 RIIIRDPETGPPIPLRLVITNVSGYVVKVELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1805-2353 |
0e+00 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 618.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1805 QEYPEGRDVIVIGNDITFRIGSFGPGEDLLYLRASEMARAEaIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGF 1884
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1885 KylyLTPQDYTRISSlnsvhckhieegGESRYMITDIIGKDDGLGVENLRGSGMIAGESSLAYEEIVTISLVTCRAIGIG 1964
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1965 AYLVRLGQRVIQVEN-SHIILTGASALNKVLGrEVYTSNNQLGGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNH 2043
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2044 S---PVPIITPTDPIDRE---IEFLPS--RAPYDPRWMLAGRphptlkgtwqsgfFDHGSFKEIMAPWAQTVVTGRARLG 2115
Cdd:pfam01039 224 NnrePVPIVPTKDPPDRDaplVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2116 GIPVGVIAVETRtvevavpadpanldseakiiQQAGqVWFPDSAYKTAQAIKDFNREKLPLMIFANWRGFSGGMKDMYDQ 2195
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2196 VLKFGAYIVDGLRQYKQPILIYIrpMRELRGGSWVVIDATINPLCIeMYADKESRGGVLEPEGTVEIKFRKEDLIKSMRR 2275
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVI--PRKAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2138330 2276 IDPAYKKlmeqlgepdlsdkdrkdlEGRLKAREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARtFLYW 2353
Cdd:pfam01039 427 KDLAATR------------------KQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
259-768 |
5.43e-115 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 373.97 E-value: 5.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 259 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVRMVTPEDlkANAEYIKMAD---HYGPAPGgpnNNNYANVELIV 335
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADeavCIGPAPA---AESYLNIDAII 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 336 DIAKRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPPrlrP--MVGLGDKIASTVVAQTLQVPTLPrsGSaltvewte 413
Cdd:COG4770 68 AAAKATGADAIHPGYGFLSENADFAEACEDAGIVFIGPS---PeaIRAMGDKIAAKKLMKAAGVPVVP--GS-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 414 ddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSE---IPGSP-I 489
Cdd:COG4770 135 -----------------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREakaAFGDDrV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 490 FLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYL 569
Cdd:COG4770 198 YLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 570 YSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPLH-RLKDIRllygespwgdspisfensahlpcPRGHV 648
Cdd:COG4770 278 VDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPfTQEDIK-----------------------LRGHA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 649 IATRITSENPDEGFKPSSGTVQELNFRSSKNVwgyfTVAAtgGLHE-FAISQF-----GHCFSWGENRKEAISNMVVALK 722
Cdd:COG4770 335 IECRINAEDPARGFLPSPGTITRLRPPGGPGV----RVDS--GVYEgYEIPPYydsmiAKLIVWGPDREEAIARMRRALA 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2138330 723 ELSLRGdFRTTVEYLINLLETESFQNNYIDTGWLDYLIAEKVQKKP 768
Cdd:COG4770 409 EFVIEG-VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAA 453
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
259-766 |
1.58e-100 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 331.77 E-value: 1.58e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 259 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVRMVTPEDlkANAEYIKMADH---YGPAPGgpnNNNYANVELIV 335
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEavcIGPAPS---KKSYLNIPAII 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 336 DIAKRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGP-PR-LRPMvglGDKIASTVVAQTLQVPTLPrsGSaltvewte 413
Cdd:PRK08591 68 SAAEITGADAIHPGYGFLSENADFAEICEDSGFTFIGPsAEtIRLM---GDKVTAKATMKKAGVPVVP--GS-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 414 ddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEIP---GSP-I 489
Cdd:PRK08591 135 -----------------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 490 FLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYL 569
Cdd:PRK08591 198 YMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 570 YSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPLH-RLKDIRLlygespwgdspisfensahlpcpRGHV 648
Cdd:PRK08591 278 YEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 649 IATRITSENPDEGFKPSSGTVQelnfrssknvwGYFtvaATGGLH---EFAI-----------SQFGHCFSWGENRKEAI 714
Cdd:PRK08591 335 IECRINAEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvDSAVytgytippyydSMIGKLIVHGETREEAI 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2138330 715 SNMVVALKELSLRGdFRTTVEYLINLLETESFQNNYIDTGWLDYLIAEKVQK 766
Cdd:PRK08591 401 ARMKRALSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
261-757 |
2.10e-78 |
|
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: 285.18 E-value: 2.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 261 KVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVRMVTPED------LKANAEY-IKMADHYGPApggpnnNNYANVEL 333
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 334 IVDIAKRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPPRlRPMVGLGDKIASTVVAQTLQVPTLPRSgsaltvewte 413
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKA-EVMDQLGDKVAARNLAIKAGVPVVPGT---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 414 ddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEIPGS----PI 489
Cdd:TIGR01235 135 -----------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 490 FLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYL 569
Cdd:TIGR01235 198 YVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 570 YSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPLHRLK-------DIRLlygespwgdspisfensahlp 642
Cdd:TIGR01235 278 VDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQlgvpnqeDIRT--------------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 643 cpRGHVIATRITSENPDEGFKPSSGTVQElnFRSSKnvwGYFTVAATGGLHEFAI------SQFGHCFSWGENRKEAISN 716
Cdd:TIGR01235 337 --NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSAG---GFGIRLDGGNSYAGAIitpyydSLLVKVSAWASTPEEAAAK 409
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2138330 717 MVVALKELSLRGdFRTTVEYLINLLETESFQNNYIDTGWLD 757
Cdd:TIGR01235 410 MDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
420-613 |
3.61e-54 |
|
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: 189.05 E-value: 3.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 420 KRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEIPGSP----IFLMKLA 495
Cdd:pfam02786 10 KEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 496 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQD-G 574
Cdd:pfam02786 90 KGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsG 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 2138330 575 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPL 613
Cdd:pfam02786 170 EYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
652-757 |
1.92e-27 |
|
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: 108.27 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 652 RITSENPDEGFKPSSGTVQELNFRSSKNVwgYFTVAATGGLHE--FAISQFGHCFSWGENRKEAISNMVVALKELSLRGd 729
Cdd:smart00878 3 RINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG- 79
|
90 100
....*....|....*....|....*...
gi 2138330 730 FRTTVEYLINLLETESFQNNYIDTGWLD 757
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1792-2185 |
6.39e-25 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 111.66 E-value: 6.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1792 EVGM-VAFKMRFKTQEYP-----------EGRDVIVIGNDITFRIGSFGP--GEDLLylRASEMARAEAIPKIYVAANSG 1857
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPgdgvvtgigtvDGRPVVVVANDFTVKGGSLGPmtAKKIL--RAQDIALENGLPVIYLVDSGG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1858 ARIGMaeeikhmfhvawvdpedphkgfkylyltpqdytrisslnsvhckhieeggesrymitdiigkddglGVENLRGSG 1937
Cdd:COG4799 129 ARLQE------------------------------------------------------------------GVESFAGYG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1938 MIAGESSLAYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVE-NSHIILTGASALNKVLGREVytSNNQLGGVQiMHY--N 2014
Cdd:COG4799 143 RIFYRNARSSGGIPQISVIMGPCAAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2015 GVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDP--IDREI-EFLP--SRAPYDPRWMLAGrphptlkgtwqsg 2089
Cdd:COG4799 220 GVADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPParDPEELyGIVPedPRKPYDMREVIAR------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2090 FFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAvetrtvevavpADPANLdseakiiqqAGqVWFPDSAYKTAQAIKDF 2169
Cdd:COG4799 287 LVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA-----------NQPMVL---------AG-VLDIDAADKAARFIRLC 345
|
410
....*....|....*.
gi 2138330 2170 NREKLPLMIFANWRGF 2185
Cdd:COG4799 346 DAFNIPLVFLVDVPGF 361
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
893-959 |
1.62e-14 |
|
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: 70.32 E-value: 1.62e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2138330 893 TVLRSPSAGKL-----TQITVEDGGHVEAGRRYAEMEVMKMIMTLNVQERGRVKYIKRP-GAVLEAGCVVARL 959
Cdd:pfam00364 1 TEIKSPMIGESvregvVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
894-959 |
2.88e-14 |
|
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: 69.37 E-value: 2.88e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2138330 894 VLRSPSAGKLTQITVEDGGHVEAGRRYAEMEVMKMIMTLNVQERGRVKYIK-RPGAVLEAGCVVARL 959
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
900-960 |
9.86e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 42.47 E-value: 9.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2138330 900 AGKLTQITVEDGGHVEAGRRYAEMEVMKMIMTLNVQERGRVKYIKRP-GAVLEAGCVVARLE 960
Cdd:PRK08225 9 AGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQeGDFVNEGDVLLEIE 70
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1942-2204 |
2.10e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 46.72 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1942 ESSLAYEEIVTISLVTCRAIGIGAYLVRLG-QRVIQVENSHIILTGASALNKVLGREVytSNNQLGGVQImH--YNGVSH 2018
Cdd:PLN02820 198 QARMSSAGIPQIALVLGSCTAGGAYVPAMAdESVIVKGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-HckVSGVSD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2019 ITVPDDFEGV---YTILEWL-----SYMPKDNHSPVPII-TPTDPID--REIEFLPSRAPYDPRWMLAGrphptlkgtwq 2087
Cdd:PLN02820 275 HFAQDELHALaigRNIVKNLhlaakQGMENTLGSKNPEYkEPLYDVKelRGIVPADHKQSFDVRSVIAR----------- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2088 sgFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAvetrtvevavpadpanldseakiiqqAGQVWFPDSAYKTAQAIK 2167
Cdd:PLN02820 344 --IVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALKGAHFIE 395
|
250 260 270
....*....|....*....|....*....|....*..
gi 2138330 2168 DFNREKLPLMIFANWRGFSGGMKDMYDQVLKFGAYIV 2204
Cdd:PLN02820 396 LCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMV 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
960-1713 |
0e+00 |
|
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various eukaryotic acetyl-CoA carboxylases, N-terminal to the catalytic domain (pfam01039). This enzyme (EC:6.4.1.2) is involved in the synthesis of long-chain fatty acids, as it catalyzes the rate-limiting step in this process.
Pssm-ID: 462429 Cd Length: 718 Bit Score: 933.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 960 ELDDPSKVHPAEPFTGELPAQQNTADLGKKLHRVFHSVLGSLTNVMSGFCLpepffSIKLKEWVQKLMMTLRHPSL-LLD 1038
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELpYLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1039 VQEIMTSRAGRIPPPVEKSVRKVMAQYASNitsvLCQFPSQQIATILDCHAATLQRKADREVFFINTQSMVQLVQRYRSG 1118
Cdd:pfam08326 76 WQEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1119 IRGHMKTVVIDLLRRYLRVETIFgkardadanSSGMVggvrslsftsvwvvlsppaHYDKCVINLREQFKPDMSQVLDCI 1198
Cdd:pfam08326 152 LKGHEYSVFASLLEEYYDVEKLF---------SGGNV-------------------REEDVILKLRDENKDDLDKVVDIV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1199 FSHAQVTKKNQLVIMLIDELCGP---DPSLSDELISILNELTQLSKSEHCKVALRARQILIAS--PSYELRHNQVESIFL 1273
Cdd:pfam08326 204 LSHSRVSSKNKLILALLDHYRPNcpnVSNVAKELRPVLKKLAELESRETAKVALKAREVLIQCalPSLEERKNQMEHILK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1274 SAIDMYGH--------QFCPENLQKLILSETTIFDVLNTFFYHANKVVCMASLEVYVGGAYIAYVLNSLQHRQLPDGTCV 1345
Cdd:pfam08326 284 SSVVESGYgesgwkhrEPSLEVLKELIDSKYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1346 VEFQFMLPSSHPNRMTVPISITNPDLLRHTTEL------FMDSGFSPLCQRMGAMVAFRRFEDFTRNFDEVISCFANVPK 1419
Cdd:pfam08326 364 VSWQFQLPSSHSSEFGSPLSPSSDSSPPFKRIAsvsdlsYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1420 DPPLfseartslyseddcKSLREEPIHILNVSIQCADHLE-DEALVPILRTFVQSKKNILVDYGLRRIPFLIAQE-KEFP 1497
Cdd:pfam08326 444 ESGE--------------SNSSDEPINVLNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKdGQYP 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1498 KFFTFRARDEFAEDRIYRHLEPALAFQLELNRMRNFDLTAVPCANHKMHLYLGAAKVegryEVTDHRFFIRAIIRHSDLI 1577
Cdd:pfam08326 510 KYFTFRGPDNYEEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKE----NPTDKRFFVRAIIRPGRLR 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1578 TKEASFEYLQNEGERLLLEAMDELEVAfNNTNVRTDCNHIFLNFVPTVIMDPNKIEESVRYMVMRYGSRLWKLRVLQAEV 1657
Cdd:pfam08326 586 DDIPTAEYLISEAERLLNDILDALEVA-SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEI 664
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 2138330 1658 KINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRsGNIMFHSFGnKQGPQH 1713
Cdd:pfam08326 665 RIIIRDPETGPPIPLRLVITNVSGYVVKVELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1805-2353 |
0e+00 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 618.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1805 QEYPEGRDVIVIGNDITFRIGSFGPGEDLLYLRASEMARAEaIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGF 1884
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1885 KylyLTPQDYTRISSlnsvhckhieegGESRYMITDIIGKDDGLGVENLRGSGMIAGESSLAYEEIVTISLVTCRAIGIG 1964
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1965 AYLVRLGQRVIQVEN-SHIILTGASALNKVLGrEVYTSNNQLGGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNH 2043
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2044 S---PVPIITPTDPIDRE---IEFLPS--RAPYDPRWMLAGRphptlkgtwqsgfFDHGSFKEIMAPWAQTVVTGRARLG 2115
Cdd:pfam01039 224 NnrePVPIVPTKDPPDRDaplVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2116 GIPVGVIAVETRtvevavpadpanldseakiiQQAGqVWFPDSAYKTAQAIKDFNREKLPLMIFANWRGFSGGMKDMYDQ 2195
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2196 VLKFGAYIVDGLRQYKQPILIYIrpMRELRGGSWVVIDATINPLCIeMYADKESRGGVLEPEGTVEIKFRKEDLIKSMRR 2275
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVI--PRKAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2138330 2276 IDPAYKKlmeqlgepdlsdkdrkdlEGRLKAREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARtFLYW 2353
Cdd:pfam01039 427 KDLAATR------------------KQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
259-768 |
5.43e-115 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 373.97 E-value: 5.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 259 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVRMVTPEDlkANAEYIKMAD---HYGPAPGgpnNNNYANVELIV 335
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADeavCIGPAPA---AESYLNIDAII 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 336 DIAKRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPPrlrP--MVGLGDKIASTVVAQTLQVPTLPrsGSaltvewte 413
Cdd:COG4770 68 AAAKATGADAIHPGYGFLSENADFAEACEDAGIVFIGPS---PeaIRAMGDKIAAKKLMKAAGVPVVP--GS-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 414 ddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSE---IPGSP-I 489
Cdd:COG4770 135 -----------------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREakaAFGDDrV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 490 FLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYL 569
Cdd:COG4770 198 YLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 570 YSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPLH-RLKDIRllygespwgdspisfensahlpcPRGHV 648
Cdd:COG4770 278 VDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPfTQEDIK-----------------------LRGHA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 649 IATRITSENPDEGFKPSSGTVQELNFRSSKNVwgyfTVAAtgGLHE-FAISQF-----GHCFSWGENRKEAISNMVVALK 722
Cdd:COG4770 335 IECRINAEDPARGFLPSPGTITRLRPPGGPGV----RVDS--GVYEgYEIPPYydsmiAKLIVWGPDREEAIARMRRALA 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2138330 723 ELSLRGdFRTTVEYLINLLETESFQNNYIDTGWLDYLIAEKVQKKP 768
Cdd:COG4770 409 EFVIEG-VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAA 453
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
259-766 |
1.58e-100 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 331.77 E-value: 1.58e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 259 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVRMVTPEDlkANAEYIKMADH---YGPAPGgpnNNNYANVELIV 335
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEavcIGPAPS---KKSYLNIPAII 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 336 DIAKRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGP-PR-LRPMvglGDKIASTVVAQTLQVPTLPrsGSaltvewte 413
Cdd:PRK08591 68 SAAEITGADAIHPGYGFLSENADFAEICEDSGFTFIGPsAEtIRLM---GDKVTAKATMKKAGVPVVP--GS-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 414 ddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEIP---GSP-I 489
Cdd:PRK08591 135 -----------------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 490 FLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYL 569
Cdd:PRK08591 198 YMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 570 YSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPLH-RLKDIRLlygespwgdspisfensahlpcpRGHV 648
Cdd:PRK08591 278 YEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 649 IATRITSENPDEGFKPSSGTVQelnfrssknvwGYFtvaATGGLH---EFAI-----------SQFGHCFSWGENRKEAI 714
Cdd:PRK08591 335 IECRINAEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvDSAVytgytippyydSMIGKLIVHGETREEAI 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2138330 715 SNMVVALKELSLRGdFRTTVEYLINLLETESFQNNYIDTGWLDYLIAEKVQK 766
Cdd:PRK08591 401 ARMKRALSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
257-757 |
2.51e-96 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 340.19 E-value: 2.51e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 257 RVIEKVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVRMVTPED------LKANAEYikmadHYGpAPGGPNNNnYAN 330
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAA---------TELGIRTVAIYSEEDklslhrFKADEAY-----LIG-EGKHPVRA-YLD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 331 VELIVDIAKRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPPrLRPMVGLGDKIASTVVAQTLQVPTLPRSGSAltve 410
Cdd:PRK12999 67 IDEIIRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPT-AEVLRLLGDKVAARNAAIKAGVPVIPGSEGP---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 411 wteddlqqgkrisvpedvydkgcVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEIP---GS 487
Cdd:PRK12999 142 -----------------------IDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafGN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 488 P-IFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTV 566
Cdd:PRK12999 199 DeVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 567 EYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPLHRLkdirllygespwGDSPISFENsahlPCPRG 646
Cdd:PRK12999 279 EFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATLHDL------------EIGIPSQED----IRLRG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 647 HVIATRITSENPDEGFKPSSGTVQElnFRSSknvwGYFTVAATGGLHeFA---ISQFghcF--------SWGENRKEAIS 715
Cdd:PRK12999 343 YAIQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVRLDGGNA-FAgaeITPY---YdsllvkltAWGRTFEQAVA 412
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2138330 716 NMVVALKELSLRGdFRTTVEYLINLLETESFQNNYIDTGWLD 757
Cdd:PRK12999 413 RMRRALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFID 453
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
259-757 |
1.34e-92 |
|
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: 328.58 E-value: 1.34e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 259 IEKVLIANNG-IAavkcmrsIR--RWAYEMfrnerAIRFVRMVTPED------LKANAEYikmadHYGpAPGGPNNNnYA 329
Cdd:COG1038 4 IKKVLVANRGeIA-------IRvfRAATEL-----GIRTVAIYSEEDryslhrFKADEAY-----LIG-EGKGPVDA-YL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 330 NVELIVDIAKRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPPrLRPMVGLGDKIASTVVAQTLQVPTLPrsGSaltv 409
Cdd:COG1038 65 DIEEIIRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPS-PEVLEMLGDKVAARAAAIEAGVPVIP--GT---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 410 ewteddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEIP---G 486
Cdd:COG1038 138 ---------------------EGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 487 SP-IFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGT 565
Cdd:COG1038 197 DDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 566 VEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPLHrlkdirllygespwgDSPISFENSAHLPCpR 645
Cdd:COG1038 277 VEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSLD---------------DPEIGIPSQEDIRL-N 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 646 GHVIATRITSENPDEGFKPSSGTVQElnFRSSknvwGYFTV---AATGglheFA---ISQFghcF--------SWGENRK 711
Cdd:COG1038 341 GYAIQCRITTEDPANNFMPDTGRITA--YRSA----GGFGIrldGGNA----YTgavITPY---YdsllvkvtAWGRTFE 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2138330 712 EAISNMVVALKELSLRGdFRTTVEYLINLLETESFQNNYIDTGWLD 757
Cdd:COG1038 408 EAIRKMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFID 452
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
259-759 |
5.23e-91 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 304.26 E-value: 5.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 259 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVRMVTPEDlkANAEYIKMADHYGPAPGGPNNNNYANVELIVDIA 338
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLG---------IRTVAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 339 KRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPPR--LRPMvglGDKIASTVVAQTLQVPTLPRSGSALTvewteddl 416
Cdd:PRK06111 71 KKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSAdiIAKM---GSKIEARRAMQAAGVPVVPGITTNLE-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 417 qqgkrisvpedvydkgcvkDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEIP---GSP-IFLM 492
Cdd:PRK06111 140 -------------------DAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAAnffGNGeMYIE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 493 KLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQ 572
Cdd:PRK06111 201 KYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 573 DGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPL-HRLKDIRLlygespwgdspisfensahlpcpRGHVIAT 651
Cdd:PRK06111 281 QKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR-----------------------SGHAIEV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 652 RITSENPDEgFKPSSGTVQELNFRSSKNVWGYFTVAATGGLHEFAISQFGHCFSWGENRKEAISNMVVALKELSLRGdFR 731
Cdd:PRK06111 338 RIYAEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEG-IK 415
|
490 500
....*....|....*....|....*....
gi 2138330 732 TTVEYLINLLETESFQNNYIDTGWL-DYL 759
Cdd:PRK06111 416 TNIPLLLQVLEDPVFKAGGYTTGFLtKQL 444
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
260-766 |
9.63e-89 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 299.59 E-value: 9.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 260 EKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVRMVTPEDlkANAEYIKMAD---HYGPAPGgpnNNNYANVELIVD 336
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACR---------ELGIKTVAVYSEAD--KNALFVKYADeayPIGPAPP---SKSYLNIERIID 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 337 IAKRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPPRlRPMVGLGDKIASTVVAQTLQVPTLPrsgsaltveWTEDdl 416
Cdd:PRK08654 69 VAKKAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSS-DVIEAMGSKINAKKLMKKAGVPVLP---------GTEE-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 417 qqgkrisvpedvydkgCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSeIPGS-----PIFL 491
Cdd:PRK08654 137 ----------------GIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTQS-IAQSafgdsTVFI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 492 MKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYS 571
Cdd:PRK08654 200 EKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 572 qDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPL-HRLKDIRLlygespwgdspisfensahlpcpRGHVIA 650
Cdd:PRK08654 280 -NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELsFKQEDITI-----------------------RGHAIE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 651 TRITSENPDEGFKPSSGTVQelNFRSSknvwGYFTVAATGGLH------EFAISQFGHCFSWGENRKEAISNMVVALKEL 724
Cdd:PRK08654 336 CRINAEDPLNDFAPSPGKIK--RYRSP----GGPGVRVDSGVHmgyeipPYYDSMISKLIVWGRTREEAIARMRRALYEY 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2138330 725 SLRGdFRTTVEYLINLLETESFQNNYIDTGWLD--YLIAEKVQK 766
Cdd:PRK08654 410 VIVG-VKTNIPFHKAVMENENFVRGNLHTHFIEeeTTILEEMKR 452
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
259-779 |
3.15e-84 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 285.50 E-value: 3.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 259 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVRMVTPEDLKANAeyIKMAD---HYGPAPGgpnNNNYANVELIV 335
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAAR---------ELGMRTVAACSDADRDSLA--ARMADeavHIGPSHA---AKSYLNPAAIL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 336 DIAKRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPPR--LRPMvglGDKIASTVVAQTLQVPTLPrsGSAltvewte 413
Cdd:PRK12833 71 AAARQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAqtIRTM---GDKARARRTARRAGVPTVP--GSD------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 414 ddlqqgkrisvpedvydkGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIR----ETESAEDFPILFRQVQSEIPGSPI 489
Cdd:PRK12833 139 ------------------GVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRvahdAAQLAAELPLAQREAQAAFGDGGV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 490 FLMKLAQHARHLEVQILADQYgNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYL 569
Cdd:PRK12833 201 YLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 570 Y-SQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPLH-RLKDIRLlygespwgdspisfensahlpcpRGH 647
Cdd:PRK12833 280 FdDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRfAQGDIAL-----------------------RGA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 648 VIATRITSENPDEGFKPSSGTVQELNF------RSSKNVWGYFTVAAtgglheFAISQFGHCFSWGENRKEAISNMVVAL 721
Cdd:PRK12833 337 ALECRINAEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYPGYRVPP------FYDSLLAKLIVHGEDRAAALARAARAL 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2138330 722 KELSLRGdFRTTVEYLINLLETESFQNNYIDTGWLDYLIAEKVQKKPNIMLGVVCGAL 779
Cdd:PRK12833 411 RELRIDG-MKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAALDAAASAAVGEAA 467
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
259-756 |
2.50e-83 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 281.99 E-value: 2.50e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 259 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVRMVTPEDlkANAEYIKMADH---YGPAPGGpnnNNYANVELIV 335
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACR---------EMGIETVAVYSEAD--KDALHVQLADEavcIGPASSK---DSYLNIQNII 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 336 DIAKRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPpRLRPMVGLGDKIASTVVAQTLQVPTLPRSgsaltvewtedd 415
Cdd:PRK05586 68 SATVLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGP-DSETIELMGNKSNAREIMIKAGVPVVPGS------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 416 lqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEIPGS----PIFL 491
Cdd:PRK05586 135 ---------------EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 492 MKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYS 571
Cdd:PRK05586 200 EKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 572 QDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPLH-RLKDIRLlygespwgdspisfensahlpcpRGHVIA 650
Cdd:PRK05586 280 KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSiKQEDIKI-----------------------NGHSIE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 651 TRITSENPDEGFKPSSGTVQELNFRSSKNVwgYFTVAATGG--LHEFAISQFGHCFSWGENRKEAISNMVVALKELSLRG 728
Cdd:PRK05586 337 CRINAEDPKNGFMPCPGKIEELYIPGGLGV--RVDSAVYSGytIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEG 414
|
490 500
....*....|....*....|....*...
gi 2138330 729 dFRTTVEYLINLLETESFQNNYIDTGWL 756
Cdd:PRK05586 415 -VNTNIDFQFIILEDEEFIKGTYDTSFI 441
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
259-757 |
4.98e-81 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 275.47 E-value: 4.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 259 IEKVLIANNGIAAVKCMRSIRrwayEMFRNERAIrfvrmVTPEDLKANaeYIKMADHYGPAPGGPNNNNYANVELIVDIA 338
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQ----EMGKEAIAI-----YSTADKDAL--YLKYADAKICIGGAKSSESYLNIPAIISAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 339 KRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPpRLRPMVGLGDKIASTVVAQTLQVPTLPRSgsaltvewteddlqq 418
Cdd:PRK08462 73 EIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGP-SVEVMALMSDKSKAKEVMKRAGVPVIPGS--------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 419 gkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEIPGS----PIFLMKL 494
Cdd:PRK08462 137 ------------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAfgdgTMYMEKF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 495 AQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDG 574
Cdd:PRK08462 205 INNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 575 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPLHRLKDIRLlygespwgdspisfensahlpcpRGHVIATRIT 654
Cdd:PRK08462 285 DFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKL-----------------------KGHAIECRIT 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 655 SENPdEGFKPSSGTVQEL------NFRSSKNVWGYFTVAAtgglheFAISQFGHCFSWGENRKEAISNMVVALKELSLRG 728
Cdd:PRK08462 342 AEDP-KKFYPSPGKITKWiapggrNVRMDSHAYAGYVVPP------YYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEG 414
|
490 500
....*....|....*....|....*....
gi 2138330 729 dFRTTVEYLINLLETESFQNNYIDTGWLD 757
Cdd:PRK08462 415 -IKTTIPFHLEMMENADFINNKYDTKYLE 442
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
258-779 |
4.03e-79 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 270.82 E-value: 4.03e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 258 VIEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVRMVTPEDlkANAEYIKMAD---HYGPAPGGpnnnNYANVELI 334
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACA---------EMGIRSVAIYSEAD--RHALHVKRADeaySIGADPLA----GYLNPRRL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 335 VDIAKRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPPR--LRPMvglGDKIASTVVAQTLQVPTLPRSgsaltvewt 412
Cdd:PRK07178 66 VNLAVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAevIRRM---GDKTEARRAMIKAGVPVTPGS--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 413 eddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEIP---GSP- 488
Cdd:PRK07178 134 ------------------EGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafGSAe 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 489 IFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEY 568
Cdd:PRK07178 196 VFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEF 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 569 LYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPL-HRLKDIRLlygespwgdspisfensahlpcpRGH 647
Cdd:PRK07178 276 LLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH-----------------------RGF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 648 VIATRITSENPDEGFKPSSGTVQElnfrssknvwgYFTVAATGGLHEFAI-----------SQFGHCFSWGENRKEAISN 716
Cdd:PRK07178 333 ALQFRINAEDPKNDFLPSFGKITR-----------YYAPGGPGVRTDTAIytgytippyydSMCAKLIVWALTWEEALDR 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2138330 717 MVVALKELSLRGdFRTTVEYLINLLETESFQNNYIDTGWLDY---LIAEKVQKKPNIMLGVVCGAL 779
Cdd:PRK07178 402 GRRALDDMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVEShpeLTNYSIKRKPEELAAAIAAAI 466
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
261-757 |
2.10e-78 |
|
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: 285.18 E-value: 2.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 261 KVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVRMVTPED------LKANAEY-IKMADHYGPApggpnnNNYANVEL 333
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 334 IVDIAKRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPPRlRPMVGLGDKIASTVVAQTLQVPTLPRSgsaltvewte 413
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKA-EVMDQLGDKVAARNLAIKAGVPVVPGT---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 414 ddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEIPGS----PI 489
Cdd:TIGR01235 135 -----------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 490 FLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYL 569
Cdd:TIGR01235 198 YVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 570 YSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPLHRLK-------DIRLlygespwgdspisfensahlp 642
Cdd:TIGR01235 278 VDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQlgvpnqeDIRT--------------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 643 cpRGHVIATRITSENPDEGFKPSSGTVQElnFRSSKnvwGYFTVAATGGLHEFAI------SQFGHCFSWGENRKEAISN 716
Cdd:TIGR01235 337 --NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSAG---GFGIRLDGGNSYAGAIitpyydSLLVKVSAWASTPEEAAAK 409
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2138330 717 MVVALKELSLRGdFRTTVEYLINLLETESFQNNYIDTGWLD 757
Cdd:TIGR01235 410 MDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
259-781 |
1.36e-63 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 225.85 E-value: 1.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 259 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVRMVTPEDlkANAEYIKMADHYGPAPGGPNNNnYANVELIVDIA 338
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACR---------DLHIKSVAIYTEPD--RECLHVKIADEAYRIGTDPIKG-YLDVKRIVEIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 339 KRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPPR--LRPMvglGDKIASTVVAQTLQVPTLPrsgsaltvewteddl 416
Cdd:PRK08463 70 KACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSevIRKM---GNKNIARYLMKKNGIPIVP--------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 417 qqgkrisvpedvydkGCVKDVDEGLEA----AERIGFPLMIKASEGGGGKGIRETESAEDFPILF----RQVQSEIPGSP 488
Cdd:PRK08463 132 ---------------GTEKLNSESMEEikifARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFesckREALAYFNNDE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 489 IFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEY 568
Cdd:PRK08463 197 VFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEF 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 569 LYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPLH-RLKDIRllygespwgdspisfensahlpcPRGH 647
Cdd:PRK08463 277 LLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDlEQSDIK-----------------------PRGF 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 648 VIATRITSENPDEGFKPSSGTVQEL------NFRSSKNVWGYFTVAAtgglheFAISQFGHCFSWGENRKEAISNMVVAL 721
Cdd:PRK08463 334 AIEARITAENVWKNFIPSPGKITEYypalgpSVRVDSHIYKDYTIPP------YYDSMLAKLIVKATSYDLAVNKLERAL 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2138330 722 KELSLRGdFRTTVEYLINLLETESFQNNYIDTGWLDYLIAE-------KVQKKPNIMLGVVCGALER 781
Cdd:PRK08463 408 KEFVIDG-IRTTIPFLIAITKTREFRRGYFDTSYIETHMQEllektedRHQENKEEVIAAIAAALKK 473
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
420-613 |
3.61e-54 |
|
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: 189.05 E-value: 3.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 420 KRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEIPGSP----IFLMKLA 495
Cdd:pfam02786 10 KEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 496 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQD-G 574
Cdd:pfam02786 90 KGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsG 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 2138330 575 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGAPL 613
Cdd:pfam02786 170 EYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
331-612 |
5.64e-36 |
|
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: 138.47 E-value: 5.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 331 VELIVDIAKRIPLQAVWAGWGHALEnpKLPELlckngVAFLGPPRLRP--MVGLGDKIASTVVAQTLQVPTlPRSGsalt 408
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVE--TAAEL-----AEELGLPGPSPeaIRAMRDKVLMREALAAAGVPV-PGFA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 409 vewteddlqqgkrisvpedvydkgCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEI---- 484
Cdd:COG0439 74 ------------------------LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkags 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 485 PGSPIFLMKLAQHaRHLEVQILADQyGNAVSlfgrdCSIQRRHQK---IVE---EAPATIAPlAIFEFMEQCAIRLAKTV 558
Cdd:COG0439 130 PNGEVLVEEFLEG-REYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPLPE-ELRAEIGELVARALRAL 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2138330 559 GYV-SAGTVEYLYSQDGSFHFLELNPRLQVEH--PCTEMIADVNLPAAQLQIAMGAP 612
Cdd:COG0439 202 GYRrGAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
259-374 |
1.83e-35 |
|
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: 131.45 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 259 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVRMVTPEDlkANAEYIKMADHYGPAPGGPNNNNYANVELIVDIA 338
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELG---------IRTVAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAA 69
|
90 100 110
....*....|....*....|....*....|....*.
gi 2138330 339 KRIPLQAVWAGWGHALENPKLPELLCKNGVAFLGPP 374
Cdd:pfam00289 70 KETGADAIHPGYGFLSENAEFARACEEAGIIFIGPS 105
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
652-757 |
1.92e-27 |
|
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: 108.27 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 652 RITSENPDEGFKPSSGTVQELNFRSSKNVwgYFTVAATGGLHE--FAISQFGHCFSWGENRKEAISNMVVALKELSLRGd 729
Cdd:smart00878 3 RINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG- 79
|
90 100
....*....|....*....|....*...
gi 2138330 730 FRTTVEYLINLLETESFQNNYIDTGWLD 757
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1792-2185 |
6.39e-25 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 111.66 E-value: 6.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1792 EVGM-VAFKMRFKTQEYP-----------EGRDVIVIGNDITFRIGSFGP--GEDLLylRASEMARAEAIPKIYVAANSG 1857
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPgdgvvtgigtvDGRPVVVVANDFTVKGGSLGPmtAKKIL--RAQDIALENGLPVIYLVDSGG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1858 ARIGMaeeikhmfhvawvdpedphkgfkylyltpqdytrisslnsvhckhieeggesrymitdiigkddglGVENLRGSG 1937
Cdd:COG4799 129 ARLQE------------------------------------------------------------------GVESFAGYG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1938 MIAGESSLAYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVE-NSHIILTGASALNKVLGREVytSNNQLGGVQiMHY--N 2014
Cdd:COG4799 143 RIFYRNARSSGGIPQISVIMGPCAAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2015 GVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDP--IDREI-EFLP--SRAPYDPRWMLAGrphptlkgtwqsg 2089
Cdd:COG4799 220 GVADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPParDPEELyGIVPedPRKPYDMREVIAR------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2090 FFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAvetrtvevavpADPANLdseakiiqqAGqVWFPDSAYKTAQAIKDF 2169
Cdd:COG4799 287 LVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA-----------NQPMVL---------AG-VLDIDAADKAARFIRLC 345
|
410
....*....|....*.
gi 2138330 2170 NREKLPLMIFANWRGF 2185
Cdd:COG4799 346 DAFNIPLVFLVDVPGF 361
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
652-757 |
8.41e-24 |
|
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: 97.95 E-value: 8.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 652 RITSENPDEGFKPSSGTVQELNFRSSKNVWGYFTVAATGGLHEFAISQFGHCFSWGENRKEAISNMVVALKELSLRGdFR 731
Cdd:pfam02785 3 RIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-VK 81
|
90 100
....*....|....*....|....*.
gi 2138330 732 TTVEYLINLLETESFQNNYIDTGWLD 757
Cdd:pfam02785 82 TNIPFLRAILEHPDFRAGEVDTGFLE 107
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
893-959 |
1.62e-14 |
|
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: 70.32 E-value: 1.62e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2138330 893 TVLRSPSAGKL-----TQITVEDGGHVEAGRRYAEMEVMKMIMTLNVQERGRVKYIKRP-GAVLEAGCVVARL 959
Cdd:pfam00364 1 TEIKSPMIGESvregvVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
894-959 |
2.88e-14 |
|
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: 69.37 E-value: 2.88e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2138330 894 VLRSPSAGKLTQITVEDGGHVEAGRRYAEMEVMKMIMTLNVQERGRVKYIK-RPGAVLEAGCVVARL 959
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
422-613 |
1.20e-08 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 59.56 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 422 ISVPEDVYdkgcVKDVDEGLEAAERIGFPLMIKASEG--------GGGKGIRETESAEDFPILFRQ---------VQSEI 484
Cdd:COG3919 130 VPVPKTVV----LDSADDLDALAEDLGFPVVVKPADSvgydelsfPGKKKVFYVDDREELLALLRRiaaagyeliVQEYI 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 485 PG--SPIFLmklaqharhleVQILADQYGNAVSLFGrdcsiqrrHQKIVEeAPATIAPLAIFEF-----MEQCAIRLAKT 557
Cdd:COG3919 206 PGddGEMRG-----------LTAYVDRDGEVVATFT--------GRKLRH-YPPAGGNSAARESvddpeLEEAARRLLEA 265
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2138330 558 VGYVSAGTVEYLY-SQDGSFHFLELNPRLQVEHPCTEmIADVNLPAAQLQIAMGAPL 613
Cdd:COG3919 266 LGYHGFANVEFKRdPRDGEYKLIEINPRFWRSLYLAT-AAGVNFPYLLYDDAVGRPL 321
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
432-584 |
9.46e-07 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 54.40 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 432 GCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDfpiLFRQVQSEI---PGSPIFLMKLAQHARHLEVQILAD 508
Cdd:PLN02735 721 GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDK---LKTYLETAVevdPERPVLVDKYLSDATEIDVDALAD 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 509 QYGNAV-----------SLFGRD--CSIQRrhQKIVEEAPATIaplaifefmEQCAIRLAKTVGYVSAGTVEYLYSQDGS 575
Cdd:PLN02735 798 SEGNVViggimehieqaGVHSGDsaCSLPT--QTIPSSCLATI---------RDWTTKLAKRLNVCGLMNCQYAITPSGE 866
|
....*....
gi 2138330 576 FHFLELNPR 584
Cdd:PLN02735 867 VYIIEANPR 875
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
408-638 |
1.46e-06 |
|
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: 53.85 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 408 TVEWTED-DLQQGKRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASE--GGGGKGIRETEsaEDFPILFRQVQSEI 484
Cdd:TIGR01369 121 AIKKAEDrELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGIAYNR--EELKEIAERALSAS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 485 PGSPIFLMKLAQHARHLEVQILADQYGNAVSLfgrdCSIQR-----RH--QKIVeeapatIAP---LAIFEF--MEQCAI 552
Cdd:TIGR01369 199 PINQVLVEKSLAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHtgDSIV------VAPsqtLTDKEYqmLRDASI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 553 RLAKTVGYVSAGTVEY-LYSQDGSFHFLELNPRLQ---------VEHPctemIADVnlpAAQLqiAMGAPLHRLK-DIRl 621
Cdd:TIGR01369 269 KIIRELGIEGGCNVQFaLNPDSGRYYVIEVNPRVSrssalaskaTGYP----IAKV---AAKL--AVGYTLDELKnPVT- 338
|
250
....*....|....*..
gi 2138330 622 lygespwGDSPISFENS 638
Cdd:TIGR01369 339 -------GTTPASFEPS 348
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
434-613 |
3.91e-06 |
|
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: 52.69 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 434 VKDVDEGLEAAERIGFPLMIKASEGGGGKGIRETESAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQILADqyGNA 513
Cdd:TIGR01369 690 ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 514 VSLFGrdcsIQrRHqkiVEEA-----------PATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSqDGSFHFLELN 582
Cdd:TIGR01369 768 VLIPG----IM-EH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVN 838
|
170 180 190
....*....|....*....|....*....|.
gi 2138330 583 PRLQVEHPCTEMIADVNLPAAQLQIAMGAPL 613
Cdd:TIGR01369 839 PRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
900-960 |
9.86e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 42.47 E-value: 9.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2138330 900 AGKLTQITVEDGGHVEAGRRYAEMEVMKMIMTLNVQERGRVKYIKRP-GAVLEAGCVVARLE 960
Cdd:PRK08225 9 AGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQeGDFVNEGDVLLEIE 70
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
434-584 |
1.25e-04 |
|
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: 47.18 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 434 VKDVDEGLEAAERIGFPLMIKASE--GGGGKGIRETEsaEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQILADQYG 511
Cdd:COG0458 135 ATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGIVYNE--EELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGED 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 512 NAVSLfgrdCSIQrrHqkiVEEA------PATIAP-----LAIFEFMEQCAIRLAKTVGYVSAGTVEYLYsQDGSFHFLE 580
Cdd:COG0458 213 NVIIV----GIME--H---IEPAgvhsgdSICVAPpqtlsDKEYQRLRDATLKIARALGVVGLCNIQFAV-DDGRVYVIE 282
|
....
gi 2138330 581 LNPR 584
Cdd:COG0458 283 VNPR 286
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1942-2204 |
2.10e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 46.72 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 1942 ESSLAYEEIVTISLVTCRAIGIGAYLVRLG-QRVIQVENSHIILTGASALNKVLGREVytSNNQLGGVQImH--YNGVSH 2018
Cdd:PLN02820 198 QARMSSAGIPQIALVLGSCTAGGAYVPAMAdESVIVKGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-HckVSGVSD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2019 ITVPDDFEGV---YTILEWL-----SYMPKDNHSPVPII-TPTDPID--REIEFLPSRAPYDPRWMLAGrphptlkgtwq 2087
Cdd:PLN02820 275 HFAQDELHALaigRNIVKNLhlaakQGMENTLGSKNPEYkEPLYDVKelRGIVPADHKQSFDVRSVIAR----------- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 2088 sgFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAvetrtvevavpadpanldseakiiqqAGQVWFPDSAYKTAQAIK 2167
Cdd:PLN02820 344 --IVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALKGAHFIE 395
|
250 260 270
....*....|....*....|....*....|....*..
gi 2138330 2168 DFNREKLPLMIFANWRGFSGGMKDMYDQVLKFGAYIV 2204
Cdd:PLN02820 396 LCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMV 432
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
877-953 |
2.73e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 43.20 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2138330 877 RTIGNKTCVFEK--ENDPTVLRSPSAGKLTQITVEDGGHVEAGRRYAEMEVMKMIMTLNVQERGRVKYI-KRPGAVLEAG 953
Cdd:PRK12999 1059 RSVKSTVAAREKadPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVlVKAGDQVEAG 1138
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
434-473 |
7.37e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 41.62 E-value: 7.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2138330 434 VKDVDEGLEAAERIGFPLMIKAS--EGGGGKGIRETEsaEDF 473
Cdd:PRK05294 149 AHSMEEALEVAEEIGYPVIIRPSftLGGTGGGIAYNE--EEL 188
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