|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
952-1678 |
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: 996.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 952 ELDDPSKVHAAQPFTGELPAQQTLPILGEKLHQVFHGVLENLTNVMSGYCLpepffSMKLKDWVQKLMMTLRHPSLPLLE 1031
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1032 LQEIMTSVAGRIPAPVEKAVRRVMAQYASNitsvLCQFPSQQIATILDCHAATLQRKADREVFFMNTQSIVQLVQRYRSG 1111
Cdd:pfam08326 76 WQEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1112 TRGYMKAVVLDLLRKYLNVEHHFQQA--HYDKCVINLREQFKPDMTQVLDCIFSHSQVAKKNQLVTMLIDELCGP---DP 1186
Cdd:pfam08326 152 LKGHEYSVFASLLEEYYDVEKLFSGGnvREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1187 TLSDELTSILCELTQLSRSEHCKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCPENLKKLIL 1258
Cdd:pfam08326 232 NVAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELID 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1259 SETTIFDVLPTFFYHENKVVCMASLEVYVRRGYIAYELNSLQHRELPDGTCVVEFQFMLPSSHPNRMAVPISVSNPDLLR 1338
Cdd:pfam08326 312 SKYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSPP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1339 H------STELFMDSGFSPLCQRMGAMVAFRRFEEFTRNFDEVISCFANVQtdtllfskactslySEEDSKSLREEPIHI 1412
Cdd:pfam08326 392 FkriasvSDLSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEP--------------EESGESNSSDEPINV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1413 LNVAIQCAD-HMEDEALVPVFRAFVQSKKHILVDYGLRRITFLVAQE-REFPKFFTFRARDEFAEDRIYRHLEPALAFQL 1490
Cdd:pfam08326 458 LNVAIRDAEgSDSDEELLERLEEILKENKEELLAAGVRRITFIIGRKdGQYPKYFTFRGPDNYEEDPIIRHIEPALAFQL 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1491 ELSRMRNFDLTAVPCANHKMHLYLGAAKVKEglevTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAf 1570
Cdd:pfam08326 538 ELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRDDIPTAEYLISEAERLLNDILDALEVA- 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1571 NNTSVRTDCNHIFLNFVPTVIMDPLKIEESVRDMVMRYGSRLWKLRVLQAEVKINIRQTTSDSAIPIRLFITNESGYYLD 1650
Cdd:pfam08326 613 SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGPPIPLRLVITNVSGYVVK 692
|
730 740
....*....|....*....|....*...
gi 157042798 1651 ISLYREVTDSRsGNIMFHSFGnKQGSLH 1678
Cdd:pfam08326 693 VELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1770-2324 |
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: 586.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1770 PEYPEGRDAVVIGNDITFQIGSFGIGEDFLYLRASEMARtEGIPQIYLAANSGARMGLAEEIKQIFQVAWVDPEDPHKGF 1849
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGR-KRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1850 RylyLTPQDYTQIssqnsvhckhieDEGESRYVIVDVIGKDANLGVENLRGSGMIAGEASLAYEKTVTISMVTCRALGIG 1929
Cdd:pfam01039 80 K---ILRAMEIAI------------KTGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1930 AYLVRLGQRVIQVEN-SHIILTGAGALNKVLGrEVYTSNNQLGGVQIMHTNGVSHVTVPDDFEGVCTILEWLSFIPKD-- 2006
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPap 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 2007 -NRSPVPITTPSDPIDRE---IEFTPT--KAPYDPRWMLAGRphptlkgtwqsgfFDHGSFKEIMAPWAQTVVTGRARLG 2080
Cdd:pfam01039 224 nNREPVPIVPTKDPPDRDaplVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 2081 GIPVGVIAVETRtvevavpadpanldseakiiQQAGqVWFPDSAYKTAQVIRDFNKERLPLMIFANWRGFSGGMKDMYEQ 2160
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 2161 MLKFGAYIVDGLRLYEQPILIYIPPcaELRGGSWVVLDSTINPLCIeMYADKESRGGVLEPEGTVEIKFRKKDLVKTIRR 2240
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 2241 IDPvckklvgqlgkaqlpdkdRKELEGQLKAREELLLPIYHQVAVQFADLHDTPGHMLEKGIISDVLEWKTARtFFYWRL 2320
Cdd:pfam01039 427 KDL------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPWRK 487
|
....
gi 157042798 2321 RRLL 2324
Cdd:pfam01039 488 HGNI 491
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
250-776 |
9.65e-133 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 425.20 E-value: 9.65e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 250 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVVMVTPEDlkANAEYIKMADQYVPVPGGPNNNNYANVELIIDIA 329
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 330 KRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSgsgltvewtedsrhqg 409
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 410 kcisvpedvyeQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSE---IPGSP-IFLMKLA 485
Cdd:COG4770 135 -----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREakaAFGDDrVYLEKYI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 486 QNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGS 565
Cdd:COG4770 204 ERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 566 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpipfetplsppiaRGHVIAARIT 644
Cdd:COG4770 284 FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPfTQEDIKL-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 645 SENPDEGFKPSSGTVQELNF------------RSNKNVWGYFsvaaagglhefaDSQFGHCFSWGENREEAISNMVVALK 712
Cdd:COG4770 341 AEDPARGFLPSPGTITRLRPpggpgvrvdsgvYEGYEIPPYY------------DSMIAKLIVWGPDREEAIARMRRALA 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157042798 713 ELSIRGdFRTTVEYLVNLLETESFQNNDIDTGWLDHLIAQRVQAEKPDimlgvvcgALNVADAM 776
Cdd:COG4770 409 EFVIEG-VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE--------ELALAAAM 463
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
250-756 |
1.81e-115 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 374.91 E-value: 1.81e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 250 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADQYVPVPGGPNNNNYANVELIIDIA 329
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 330 KRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPwsGSgltvewtedsrhqg 409
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 410 kcisvpedvyeQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIP---GSP-IFLMKLA 485
Cdd:PRK08591 135 -----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 486 QNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGS 565
Cdd:PRK08591 204 ENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 566 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpipfetplsppiaRGHVIAARIT 644
Cdd:PRK08591 284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 645 SENPDEGFKPSSGTVQelnfrsnknvwGYFsvaAAGGLH--------------EFADSQFGHCFSWGENREEAISNMVVA 710
Cdd:PRK08591 341 AEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 157042798 711 LKELSIRGdFRTTVEYLVNLLETESFQNNDIDTGWLDHLIAQRVQA 756
Cdd:PRK08591 407 LSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
252-747 |
1.25e-86 |
|
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: 310.61 E-value: 1.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 252 KVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEY-IKMADQYVPVpggpnnNNYANVEL 324
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 325 IIDIAKRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSgsgltvewted 404
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 405 srhqgkcisvpedvyeQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIPGS----PIF 480
Cdd:TIGR01235 135 ----------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 481 LMKLAQNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLY 560
Cdd:TIGR01235 199 VEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 561 SQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLK-------DIRLlygespwgvtpipfetplsppi 633
Cdd:TIGR01235 279 DNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQlgvpnqeDIRT---------------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 634 aRGHVIAARITSENPDEGFKPSSGTVQElnFRSNknvwGYFSVAAAGG-------LHEFADSQFGHCFSWGENREEAISN 706
Cdd:TIGR01235 337 -NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAK 409
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 157042798 707 MVVALKELSIRGdFRTTVEYLVNLLETESFQNNDIDTGWLD 747
Cdd:TIGR01235 410 MDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
422-603 |
5.16e-56 |
|
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: 194.06 E-value: 5.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 422 GCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIPGSP----IFLMKLAQNARHLEVQVLA 497
Cdd:pfam02786 22 GPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 498 DQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQD-GSFHFLELNPRLQ 576
Cdd:pfam02786 102 DAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsGEYYFIEMNTRLQ 181
|
170 180
....*....|....*....|....*..
gi 157042798 577 VEHPCTEMIADVNLPAAQLQIAMGVPL 603
Cdd:pfam02786 182 VEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
641-747 |
1.78e-33 |
|
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: 125.60 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 641 ARITSENPDEGFKPSSGTVQELNFRSNKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 718
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 157042798 719 dFRTTVEYLVNLLETESFQNNDIDTGWLD 747
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1774-2150 |
1.15e-21 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 101.64 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1774 EGRDAVVIGNDITFQIGSFG--IGEDFLylRASEMARTEGIPQIYLAANSGARMglaeeikqifqvawvdPEdphkgfry 1851
Cdd:COG4799 80 DGRPVVVVANDFTVKGGSLGpmTAKKIL--RAQDIALENGLPVIYLVDSGGARL----------------QE-------- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1852 lyltpqdytqissqnsvhckhiedegesryvivdvigkdanlGVENLRGSGMIAGEASLAYEKTVTISMVTCRALGIGAY 1931
Cdd:COG4799 134 ------------------------------------------GVESFAGYGRIFYRNARSSGGIPQISVIMGPCAAGGAY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1932 LVRLGQRVIQVE-NSHIILTGAGALNKVLGREVytSNNQLGGVQiMHT--NGVSHVTVPDDFEGVCTILEWLSFIPKDNR 2008
Cdd:COG4799 172 SPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvSGVADYLAEDEEEALALARRLLSYLPSNNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 2009 SPVPITTPSDP--IDREI-EFTPT--KAPYDPRWMLAGrphptlkgtwqsgFFDHGSFKEIMAPWAQTVVTGRARLGGIP 2083
Cdd:COG4799 249 EDPPRAEPAPParDPEELyGIVPEdpRKPYDMREVIAR-------------LVDGGSFFEFKPLYGPNIVTGFARIDGRP 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157042798 2084 VGVIAvetrtvevavpADPANLdseakiiqqAGqVWFPDSAYKTAQVIRDFNKERLPLMIFANWRGF 2150
Cdd:COG4799 316 VGIVA-----------NQPMVL---------AG-VLDIDAADKAARFIRLCDAFNIPLVFLVDVPGF 361
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
885-951 |
1.53e-16 |
|
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: 76.10 E-value: 1.53e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157042798 885 TVLRSPSAGKLM-----QYTVEDGDHVEAGSSYAEMEVMKMIMTLNVQESGRVKYIKRP-GVILEAGCVVARL 951
Cdd:pfam00364 1 TEIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
886-951 |
6.45e-15 |
|
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: 71.29 E-value: 6.45e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157042798 886 VLRSPSAGKLMQYTVEDGDHVEAGSSYAEMEVMKMIMTLNVQESGRVKYIK-RPGVILEAGCVVARL 951
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
892-952 |
9.80e-06 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 45.55 E-value: 9.80e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157042798 892 AGKLMQYTVEDGDHVEAGSSYAEMEVMKMIMTLNVQESGRVKYIKRP-GVILEAGCVVARLE 952
Cdd:PRK08225 9 AGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQeGDFVNEGDVLLEIE 70
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1907-2169 |
1.68e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 46.72 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1907 EASLAYEKTVTISMV--TCRAlGiGAYLVRLG-QRVIQVENSHIILTGAGALNKVLGREVytSNNQLGGVQImH--TNGV 1981
Cdd:PLN02820 198 QARMSSAGIPQIALVlgSCTA-G-GAYVPAMAdESVIVKGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-HckVSGV 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1982 SHVTVPDDFEGVC---TILEWLSFIPKDNRSPV------PITTPSDPID--REIEFTPTKAPYDPRWMLAGrphptlkgt 2050
Cdd:PLN02820 273 SDHFAQDELHALAigrNIVKNLHLAAKQGMENTlgsknpEYKEPLYDVKelRGIVPADHKQSFDVRSVIAR--------- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 2051 wqsgFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAvetrtvevavpadpanldseakiiqqAGQVWFPDSAYKTAQV 2130
Cdd:PLN02820 344 ----IVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALKGAHF 393
|
250 260 270
....*....|....*....|....*....|....*....
gi 157042798 2131 IRDFNKERLPLMIFANWRGFSGGMKDMYEQMLKFGAYIV 2169
Cdd:PLN02820 394 IELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMV 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 ... |
952-1678 |
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: 996.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 952 ELDDPSKVHAAQPFTGELPAQQTLPILGEKLHQVFHGVLENLTNVMSGYCLpepffSMKLKDWVQKLMMTLRHPSLPLLE 1031
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1032 LQEIMTSVAGRIPAPVEKAVRRVMAQYASNitsvLCQFPSQQIATILDCHAATLQRKADREVFFMNTQSIVQLVQRYRSG 1111
Cdd:pfam08326 76 WQEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1112 TRGYMKAVVLDLLRKYLNVEHHFQQA--HYDKCVINLREQFKPDMTQVLDCIFSHSQVAKKNQLVTMLIDELCGP---DP 1186
Cdd:pfam08326 152 LKGHEYSVFASLLEEYYDVEKLFSGGnvREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1187 TLSDELTSILCELTQLSRSEHCKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCPENLKKLIL 1258
Cdd:pfam08326 232 NVAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELID 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1259 SETTIFDVLPTFFYHENKVVCMASLEVYVRRGYIAYELNSLQHRELPDGTCVVEFQFMLPSSHPNRMAVPISVSNPDLLR 1338
Cdd:pfam08326 312 SKYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSPP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1339 H------STELFMDSGFSPLCQRMGAMVAFRRFEEFTRNFDEVISCFANVQtdtllfskactslySEEDSKSLREEPIHI 1412
Cdd:pfam08326 392 FkriasvSDLSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEP--------------EESGESNSSDEPINV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1413 LNVAIQCAD-HMEDEALVPVFRAFVQSKKHILVDYGLRRITFLVAQE-REFPKFFTFRARDEFAEDRIYRHLEPALAFQL 1490
Cdd:pfam08326 458 LNVAIRDAEgSDSDEELLERLEEILKENKEELLAAGVRRITFIIGRKdGQYPKYFTFRGPDNYEEDPIIRHIEPALAFQL 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1491 ELSRMRNFDLTAVPCANHKMHLYLGAAKVKEglevTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAf 1570
Cdd:pfam08326 538 ELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRDDIPTAEYLISEAERLLNDILDALEVA- 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1571 NNTSVRTDCNHIFLNFVPTVIMDPLKIEESVRDMVMRYGSRLWKLRVLQAEVKINIRQTTSDSAIPIRLFITNESGYYLD 1650
Cdd:pfam08326 613 SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGPPIPLRLVITNVSGYVVK 692
|
730 740
....*....|....*....|....*...
gi 157042798 1651 ISLYREVTDSRsGNIMFHSFGnKQGSLH 1678
Cdd:pfam08326 693 VELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1770-2324 |
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: 586.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1770 PEYPEGRDAVVIGNDITFQIGSFGIGEDFLYLRASEMARtEGIPQIYLAANSGARMGLAEEIKQIFQVAWVDPEDPHKGF 1849
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGR-KRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1850 RylyLTPQDYTQIssqnsvhckhieDEGESRYVIVDVIGKDANLGVENLRGSGMIAGEASLAYEKTVTISMVTCRALGIG 1929
Cdd:pfam01039 80 K---ILRAMEIAI------------KTGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1930 AYLVRLGQRVIQVEN-SHIILTGAGALNKVLGrEVYTSNNQLGGVQIMHTNGVSHVTVPDDFEGVCTILEWLSFIPKD-- 2006
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPap 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 2007 -NRSPVPITTPSDPIDRE---IEFTPT--KAPYDPRWMLAGRphptlkgtwqsgfFDHGSFKEIMAPWAQTVVTGRARLG 2080
Cdd:pfam01039 224 nNREPVPIVPTKDPPDRDaplVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 2081 GIPVGVIAVETRtvevavpadpanldseakiiQQAGqVWFPDSAYKTAQVIRDFNKERLPLMIFANWRGFSGGMKDMYEQ 2160
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 2161 MLKFGAYIVDGLRLYEQPILIYIPPcaELRGGSWVVLDSTINPLCIeMYADKESRGGVLEPEGTVEIKFRKKDLVKTIRR 2240
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 2241 IDPvckklvgqlgkaqlpdkdRKELEGQLKAREELLLPIYHQVAVQFADLHDTPGHMLEKGIISDVLEWKTARtFFYWRL 2320
Cdd:pfam01039 427 KDL------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPWRK 487
|
....
gi 157042798 2321 RRLL 2324
Cdd:pfam01039 488 HGNI 491
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
250-776 |
9.65e-133 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 425.20 E-value: 9.65e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 250 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVVMVTPEDlkANAEYIKMADQYVPVPGGPNNNNYANVELIIDIA 329
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 330 KRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSgsgltvewtedsrhqg 409
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 410 kcisvpedvyeQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSE---IPGSP-IFLMKLA 485
Cdd:COG4770 135 -----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREakaAFGDDrVYLEKYI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 486 QNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGS 565
Cdd:COG4770 204 ERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 566 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpipfetplsppiaRGHVIAARIT 644
Cdd:COG4770 284 FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPfTQEDIKL-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 645 SENPDEGFKPSSGTVQELNF------------RSNKNVWGYFsvaaagglhefaDSQFGHCFSWGENREEAISNMVVALK 712
Cdd:COG4770 341 AEDPARGFLPSPGTITRLRPpggpgvrvdsgvYEGYEIPPYY------------DSMIAKLIVWGPDREEAIARMRRALA 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157042798 713 ELSIRGdFRTTVEYLVNLLETESFQNNDIDTGWLDHLIAQRVQAEKPDimlgvvcgALNVADAM 776
Cdd:COG4770 409 EFVIEG-VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE--------ELALAAAM 463
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
250-756 |
1.81e-115 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 374.91 E-value: 1.81e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 250 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADQYVPVPGGPNNNNYANVELIIDIA 329
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 330 KRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPwsGSgltvewtedsrhqg 409
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 410 kcisvpedvyeQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIP---GSP-IFLMKLA 485
Cdd:PRK08591 135 -----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 486 QNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGS 565
Cdd:PRK08591 204 ENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 566 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpipfetplsppiaRGHVIAARIT 644
Cdd:PRK08591 284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 645 SENPDEGFKPSSGTVQelnfrsnknvwGYFsvaAAGGLH--------------EFADSQFGHCFSWGENREEAISNMVVA 710
Cdd:PRK08591 341 AEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 157042798 711 LKELSIRGdFRTTVEYLVNLLETESFQNNDIDTGWLDHLIAQRVQA 756
Cdd:PRK08591 407 LSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
248-747 |
9.50e-104 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 362.53 E-value: 9.50e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 248 RVIEKVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEYIkmadqyVPVPGGPNNNnYAN 321
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAA---------TELGIRTVAIYSEEDklslhrFKADEAYL------IGEGKHPVRA-YLD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 322 VELIIDIAKRIPVQAVWAGWGHASENPKLPELlCKHE-IAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSGSGltve 400
Cdd:PRK12999 67 IDEIIRVAKQAGVDAIHPGYGFLSENPEFARA-CAEAgITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGP---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 401 wtedsrhqgkcisvpedvyeqgcVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIP---GS 477
Cdd:PRK12999 142 -----------------------IDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafGN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 478 P-IFLMKLAQNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTV 556
Cdd:PRK12999 199 DeVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 557 EYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRL-------KDIRLlygespwgvtpipfetpl 629
Cdd:PRK12999 279 EFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATLHDLeigipsqEDIRL------------------ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 630 sppiaRGHVIAARITSENPDEGFKPSSGTVQElnFRSNknvwGYFSV------AAAGGlhEFA---DSQFGHCFSWGENR 700
Cdd:PRK12999 341 -----RGYAIQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVrldggnAFAGA--EITpyyDSLLVKLTAWGRTF 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 157042798 701 EEAISNMVVALKELSIRGdFRTTVEYLVNLLETESFQNNDIDTGWLD 747
Cdd:PRK12999 408 EQAVARMRRALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFID 453
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
250-753 |
4.91e-102 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 336.23 E-value: 4.91e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 250 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVVMVTPEDlkANAEYIKMADQYVPVPGGPNNNNYANVELIIDIA 329
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLG---------IRTVAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 330 KRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSGSGLTvewtedsrhqg 409
Cdd:PRK06111 71 KKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLE----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 410 kcisvpedvyeqgcvkDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIP---GSP-IFLMKLA 485
Cdd:PRK06111 140 ----------------DAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAAnffGNGeMYIEKYI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 486 QNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGS 565
Cdd:PRK06111 204 EDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 566 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL-HRLKDIRLlygespwgvtpipfetplsppiaRGHVIAARIT 644
Cdd:PRK06111 284 FYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR-----------------------SGHAIEVRIY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 645 SENPDEgFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTV 724
Cdd:PRK06111 341 AEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEG-IKTNI 418
|
490 500
....*....|....*....|....*....
gi 157042798 725 EYLVNLLETESFQNNDIDTGWLDHLIAQR 753
Cdd:PRK06111 419 PLLLQVLEDPVFKAGGYTTGFLTKQLVKK 447
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
251-747 |
5.18e-101 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 335.03 E-value: 5.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 251 EKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADQYVPVPGGPNNNNYANVELIIDIAK 330
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACR---------ELGIKTVAVYSEAD--KNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 331 RIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSgsgltvewtedsrhqgk 410
Cdd:PRK08654 72 KAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGT----------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 411 cisvpedvyeQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSeIPGS-----PIFLMKLA 485
Cdd:PRK08654 135 ----------EEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTQS-IAQSafgdsTVFIEKYL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 486 QNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSqDGS 565
Cdd:PRK08654 204 EKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGN 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 566 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL-HRLKDIRLlygespwgvtpipfetplsppiaRGHVIAARIT 644
Cdd:PRK08654 283 FYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELsFKQEDITI-----------------------RGHAIECRIN 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 645 SENPDEGFKPSSGTVQelnfrsnknvwGYFSVAAAG-----GLH------EFADSQFGHCFSWGENREEAISNMVVALKE 713
Cdd:PRK08654 340 AEDPLNDFAPSPGKIK-----------RYRSPGGPGvrvdsGVHmgyeipPYYDSMISKLIVWGRTREEAIARMRRALYE 408
|
490 500 510
....*....|....*....|....*....|....
gi 157042798 714 LSIRGdFRTTVEYLVNLLETESFQNNDIDTGWLD 747
Cdd:PRK08654 409 YVIVG-VKTNIPFHKAVMENENFVRGNLHTHFIE 441
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
250-747 |
9.46e-99 |
|
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: 347.45 E-value: 9.46e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 250 IEKVLIANNG-IAavkcmrsIR--RWAYEMfrnerAIRFVVMVTPED------LKANAEYIkmadqyVPVPGGPNNNnYA 320
Cdd:COG1038 4 IKKVLVANRGeIA-------IRvfRAATEL-----GIRTVAIYSEEDryslhrFKADEAYL------IGEGKGPVDA-YL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 321 NVELIIDIAKRIPVQAVWAGWGHASENPKLPELlCKHE-IAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPwsGSGltv 399
Cdd:COG1038 65 DIEEIIRVAKEKGVDAIHPGYGFLSENPEFARA-CEEAgITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP--GTE--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 400 ewtedsrhqgkcisvpedvyeqGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIP---G 476
Cdd:COG1038 139 ----------------------GPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 477 SP-IFLMKLAQNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGT 555
Cdd:COG1038 197 DDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 556 VEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-------RLKDIRLlygespwgvtpipfetp 628
Cdd:COG1038 277 VEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSLDdpeigipSQEDIRL----------------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 629 lsppiaRGHVIAARITSENPDEGFKPSSGTVQElnFRSnknvwgyfsvaaAGGlhefadsqFG------HCFS------- 695
Cdd:COG1038 340 ------NGYAIQCRITTEDPANNFMPDTGRITA--YRS------------AGG--------FGirldggNAYTgavitpy 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157042798 696 ----------WGENREEAISNMVVALKELSIRGdFRTTVEYLVNLLETESFQNNDIDTGWLD 747
Cdd:COG1038 392 ydsllvkvtaWGRTFEEAIRKMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFID 452
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
250-748 |
1.45e-94 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 314.38 E-value: 1.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 250 IEKVLIANNGIAAVKCMRSIRrwayEMfrNERAIrfVVMVTPEDlkaNAEYIKMADQYVPVPGGPNNNNYANVELIIDIA 329
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQ----EM--GKEAI--AIYSTADK---DALYLKYADAKICIGGAKSSESYLNIPAIISAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 330 KRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSgsgltvewtedsrhqg 409
Cdd:PRK08462 73 EIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGS---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 410 kcisvpedvyeQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIPGS----PIFLMKLA 485
Cdd:PRK08462 137 -----------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAfgdgTMYMEKFI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 486 QNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGS 565
Cdd:PRK08462 206 NNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 566 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLlygespwgvtpipfetplsppiaRGHVIAARITS 645
Cdd:PRK08462 286 FYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKL-----------------------KGHAIECRITA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 646 ENPdEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGd 719
Cdd:PRK08462 343 EDP-KKFYPSPGKITKWiapggrNVRMDSHAYAGYVVPP------YYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEG- 414
|
490 500
....*....|....*....|....*....
gi 157042798 720 FRTTVEYLVNLLETESFQNNDIDTGWLDH 748
Cdd:PRK08462 415 IKTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
250-746 |
7.07e-93 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 309.72 E-value: 7.07e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 250 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADQYVPVPGGPNNNNYANVELIIDIA 329
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACR---------EMGIETVAVYSEAD--KDALHVQLADEAVCIGPASSKDSYLNIQNIISAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 330 KRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSgsgltvewtedsrhqg 409
Cdd:PRK05586 71 VLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 410 kcisvpedvyeQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIPGS----PIFLMKLA 485
Cdd:PRK05586 135 -----------EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 486 QNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGS 565
Cdd:PRK05586 204 ENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 566 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpipfetplsppiaRGHVIAARIT 644
Cdd:PRK05586 284 FYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSiKQEDIKI-----------------------NGHSIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 645 SENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTV 724
Cdd:PRK05586 341 AEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEG-VNTNI 419
|
490 500
....*....|....*....|..
gi 157042798 725 EYLVNLLETESFQNNDIDTGWL 746
Cdd:PRK05586 420 DFQFIILEDEEFIKGTYDTSFI 441
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
250-756 |
1.42e-88 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 297.82 E-value: 1.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 250 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDLKANAeyIKMADQYVPVPGGPNNNNYANVELIIDIA 329
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAAR---------ELGMRTVAACSDADRDSLA--ARMADEAVHIGPSHAAKSYLNPAAILAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 330 KRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSgsgltvewtedsrhqg 409
Cdd:PRK12833 74 RQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGS---------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 410 kcisvpedvyeQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIP---GSP-IFLMKLA 485
Cdd:PRK12833 138 -----------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQaafGDGgVYLERFI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 486 QNARHLEVQVLADQYgNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLY-SQDG 564
Cdd:PRK12833 207 ARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFdDARG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 565 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpipfetplsppiaRGHVIAARI 643
Cdd:PRK12833 286 EFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRfAQGDIAL-----------------------RGAALECRI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 644 TSENPDEGFKPSSGTVQELNF------RSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIR 717
Cdd:PRK12833 343 NAEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYPGYRVPP------FYDSLLAKLIVHGEDRAAALARAARALRELRID 416
|
490 500 510
....*....|....*....|....*....|....*....
gi 157042798 718 GdFRTTVEYLVNLLETESFQNNDIDTGWLDHLIAQRVQA 756
Cdd:PRK12833 417 G-MKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAA 454
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
252-747 |
1.25e-86 |
|
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: 310.61 E-value: 1.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 252 KVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEY-IKMADQYVPVpggpnnNNYANVEL 324
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 325 IIDIAKRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSgsgltvewted 404
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 405 srhqgkcisvpedvyeQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIPGS----PIF 480
Cdd:TIGR01235 135 ----------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 481 LMKLAQNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLY 560
Cdd:TIGR01235 199 VEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 561 SQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLK-------DIRLlygespwgvtpipfetplsppi 633
Cdd:TIGR01235 279 DNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQlgvpnqeDIRT---------------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 634 aRGHVIAARITSENPDEGFKPSSGTVQElnFRSNknvwGYFSVAAAGG-------LHEFADSQFGHCFSWGENREEAISN 706
Cdd:TIGR01235 337 -NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAK 409
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 157042798 707 MVVALKELSIRGdFRTTVEYLVNLLETESFQNNDIDTGWLD 747
Cdd:TIGR01235 410 MDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
249-747 |
6.40e-86 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 290.47 E-value: 6.40e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 249 VIEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADQYV-----PVPGgpnnnnYANVE 323
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACA---------EMGIRSVAIYSEAD--RHALHVKRADEAYsigadPLAG------YLNPR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 324 LIIDIAKRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWSgsgltvewte 403
Cdd:PRK07178 64 RLVNLAVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGS---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 404 dsrhqgkcisvpedvyeQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIP---GSP-I 479
Cdd:PRK07178 134 -----------------EGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafGSAeV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 480 FLMKLAQNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYL 559
Cdd:PRK07178 197 FLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 560 YSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL-HRLKDIRLlygespwgvtpipfetplsppiaRGHV 638
Cdd:PRK07178 277 LDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH-----------------------RGFA 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 639 IAARITSENPDEGFKPSSGTVQElnfrsnknvwgYFSVAAAG---------GLH--EFADSQFGHCFSWGENREEAISNM 707
Cdd:PRK07178 334 LQFRINAEDPKNDFLPSFGKITR-----------YYAPGGPGvrtdtaiytGYTipPYYDSMCAKLIVWALTWEEALDRG 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 157042798 708 VVALKELSIRGdFRTTVEYLVNLLETESFQNNDIDTGWLD 747
Cdd:PRK07178 403 RRALDDMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVE 441
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
250-770 |
7.66e-69 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 241.26 E-value: 7.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 250 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADQYVPVPGGPNNNnYANVELIIDIA 329
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACR---------DLHIKSVAIYTEPD--RECLHVKIADEAYRIGTDPIKG-YLDVKRIVEIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 330 KRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEAMWALGDKIASTIVAQTLQIPTLPWsgsgltvewTEDSRHQg 409
Cdd:PRK08463 70 KACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPG---------TEKLNSE- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 410 kcisvpedvyeqgcvkDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLF----RQVQSEIPGSPIFLMKLA 485
Cdd:PRK08463 140 ----------------SMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFesckREALAYFNNDEVFMEKYV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 486 QNARHLEVQVLADQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGS 565
Cdd:PRK08463 204 VNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 566 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRllygespwgvtpipfetplsppiARGHVIAARIT 644
Cdd:PRK08463 284 FYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDlEQSDIK-----------------------PRGFAIEARIT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 645 SENPDEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRG 718
Cdd:PRK08463 341 AENVWKNFIPSPGKITEYypalgpSVRVDSHIYKDYTIPP------YYDSMLAKLIVKATSYDLAVNKLERALKEFVIDG 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 157042798 719 dFRTTVEYLVNLLETESFQNNDIDTGWLDHLI------AQRVQAEKPDIMLGVVCGAL 770
Cdd:PRK08463 415 -IRTTIPFLIAITKTREFRRGYFDTSYIETHMqellekTEDRHQENKEEVIAAIAAAL 471
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
422-603 |
5.16e-56 |
|
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: 194.06 E-value: 5.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 422 GCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIPGSP----IFLMKLAQNARHLEVQVLA 497
Cdd:pfam02786 22 GPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 498 DQYGNAVSLFGRDCSIQRRHQKIIEEAPATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQD-GSFHFLELNPRLQ 576
Cdd:pfam02786 102 DAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsGEYYFIEMNTRLQ 181
|
170 180
....*....|....*....|....*..
gi 157042798 577 VEHPCTEMIADVNLPAAQLQIAMGVPL 603
Cdd:pfam02786 182 VEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
250-368 |
4.72e-42 |
|
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: 150.33 E-value: 4.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 250 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVVMVTPEDlkANAEYIKMADQYVPVPGGPNNNNYANVELIIDIA 329
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELG---------IRTVAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAA 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 157042798 330 KRIPVQAVWAGWGHASENPKLPELLCKHEIAFLGPPSEA 368
Cdd:pfam00289 70 KETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
322-602 |
8.88e-39 |
|
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: 146.56 E-value: 8.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 322 VELIIDIAKRIPVQAVWAGWGHASEnpKLPELLCKHEIAflGPPSEAMWALGDKIASTIVAQTLQIPTlPWSGsgltvew 401
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVE--TAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 402 tedsrhqgkcisvpedvyeqgCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEI----PGS 477
Cdd:COG0439 74 ---------------------LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 478 PIFLMKLAQNaRHLEVQVLADQyGNAVSlfgrdCSIQRRHQK---IIE---EAPATIaAPAVFEFMEQCAVLLAKMVGYV 551
Cdd:COG0439 133 EVLVEEFLEG-REYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPL-PEELRAEIGELVARALRALGYR 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 157042798 552 -SAGTVEYLYSQDGSFHFLELNPRLQVEH--PCTEMIADVNLPAAQLQIAMGVP 602
Cdd:COG0439 205 rGAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
641-747 |
1.78e-33 |
|
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: 125.60 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 641 ARITSENPDEGFKPSSGTVQELNFRSNKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 718
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 157042798 719 dFRTTVEYLVNLLETESFQNNDIDTGWLD 747
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
641-748 |
4.06e-30 |
|
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: 116.05 E-value: 4.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 641 ARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 720
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*...
gi 157042798 721 RTTVEYLVNLLETESFQNNDIDTGWLDH 748
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1774-2150 |
1.15e-21 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 101.64 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1774 EGRDAVVIGNDITFQIGSFG--IGEDFLylRASEMARTEGIPQIYLAANSGARMglaeeikqifqvawvdPEdphkgfry 1851
Cdd:COG4799 80 DGRPVVVVANDFTVKGGSLGpmTAKKIL--RAQDIALENGLPVIYLVDSGGARL----------------QE-------- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1852 lyltpqdytqissqnsvhckhiedegesryvivdvigkdanlGVENLRGSGMIAGEASLAYEKTVTISMVTCRALGIGAY 1931
Cdd:COG4799 134 ------------------------------------------GVESFAGYGRIFYRNARSSGGIPQISVIMGPCAAGGAY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1932 LVRLGQRVIQVE-NSHIILTGAGALNKVLGREVytSNNQLGGVQiMHT--NGVSHVTVPDDFEGVCTILEWLSFIPKDNR 2008
Cdd:COG4799 172 SPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvSGVADYLAEDEEEALALARRLLSYLPSNNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 2009 SPVPITTPSDP--IDREI-EFTPT--KAPYDPRWMLAGrphptlkgtwqsgFFDHGSFKEIMAPWAQTVVTGRARLGGIP 2083
Cdd:COG4799 249 EDPPRAEPAPParDPEELyGIVPEdpRKPYDMREVIAR-------------LVDGGSFFEFKPLYGPNIVTGFARIDGRP 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157042798 2084 VGVIAvetrtvevavpADPANLdseakiiqqAGqVWFPDSAYKTAQVIRDFNKERLPLMIFANWRGF 2150
Cdd:COG4799 316 VGIVA-----------NQPMVL---------AG-VLDIDAADKAARFIRLCDAFNIPLVFLVDVPGF 361
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
885-951 |
1.53e-16 |
|
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: 76.10 E-value: 1.53e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157042798 885 TVLRSPSAGKLM-----QYTVEDGDHVEAGSSYAEMEVMKMIMTLNVQESGRVKYIKRP-GVILEAGCVVARL 951
Cdd:pfam00364 1 TEIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
886-951 |
6.45e-15 |
|
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: 71.29 E-value: 6.45e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157042798 886 VLRSPSAGKLMQYTVEDGDHVEAGSSYAEMEVMKMIMTLNVQESGRVKYIK-RPGVILEAGCVVARL 951
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
304-603 |
9.51e-11 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 66.11 E-value: 9.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 304 ADQYVPVPGgPNNNNYANVELIIDIAKRIPVQAVWA---GWGHA-SEN-PKLPELlckheIAFLGPPSEAMWALGDKIAS 378
Cdd:COG3919 48 VDEVVVVPD-PGDDPEAFVDALLELAERHGPDVLIPtgdEYVELlSRHrDELEEH-----YRLPYPDADLLDRLLDKERF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 379 TIVAQTLQIPtlpwsgsgltvewtedsrhqgkcisVPEDVYeqgcVKDVDEGLQAAEKIGFPLMIKASEG--------GG 450
Cdd:COG3919 122 YELAEELGVP-------------------------VPKTVV----LDSADDLDALAEDLGFPVVVKPADSvgydelsfPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 451 GKGIRKAESAEDFPMLFRQ---------VQSEIPGSpiflmklaqNARHLEVQVLADQYGNAVSLFGrdcsiqrrHQKII 521
Cdd:COG3919 173 KKKVFYVDDREELLALLRRiaaagyeliVQEYIPGD---------DGEMRGLTAYVDRDGEVVATFT--------GRKLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 522 EeAPATIAAPAVFEF------MEQCAVLLAKmVGYVSAGTVEYLY-SQDGSFHFLELNPRLQVEHPCTEmIADVNLPAAQ 594
Cdd:COG3919 236 H-YPPAGGNSAARESvddpelEEAARRLLEA-LGYHGFANVEFKRdPRDGEYKLIEINPRFWRSLYLAT-AAGVNFPYLL 312
|
....*....
gi 157042798 595 LQIAMGVPL 603
Cdd:COG3919 313 YDDAVGRPL 321
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
422-574 |
9.47e-07 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 54.40 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 422 GCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIPGSPIFLMKLAQNARHLEVQVLADQYG 501
Cdd:PLN02735 721 GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEG 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 502 NAVSlfgrdCSIQRRhqkiIEEA-----------PATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGSFHFLE 570
Cdd:PLN02735 801 NVVI-----GGIMEH----IEQAgvhsgdsacslPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIE 871
|
....
gi 157042798 571 LNPR 574
Cdd:PLN02735 872 ANPR 875
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
892-952 |
9.80e-06 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 45.55 E-value: 9.80e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157042798 892 AGKLMQYTVEDGDHVEAGSSYAEMEVMKMIMTLNVQESGRVKYIKRP-GVILEAGCVVARLE 952
Cdd:PRK08225 9 AGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQeGDFVNEGDVLLEIE 70
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
426-574 |
3.22e-05 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 48.34 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 426 DVDEGLqAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQ-----VQSEIPGSPIflmklaqnarhlEVQVLADQY 500
Cdd:PRK12767 137 DFKAAL-AKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYvpnliIQEFIEGQEY------------TVDVLCDLN 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157042798 501 GNAVSLFGRdcsiqRRHQKIIEEA--PATIAAPAVFEFMEQCAVLLakmvGYVSAGTVEYLYSqDGSFHFLELNPR 574
Cdd:PRK12767 204 GEVISIVPR-----KRIEVRAGETskGVTVKDPELFKLAERLAEAL----GARGPLNIQCFVT-DGEPYLFEINPR 269
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
424-603 |
4.52e-05 |
|
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: 48.84 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 424 VKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIPGSPIFLMKLAQNARHLEVQVLADqyGNA 503
Cdd:TIGR01369 690 ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 504 VSLFGrdcsIQrRHqkiIEEA-----------PATIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSqDGSFHFLELN 572
Cdd:TIGR01369 768 VLIPG----IM-EH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVN 838
|
170 180 190
....*....|....*....|....*....|.
gi 157042798 573 PRLQVEHPCTEMIADVNLPAAQLQIAMGVPL 603
Cdd:TIGR01369 839 PRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
416-626 |
5.97e-05 |
|
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: 48.46 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 416 EDVYEQGCVKDVDEGLQAAEKIGFPLMIKASE--GGGGKGIrkAESAEDFPMLFRQVQSEIPGSPIFLMKLAQNARHLEV 493
Cdd:TIGR01369 140 EPVPESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSASPINQVLVEKSLAGWKEIEY 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 494 QVLADQYGNAVSLfgrdCSIQRRHQKIIEEAPATIAAPAV------FEFMEQCAVLLAKMVGYVSAGTVEY-LYSQDGSF 566
Cdd:TIGR01369 218 EVMRDSNDNCITV----CNMENFDPMGVHTGDSIVVAPSQtltdkeYQMLRDASIKIIRELGIEGGCNVQFaLNPDSGRY 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 567 HFLELNPRLQ---------VEHPctemIADVnlpAAQLqiAMGVPLHRLK-DIRllygespwGVTPIPFE 626
Cdd:TIGR01369 294 YVIEVNPRVSrssalaskaTGYP----IAKV---AAKL--AVGYTLDELKnPVT--------GTTPASFE 346
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
424-574 |
5.99e-05 |
|
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: 48.34 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 424 VKDVDEGLQAAEKIGFPLMIKASE--GGGGKGIrkAESAEDFPMLFRQVQSEIPGSPIFLMKLAQNARHLEVQVLADQYG 501
Cdd:COG0458 135 ATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGED 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 502 NAVSLfgrdCSIQrrHqkiIEEA-----PATIAAPA------VFEFMEQCAVLLAKMVGYVSAGTVEYLYsQDGSFHFLE 570
Cdd:COG0458 213 NVIIV----GIME--H---IEPAgvhsgDSICVAPPqtlsdkEYQRLRDATLKIARALGVVGLCNIQFAV-DDGRVYVIE 282
|
....
gi 157042798 571 LNPR 574
Cdd:COG0458 283 VNPR 286
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
416-504 |
7.37e-05 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 48.43 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 416 EDVYEQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGIRKAESAEDFPMLFRQVQSEIPGSPIFLMKLAQNARHLEVQV 495
Cdd:PRK12815 141 EPVPESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEV 220
|
....*....
gi 157042798 496 LADQYGNAV 504
Cdd:PRK12815 221 MRDRNGNCI 229
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
439-601 |
7.90e-05 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 47.61 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 439 FPLMIKASEGGGGKGIRKAESAE--DFPMLFrqvQSEIPGSPIflmklaqnarhlEVQVLADqygnavslfGRDCSIQRR 516
Cdd:COG2232 139 GPWLVKPIGGAGGWHIRPADSEAppAPGRYF---QRYVEGTPA------------SVLFLAD---------GSDARVLGF 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 517 HQKIIEEAPA-----------TIAAPAVFEFMEQCAVLLAKMVGYVSAGTVEYLYSQDGsFHFLELNPRLQVEHPCTEMI 585
Cdd:COG2232 195 NRQLIGPAGErpfryggnigpLALPPALAEEMRAIAEALVAALGLVGLNGVDFILDGDG-PYVLEVNPRPQASLDLYEDA 273
|
170
....*....|....*.
gi 157042798 586 ADVNLPAAQLQIAMGV 601
Cdd:COG2232 274 TGGNLFDAHLRACRGE 289
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1907-2169 |
1.68e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 46.72 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1907 EASLAYEKTVTISMV--TCRAlGiGAYLVRLG-QRVIQVENSHIILTGAGALNKVLGREVytSNNQLGGVQImH--TNGV 1981
Cdd:PLN02820 198 QARMSSAGIPQIALVlgSCTA-G-GAYVPAMAdESVIVKGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-HckVSGV 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 1982 SHVTVPDDFEGVC---TILEWLSFIPKDNRSPV------PITTPSDPID--REIEFTPTKAPYDPRWMLAGrphptlkgt 2050
Cdd:PLN02820 273 SDHFAQDELHALAigrNIVKNLHLAAKQGMENTlgsknpEYKEPLYDVKelRGIVPADHKQSFDVRSVIAR--------- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157042798 2051 wqsgFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAvetrtvevavpadpanldseakiiqqAGQVWFPDSAYKTAQV 2130
Cdd:PLN02820 344 ----IVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALKGAHF 393
|
250 260 270
....*....|....*....|....*....|....*....
gi 157042798 2131 IRDFNKERLPLMIFANWRGFSGGMKDMYEQMLKFGAYIV 2169
Cdd:PLN02820 394 IELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMV 432
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
885-952 |
9.62e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 40.00 E-value: 9.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157042798 885 TVLRSPSAGKlmQYTVEDGDHVEAGSSYAEMEVMKMIMTLNVQESGRV-KYIKRPGVILEAGCVVARLE 952
Cdd:PRK07051 13 TFYRRPSPDA--PPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVvEFLVEDGEPVEAGQVLARIE 79
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
889-945 |
9.69e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 44.74 E-value: 9.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 157042798 889 SPSAGKLMQYTVEDGDHVEAGSSYAEMEVMKMIMTLNVQESGRVKYI-KRPGVILEAG 945
Cdd:PRK12999 1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVlVKAGDQVEAG 1138
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
900-935 |
3.26e-03 |
|
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: 38.19 E-value: 3.26e-03
10 20 30
....*....|....*....|....*....|....*.
gi 157042798 900 VEDGDHVEAGSSYAEMEVMKMIMTLNVQESGRVKYI 935
Cdd:cd06663 21 KKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKV 56
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
416-463 |
4.80e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 42.39 E-value: 4.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 157042798 416 EDVYEQGCVKDVDEGLQAAEKIGFPLMIKAS--EGGGGKGIrkAESAEDF 463
Cdd:PRK05294 141 LPVPRSGIAHSMEEALEVAEEIGYPVIIRPSftLGGTGGGI--AYNEEEL 188
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
411-454 |
6.44e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 41.68 E-value: 6.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 157042798 411 CISVPEdvyeQGCVKDVDEGLQAAEKIGFPLMIKASEGGGGKGI 454
Cdd:PRK14016 226 GVPVPE----GRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGV 265
|
|
| |
