|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
876-1602 |
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: 1004.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 876 ELDDPTKVKPAQPFTGGLPAQQTLPITGEKQHQVLRNVLDNLTNVMNGYCLpepyfSSKVKEWVAQLMKTLRDPSLPLLE 955
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 956 LQEIMTSISGRIPLSVEKSIRKVMAQYASNitsvLCRFPSQQIANVLDTHAATLQRKAEREVFFMNTQSVVQLVQRYRSG 1035
Cdd:pfam08326 76 WQEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1036 IRGYMKAVVLDLLRRYLQVEMQFQQA--HYDKCVISLREQYKPDMTPVLESIFSHAQVAKKNLLVTMLIDQLCGR---EP 1110
Cdd:pfam08326 152 LKGHEYSVFASLLEEYYDVEKLFSGGnvREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1111 TLTDELTAILNELTQLSKTEHSKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------EFCPENLKKLIL 1182
Cdd:pfam08326 232 NVAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELID 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1183 SETTIFDVLPFFFYHDNQVVRMAALEVYVRRGYIAYELNSLQHRQLSDGTCLVEFQFMLPFSHPNRMSVPISISNPDLAR 1262
Cdd:pfam08326 312 SKYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSPP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1263 H------STELFMDSGFSPLSQRMGAMVAFNKFEDFTRNFDEVISCFAEPPLESSlfsearatiygeedTKNVREEPIHI 1336
Cdd:pfam08326 392 FkriasvSDLSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESG--------------ESNSSDEPINV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1337 LNIALRRADHAE-DEKLVPIFRAFAQSKKNILVDCGLRRITFLIAQQ-REFPKFFTFRARDEFAEDRIYRHLEPALAFQL 1414
Cdd:pfam08326 458 LNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKdGQYPKYFTFRGPDNYEEDPIIRHIEPALAFQL 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1415 ELSRMRNFDLTAIPCANHKMHLYLGAAKVqagtEATDYRFFIRAIVRHSDLITKEASFEYLQNEGERLLLEAMDELEVAf 1494
Cdd:pfam08326 538 ELGRLSNFDIKPVPTENRQIHLYEAVGKE----NPTDKRFFVRAIIRPGRLRDDIPTAEYLISEAERLLNDILDALEVA- 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1495 NNTSVRTDCNHIFLNFVPTVVMDPSKIEESVRAMVMRYGSRLWKLRVLQAEVKINIRLTPTATAIPIRLSLTNESGYYLD 1574
Cdd:pfam08326 613 SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGPPIPLRLVITNVSGYVVK 692
|
730 740
....*....|....*....|....*...
gi 2024460499 1575 ISLYKEVRDPStGNIMFQSYGdKQGAQH 1602
Cdd:pfam08326 693 VELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1694-2253 |
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: 565.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1694 PEYPKGRDIMLICNDITHMIGSFGPEEDLVFLRASELARAEgIPRVYIAANSGARIGFADEIKHMFQVAWVDPEDPYKGF 1773
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1774 KylyLTPQDYTRISAmnsvhcehveegGESRYVLLDIIGKDHGFGVENLRAAGTIAGESSRAYDEIVTISMVTCRAIGIG 1853
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1854 AYLVRLGQRVIQVEN-SHIILTGVTALNKVLGrEVYTSNNQLGGVQVMHNNGISHITVPDDFEGVYTILQWLSYMPKD-- 1930
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPap 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1931 -NRSPVPVIAISDPIERE---IDFVPS--KVPYDPRWMLAGRphptlkgtwqsgfFDQGSFLEIMKPWAQTVVVGRARLG 2004
Cdd:pfam01039 224 nNREPVPIVPTKDPPDRDaplVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 2005 GLPVGVIAVETRtvevtipadpanpdseakiiQQAGqVWFPDSAFKTAQAIRDFNREHLPLMIFANWRGFSSGMKDMYDQ 2084
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 2085 MLKFGAFIVDSLRDFKQPVLVYIPPhaELRGGSWVVMDPTINPLYVeLYADKESrsvpalpnfppRGGILEPGGTVEIKF 2164
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTA-----------RIAVMGPEGAVEIKF 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 2165 RKKDLVKTMRRIDkvyaklveqlgtpelsegQRKELEKQLKAREELLLPIYYQVAVHFADLHDTPGRMQEKGVITDILEW 2244
Cdd:pfam01039 416 RKEKAAAEMRGKD------------------LAATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALW 477
|
....*....
gi 2024460499 2245 KNARsFLYW 2253
Cdd:pfam01039 478 TKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
174-684 |
1.37e-115 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 375.89 E-value: 1.37e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 174 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVVMVTPEDlkANAEYIRMADHYVPVPGGANNNNYANVELIVDIS 253
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 254 KRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPWSgsglvaqwseedqkgq 333
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 334 qmisipletygQGCVKDVEEGLEVAKRIGYPLMIKAAeggggkgIRKVEAAEEFGACFRQVQAEAP---GSP-IFLMKLA 409
Cdd:COG4770 135 -----------DGPVQDAEEALAIAEEIGYPVLIKASaggggkgMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 410 QHARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLYSEDGS 489
Cdd:COG4770 204 ERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 490 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPLHRIKDirmlygespwgdtpicfnspanPPVPRGHVIAARITS 569
Cdd:COG4770 284 FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPFTQE----------------------DIKLRGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 570 ENPEEGFKPSSGTVQELNFRSSknvwgyFSVAAAGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRGd 643
Cdd:COG4770 342 EDPARGFLPSPGTITRLRPPGG------PGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG- 414
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2024460499 644 FRTTVEYLIKLLETESFQSNEIDTGWLDHLIAEKVQAEKPD 684
Cdd:COG4770 415 VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
174-680 |
4.39e-99 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 327.53 E-value: 4.39e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 174 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIRMADHYVPVPGGANNNNYANVELIVDIS 253
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 254 KRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPwsGSglvaqwseedqkgq 333
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 334 qmisipletygQGCVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEAP---GSP-IFLMKLA 409
Cdd:PRK08591 135 -----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 410 QHARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLYSEDGS 489
Cdd:PRK08591 204 ENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 490 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPLH-RIKDIRMlygespwgdtpicfnspanppvpRGHVIAARIT 568
Cdd:PRK08591 284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 569 SENPEEGFKPSSGTVQelnfrssknvwGYFsvaAAGGLH--------------EFADSQFGHCFSWGENREEAISNMVVA 634
Cdd:PRK08591 341 AEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2024460499 635 LKELSIRGdFRTTVEYLIKLLETESFQSNEIDTGWLDHLIAEKVQA 680
Cdd:PRK08591 407 LSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
176-671 |
5.80e-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: 284.03 E-value: 5.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 176 KVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEY-IRMADHYVPVpggannNNYANVEL 248
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 249 IVDISKRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPWSgsglvaqwsee 328
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 329 dqkgqqmisipletygQGCVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEAPGS----PIF 404
Cdd:TIGR01235 135 ----------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 405 LMKLAQHARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLY 484
Cdd:TIGR01235 199 VEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 485 SEDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPLHRIK-------DIRMlygespwgdtpicfnspanppv 557
Cdd:TIGR01235 279 DNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQlgvpnqeDIRT---------------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 558 pRGHVIAARITSENPEEGFKPSSGTVQElnFRSSknvwGYFSVAAAGG-------LHEFADSQFGHCFSWGENREEAISN 630
Cdd:TIGR01235 337 -NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAK 409
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2024460499 631 MVVALKELSIRGdFRTTVEYLIKLLETESFQSNEIDTGWLD 671
Cdd:TIGR01235 410 MDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
336-527 |
2.00e-47 |
|
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: 169.41 E-value: 2.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 336 ISIPLETYGQGCVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEAPGSP----IFLMKLAQH 411
Cdd:pfam02786 12 AGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 412 ARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLY-SEDGSF 490
Cdd:pfam02786 92 PKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALdPFSGEY 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024460499 491 HFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPL 527
Cdd:pfam02786 172 YFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
565-671 |
4.19e-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: 124.45 E-value: 4.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 565 ARITSENPEEGFKPSSGTVQELNFRSSKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 642
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 2024460499 643 dFRTTVEYLIKLLETESFQSNEIDTGWLD 671
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1699-2074 |
3.01e-24 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 109.35 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1699 GRDIMLICNDITHMIGSFGPEEDLVFLRASELARAEGIPRVYIAANSGARIgfadeikhmfqvawvdPEdpykgfkylyl 1778
Cdd:COG4799 81 GRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARL----------------QE----------- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1779 tpqdytrisamnsvhcehveeggesryvlldiigkdhgfGVENLRAAGTIAGESSRAYDEIVTISMVTCRAIGIGAYLVR 1858
Cdd:COG4799 134 ---------------------------------------GVESFAGYGRIFYRNARSSGGIPQISVIMGPCAAGGAYSPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1859 LGQRVIQVE-NSHIILTG---VTAlnkVLGREVytSNNQLGGVQvMHN--NGISHITVPDDFEGVYTILQWLSYMPKDNR 1932
Cdd:COG4799 175 LSDFVIMVKgTSQMFLGGppvVKA---ATGEEV--TAEELGGAD-VHArvSGVADYLAEDEEEALALARRLLSYLPSNNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1933 SPVPVIAISDP--IEREI-DFVP--SKVPYDPRWMLAGrphptlkgtwqsgFFDQGSFLEIMKPWAQTVVVGRARLGGLP 2007
Cdd:COG4799 249 EDPPRAEPAPParDPEELyGIVPedPRKPYDMREVIAR-------------LVDGGSFFEFKPLYGPNIVTGFARIDGRP 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024460499 2008 VGVIAvetrtvevtipadpANPdseakiIQQAGqVWFPDSAFKTAQAIRDFNREHLPLMIFANWRGF 2074
Cdd:COG4799 316 VGIVA--------------NQP------MVLAG-VLDIDAADKAARFIRLCDAFNIPLVFLVDVPGF 361
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
809-875 |
2.69e-12 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 64.16 E-value: 2.69e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024460499 809 TVLRSPSAGKL-----LQYTVDDGGHVAEGSVFAEIEVMKIIMTLTVEEAGRVHYVKRP-GALLEAGCVIAQL 875
Cdd:pfam00364 1 TEIKSPMIGESvregvVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
810-875 |
3.64e-12 |
|
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: 63.59 E-value: 3.64e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024460499 810 VLRSPSAGKLLQYTVDDGGHVAEGSVFAEIEVMKIIMTLTVEEAGRVHYVK-RPGALLEAGCVIAQL 875
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
809-876 |
1.07e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 42.69 E-value: 1.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024460499 809 TVLRSPSAGKllQYTVDDGGHVAEGSVFAEIEVMKIIMTLTVEEAGRV-HYVKRPGALLEAGCVIAQLE 876
Cdd:PRK07051 13 TFYRRPSPDA--PPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVvEFLVEDGEPVEAGQVLARIE 79
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
876-1602 |
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: 1004.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 876 ELDDPTKVKPAQPFTGGLPAQQTLPITGEKQHQVLRNVLDNLTNVMNGYCLpepyfSSKVKEWVAQLMKTLRDPSLPLLE 955
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 956 LQEIMTSISGRIPLSVEKSIRKVMAQYASNitsvLCRFPSQQIANVLDTHAATLQRKAEREVFFMNTQSVVQLVQRYRSG 1035
Cdd:pfam08326 76 WQEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1036 IRGYMKAVVLDLLRRYLQVEMQFQQA--HYDKCVISLREQYKPDMTPVLESIFSHAQVAKKNLLVTMLIDQLCGR---EP 1110
Cdd:pfam08326 152 LKGHEYSVFASLLEEYYDVEKLFSGGnvREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1111 TLTDELTAILNELTQLSKTEHSKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------EFCPENLKKLIL 1182
Cdd:pfam08326 232 NVAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELID 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1183 SETTIFDVLPFFFYHDNQVVRMAALEVYVRRGYIAYELNSLQHRQLSDGTCLVEFQFMLPFSHPNRMSVPISISNPDLAR 1262
Cdd:pfam08326 312 SKYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSPP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1263 H------STELFMDSGFSPLSQRMGAMVAFNKFEDFTRNFDEVISCFAEPPLESSlfsearatiygeedTKNVREEPIHI 1336
Cdd:pfam08326 392 FkriasvSDLSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESG--------------ESNSSDEPINV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1337 LNIALRRADHAE-DEKLVPIFRAFAQSKKNILVDCGLRRITFLIAQQ-REFPKFFTFRARDEFAEDRIYRHLEPALAFQL 1414
Cdd:pfam08326 458 LNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKdGQYPKYFTFRGPDNYEEDPIIRHIEPALAFQL 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1415 ELSRMRNFDLTAIPCANHKMHLYLGAAKVqagtEATDYRFFIRAIVRHSDLITKEASFEYLQNEGERLLLEAMDELEVAf 1494
Cdd:pfam08326 538 ELGRLSNFDIKPVPTENRQIHLYEAVGKE----NPTDKRFFVRAIIRPGRLRDDIPTAEYLISEAERLLNDILDALEVA- 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1495 NNTSVRTDCNHIFLNFVPTVVMDPSKIEESVRAMVMRYGSRLWKLRVLQAEVKINIRLTPTATAIPIRLSLTNESGYYLD 1574
Cdd:pfam08326 613 SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGPPIPLRLVITNVSGYVVK 692
|
730 740
....*....|....*....|....*...
gi 2024460499 1575 ISLYKEVRDPStGNIMFQSYGdKQGAQH 1602
Cdd:pfam08326 693 VELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1694-2253 |
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: 565.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1694 PEYPKGRDIMLICNDITHMIGSFGPEEDLVFLRASELARAEgIPRVYIAANSGARIGFADEIKHMFQVAWVDPEDPYKGF 1773
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1774 KylyLTPQDYTRISAmnsvhcehveegGESRYVLLDIIGKDHGFGVENLRAAGTIAGESSRAYDEIVTISMVTCRAIGIG 1853
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1854 AYLVRLGQRVIQVEN-SHIILTGVTALNKVLGrEVYTSNNQLGGVQVMHNNGISHITVPDDFEGVYTILQWLSYMPKD-- 1930
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPap 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1931 -NRSPVPVIAISDPIERE---IDFVPS--KVPYDPRWMLAGRphptlkgtwqsgfFDQGSFLEIMKPWAQTVVVGRARLG 2004
Cdd:pfam01039 224 nNREPVPIVPTKDPPDRDaplVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 2005 GLPVGVIAVETRtvevtipadpanpdseakiiQQAGqVWFPDSAFKTAQAIRDFNREHLPLMIFANWRGFSSGMKDMYDQ 2084
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 2085 MLKFGAFIVDSLRDFKQPVLVYIPPhaELRGGSWVVMDPTINPLYVeLYADKESrsvpalpnfppRGGILEPGGTVEIKF 2164
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTA-----------RIAVMGPEGAVEIKF 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 2165 RKKDLVKTMRRIDkvyaklveqlgtpelsegQRKELEKQLKAREELLLPIYYQVAVHFADLHDTPGRMQEKGVITDILEW 2244
Cdd:pfam01039 416 RKEKAAAEMRGKD------------------LAATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALW 477
|
....*....
gi 2024460499 2245 KNARsFLYW 2253
Cdd:pfam01039 478 TKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
174-684 |
1.37e-115 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 375.89 E-value: 1.37e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 174 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVVMVTPEDlkANAEYIRMADHYVPVPGGANNNNYANVELIVDIS 253
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 254 KRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPWSgsglvaqwseedqkgq 333
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 334 qmisipletygQGCVKDVEEGLEVAKRIGYPLMIKAAeggggkgIRKVEAAEEFGACFRQVQAEAP---GSP-IFLMKLA 409
Cdd:COG4770 135 -----------DGPVQDAEEALAIAEEIGYPVLIKASaggggkgMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 410 QHARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLYSEDGS 489
Cdd:COG4770 204 ERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 490 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPLHRIKDirmlygespwgdtpicfnspanPPVPRGHVIAARITS 569
Cdd:COG4770 284 FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPFTQE----------------------DIKLRGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 570 ENPEEGFKPSSGTVQELNFRSSknvwgyFSVAAAGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRGd 643
Cdd:COG4770 342 EDPARGFLPSPGTITRLRPPGG------PGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG- 414
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2024460499 644 FRTTVEYLIKLLETESFQSNEIDTGWLDHLIAEKVQAEKPD 684
Cdd:COG4770 415 VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
174-680 |
4.39e-99 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 327.53 E-value: 4.39e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 174 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIRMADHYVPVPGGANNNNYANVELIVDIS 253
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 254 KRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPwsGSglvaqwseedqkgq 333
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 334 qmisipletygQGCVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEAP---GSP-IFLMKLA 409
Cdd:PRK08591 135 -----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 410 QHARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLYSEDGS 489
Cdd:PRK08591 204 ENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 490 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPLH-RIKDIRMlygespwgdtpicfnspanppvpRGHVIAARIT 568
Cdd:PRK08591 284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 569 SENPEEGFKPSSGTVQelnfrssknvwGYFsvaAAGGLH--------------EFADSQFGHCFSWGENREEAISNMVVA 634
Cdd:PRK08591 341 AEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2024460499 635 LKELSIRGdFRTTVEYLIKLLETESFQSNEIDTGWLDHLIAEKVQA 680
Cdd:PRK08591 407 LSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
174-672 |
3.26e-92 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 307.72 E-value: 3.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 174 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVVMVTPEDlkANAEYIRMADHYVPVPGGANNNNYANVELIVDIS 253
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLG---------IRTVAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 254 KRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPwsgsglvaqwseedqkGq 333
Cdd:PRK06111 71 KKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVP----------------G- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 334 qmISIPLEtygqgcvkDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEAP---GSP-IFLMKLA 409
Cdd:PRK06111 134 --ITTNLE--------DAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAAnffGNGeMYIEKYI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 410 QHARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLYSEDGS 489
Cdd:PRK06111 204 EDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 490 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPL-HRIKDIRMlygespwgdtpicfnspanppvpRGHVIAARIT 568
Cdd:PRK06111 284 FYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR-----------------------SGHAIEVRIY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 569 SENPEEgFKPSSGTVQELNFRSSKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTV 648
Cdd:PRK06111 341 AEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEG-IKTNI 418
|
490 500
....*....|....*....|....
gi 2024460499 649 EYLIKLLETESFQSNEIDTGWLDH 672
Cdd:PRK06111 419 PLLLQVLEDPVFKAGGYTTGFLTK 442
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
172-671 |
3.91e-91 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 324.01 E-value: 3.91e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 172 RVIEKVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEY--------IRMadhYVpvpgg 237
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAA---------TELGIRTVAIYSEEDklslhrFKADEAYligegkhpVRA---YL----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 238 annnnyaNVELIVDISKRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPWS 317
Cdd:PRK12999 66 -------DIDEIIRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 318 GSGlvaqwseedqkgqqmisipletygqgcVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAE 397
Cdd:PRK12999 139 EGP---------------------------IDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKRE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 398 AP---GSP-IFLMKLAQHARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPitiaAPAV-IEVMEK-C--AVRLA 469
Cdd:PRK12999 192 AKaafGNDeVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAP----APGLsEELRERiCeaAVKLA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 470 QMVGYVSTGTVEYLYSEDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPLHrikdirmlygespwgDTPICF 549
Cdd:PRK12999 268 RAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATLH---------------DLEIGI 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 550 NSPANPPvPRGHVIAARITSENPEEGFKPSSGTVQElnFRSSknvwGYFSV------AAAGGlhEFA---DSQFGHCFSW 620
Cdd:PRK12999 333 PSQEDIR-LRGYAIQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVrldggnAFAGA--EITpyyDSLLVKLTAW 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2024460499 621 GENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQSNEIDTGWLD 671
Cdd:PRK12999 404 GRTFEQAVARMRRALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFID 453
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
175-679 |
1.17e-89 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 302.29 E-value: 1.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 175 EKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIRMADHYVPVPGGANNNNYANVELIVDISK 254
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACR---------ELGIKTVAVYSEAD--KNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 255 RIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPWSgsglvaqwseedqkgqq 334
Cdd:PRK08654 72 KAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGT----------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 335 misipletygQGCVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACF---RQVQAEAPGSP-IFLMKLAQ 410
Cdd:PRK08654 135 ----------EEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIestQSIAQSAFGDStVFIEKYLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 411 HARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLYSeDGSF 490
Cdd:PRK08654 205 KPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 491 HFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPL-HRIKDIRMlygespwgdtpicfnspanppvpRGHVIAARITS 569
Cdd:PRK08654 284 YFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELsFKQEDITI-----------------------RGHAIECRINA 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 570 ENPEEGFKPSSGTVQelNFRSSknvwGYFSVAAAGGLH------EFADSQFGHCFSWGENREEAISNMVVALKELSIRGd 643
Cdd:PRK08654 341 EDPLNDFAPSPGKIK--RYRSP----GGPGVRVDSGVHmgyeipPYYDSMISKLIVWGRTREEAIARMRRALYEYVIVG- 413
|
490 500 510
....*....|....*....|....*....|....*...
gi 2024460499 644 FRTTVEYLIKLLETESFQSNEIDTGWLD--HLIAEKVQ 679
Cdd:PRK08654 414 VKTNIPFHKAVMENENFVRGNLHTHFIEeeTTILEEMK 451
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
171-671 |
2.93e-87 |
|
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: 312.40 E-value: 2.93e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 171 TRVIEKVLIANNG-IAavkcmrsIR--RWAYEMfrnerAIRFVVMVTPED------LKANAEY-IRMADHyvPVpggann 240
Cdd:COG1038 1 MKKIKKVLVANRGeIA-------IRvfRAATEL-----GIRTVAIYSEEDryslhrFKADEAYlIGEGKG--PV------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 241 NNYANVELIVDISKRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPwsGSG 320
Cdd:COG1038 61 DAYLDIEEIIRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP--GTE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 321 lvaqwseedqkgqqmisipletygqGCVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEAP- 399
Cdd:COG1038 139 -------------------------GPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKa 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 400 --GSP-IFLMKLAQHARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPitiaAPAV-IEVMEK-C--AVRLAQMV 472
Cdd:COG1038 194 afGDDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAP----APNLdEELREAiCeaAVKLAKAV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 473 GYVSTGTVEYLYSEDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPLH----RIK---DIRMlygespwgdt 545
Cdd:COG1038 270 GYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSLDdpeiGIPsqeDIRL---------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 546 picfnspanppvpRGHVIAARITSENPEEGFKPSSGTVQElnFRSSknvwGYFSV------AAAGG-LHEFADSQFGHCF 618
Cdd:COG1038 340 -------------NGYAIQCRITTEDPANNFMPDTGRITA--YRSA----GGFGIrldggnAYTGAvITPYYDSLLVKVT 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2024460499 619 SWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQSNEIDTGWLD 671
Cdd:COG1038 401 AWGRTFEEAIRKMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFID 452
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
174-680 |
1.84e-82 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 280.10 E-value: 1.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 174 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDLKANAeyIRMADHYVPVPGGANNNNYANVELIVDIS 253
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAAR---------ELGMRTVAACSDADRDSLA--ARMADEAVHIGPSHAAKSYLNPAAILAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 254 KRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPWSgsglvaqwseedqkgq 333
Cdd:PRK12833 74 RQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGS---------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 334 qmisipletygQGCVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEAP---GSP-IFLMKLA 409
Cdd:PRK12833 138 -----------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQaafGDGgVYLERFI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 410 QHARHLEVQVLADEYgNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLY-SEDG 488
Cdd:PRK12833 207 ARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFdDARG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 489 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPLH-RIKDIRMlygespwgdtpicfnspanppvpRGHVIAARI 567
Cdd:PRK12833 286 EFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRfAQGDIAL-----------------------RGAALECRI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 568 TSENPEEGFKPSSGTVQELNF------RSSKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIR 641
Cdd:PRK12833 343 NAEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYPGYRVPP------FYDSLLAKLIVHGEDRAAALARAARALRELRID 416
|
490 500 510
....*....|....*....|....*....|....*....
gi 2024460499 642 GdFRTTVEYLIKLLETESFQSNEIDTGWLDHLIAEKVQA 680
Cdd:PRK12833 417 G-MKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAA 454
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
174-670 |
1.83e-81 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 276.59 E-value: 1.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 174 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIRMADHYVPVPGGANNNNYANVELIVDIS 253
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACR---------EMGIETVAVYSEAD--KDALHVQLADEAVCIGPASSKDSYLNIQNIISAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 254 KRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPWSgsglvaqwseedqkgq 333
Cdd:PRK05586 71 VLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 334 qmisipletygQGCVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEAPGS----PIFLMKLA 409
Cdd:PRK05586 135 -----------EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 410 QHARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLYSEDGS 489
Cdd:PRK05586 204 ENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 490 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPLH-RIKDIRMlygespwgdtpicfnspanppvpRGHVIAARIT 568
Cdd:PRK05586 284 FYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSiKQEDIKI-----------------------NGHSIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 569 SENPEEGFKPSSGTVQELNFRSSKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTV 648
Cdd:PRK05586 341 AEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEG-VNTNI 419
|
490 500
....*....|....*....|..
gi 2024460499 649 EYLIKLLETESFQSNEIDTGWL 670
Cdd:PRK05586 420 DFQFIILEDEEFIKGTYDTSFI 441
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
174-672 |
5.05e-80 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 272.39 E-value: 5.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 174 IEKVLIANNGIAAVKCMRSIRrwayEMfrNERAIrfVVMVTPEDlkaNAEYIRMADHYVPVPGGANNNNYANVELIVDIS 253
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQ----EM--GKEAI--AIYSTADK---DALYLKYADAKICIGGAKSSESYLNIPAIISAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 254 KRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPWSgsglvaqwseedqkgq 333
Cdd:PRK08462 73 EIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGS---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 334 qmisipletygQGCVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEAPGS----PIFLMKLA 409
Cdd:PRK08462 137 -----------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAfgdgTMYMEKFI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 410 QHARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLYSEDGS 489
Cdd:PRK08462 206 NNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 490 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPLHRIKDIRMlygespwgdtpicfnspanppvpRGHVIAARITS 569
Cdd:PRK08462 286 FYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKL-----------------------KGHAIECRITA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 570 ENPEEgFKPSSGTVQEL------NFRSSKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGd 643
Cdd:PRK08462 343 EDPKK-FYPSPGKITKWiapggrNVRMDSHAYAGYVVPP------YYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEG- 414
|
490 500
....*....|....*....|....*....
gi 2024460499 644 FRTTVEYLIKLLETESFQSNEIDTGWLDH 672
Cdd:PRK08462 415 IKTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
176-671 |
5.80e-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: 284.03 E-value: 5.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 176 KVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEY-IRMADHYVPVpggannNNYANVEL 248
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 249 IVDISKRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPWSgsglvaqwsee 328
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 329 dqkgqqmisipletygQGCVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEAPGS----PIF 404
Cdd:TIGR01235 135 ----------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 405 LMKLAQHARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLY 484
Cdd:TIGR01235 199 VEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 485 SEDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPLHRIK-------DIRMlygespwgdtpicfnspanppv 557
Cdd:TIGR01235 279 DNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQlgvpnqeDIRT---------------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 558 pRGHVIAARITSENPEEGFKPSSGTVQElnFRSSknvwGYFSVAAAGG-------LHEFADSQFGHCFSWGENREEAISN 630
Cdd:TIGR01235 337 -NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAK 409
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2024460499 631 MVVALKELSIRGdFRTTVEYLIKLLETESFQSNEIDTGWLD 671
Cdd:TIGR01235 410 MDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
173-693 |
6.69e-76 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 261.58 E-value: 6.69e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 173 VIEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIRMADHYVPVpGGANNNNYANVELIVDI 252
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACA---------EMGIRSVAIYSEAD--RHALHVKRADEAYSI-GADPLAGYLNPRRLVNL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 253 SKRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPWSgsglvaqwseedqkg 332
Cdd:PRK07178 69 AVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGS--------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 333 qqmisipletygQGCVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEAP---GSP-IFLMKL 408
Cdd:PRK07178 134 ------------EGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafGSAeVFLEKC 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 409 AQHARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLYSEDG 488
Cdd:PRK07178 202 IVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 489 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPL-HRIKDIRMlygespwgdtpicfnspanppvpRGHVIAARI 567
Cdd:PRK07178 282 EVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH-----------------------RGFALQFRI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 568 TSENPEEGFKPSSGTVQElnfrssknvwgYFSVAAAG---------GLH--EFADSQFGHCFSWGENREEAISNMVVALK 636
Cdd:PRK07178 339 NAEDPKNDFLPSFGKITR-----------YYAPGGPGvrtdtaiytGYTipPYYDSMCAKLIVWALTWEEALDRGRRALD 407
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024460499 637 ELSIRGdFRTTVEYLIKLLETESFQSNEIDTGWLD-HLIAEKVQAEKPDTMLGVVCGA 693
Cdd:PRK07178 408 DMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVEsHPELTNYSIKRKPEELAAAIAA 464
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
174-694 |
8.43e-64 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 226.62 E-value: 8.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 174 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIRMADHYVPVpGGANNNNYANVELIVDIS 253
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACR---------DLHIKSVAIYTEPD--RECLHVKIADEAYRI-GTDPIKGYLDVKRIVEIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 254 KRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDAMWALGDKVASTIVAQTVQIPTLPwsgsglvaqwseedqkGQ 333
Cdd:PRK08463 70 KACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVP----------------GT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 334 QmisiPLETYGQGCVKdveeglEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEE----FGACFRQVQAEAPGSPIFLMKLA 409
Cdd:PRK08463 134 E----KLNSESMEEIK------IFARKIGYPVILKASGGGGGRGIRVVHKEEDlenaFESCKREALAYFNNDEVFMEKYV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 410 QHARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLYSEDGS 489
Cdd:PRK08463 204 VNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 490 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGiplhRIKDIRMlygespwgdtpicfnspaNPPVPRGHVIAARITS 569
Cdd:PRK08463 284 FYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG----EILDLEQ------------------SDIKPRGFAIEARITA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 570 ENPEEGFKPSSGTVQEL------NFRSSKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGd 643
Cdd:PRK08463 342 ENVWKNFIPSPGKITEYypalgpSVRVDSHIYKDYTIPP------YYDSMLAKLIVKATSYDLAVNKLERALKEFVIDG- 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024460499 644 FRTTVEYLIKLLETESFQSNEIDTGWLD-HL--IAEKVQ---AEKPDTMLGVVCGAL 694
Cdd:PRK08463 415 IRTTIPFLIAITKTREFRRGYFDTSYIEtHMqeLLEKTEdrhQENKEEVIAAIAAAL 471
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
336-527 |
2.00e-47 |
|
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: 169.41 E-value: 2.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 336 ISIPLETYGQGCVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEAPGSP----IFLMKLAQH 411
Cdd:pfam02786 12 AGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 412 ARHLEVQVLADEYGNAISLFGRDCSIQRRHQKIIEEAPITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLY-SEDGSF 490
Cdd:pfam02786 92 PKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALdPFSGEY 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024460499 491 HFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGIPL 527
Cdd:pfam02786 172 YFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
174-292 |
8.16e-36 |
|
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: 132.22 E-value: 8.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 174 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVVMVTPEDlkANAEYIRMADHYVPVPGGANNNNYANVELIVDIS 253
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELG---------IRTVAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAA 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 2024460499 254 KRIPVQAVWAGWGHASENPKLPELLQKNGIAFLGPPSDA 292
Cdd:pfam00289 70 KETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
565-671 |
4.19e-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: 124.45 E-value: 4.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 565 ARITSENPEEGFKPSSGTVQELNFRSSKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 642
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 2024460499 643 dFRTTVEYLIKLLETESFQSNEIDTGWLD 671
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
246-526 |
9.19e-32 |
|
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: 126.53 E-value: 9.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 246 VELIVDISKRIPVQAVWAGWGHASEnpKLPELLQKNGIAflGPPSDAMWALGDKVASTIVAQTVQIPTlPWSGsglvaqw 325
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVE--TAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 326 seedqkgqqmisipletygqgCVKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEA----PGS 401
Cdd:COG0439 74 ---------------------LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 402 PIFLMKLAQHaRHLEVQVLADEyGNAISlfgrdCSIQRRHQK---IIE---EAPITIaAPAVIEVMEKCAVRLAQMVGYV 475
Cdd:COG0439 133 EVLVEEFLEG-REYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPL-PEELRAEIGELVARALRALGYR 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2024460499 476 -STGTVEYLYSEDGSFHFLELNPRLQVEH--PCTEMIADVNLPAAQLQIAMGIP 526
Cdd:COG0439 205 rGAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
565-672 |
5.50e-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: 115.67 E-value: 5.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 565 ARITSENPEEGFKPSSGTVQELNFRSSKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 644
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*...
gi 2024460499 645 RTTVEYLIKLLETESFQSNEIDTGWLDH 672
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1699-2074 |
3.01e-24 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 109.35 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1699 GRDIMLICNDITHMIGSFGPEEDLVFLRASELARAEGIPRVYIAANSGARIgfadeikhmfqvawvdPEdpykgfkylyl 1778
Cdd:COG4799 81 GRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARL----------------QE----------- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1779 tpqdytrisamnsvhcehveeggesryvlldiigkdhgfGVENLRAAGTIAGESSRAYDEIVTISMVTCRAIGIGAYLVR 1858
Cdd:COG4799 134 ---------------------------------------GVESFAGYGRIFYRNARSSGGIPQISVIMGPCAAGGAYSPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1859 LGQRVIQVE-NSHIILTG---VTAlnkVLGREVytSNNQLGGVQvMHN--NGISHITVPDDFEGVYTILQWLSYMPKDNR 1932
Cdd:COG4799 175 LSDFVIMVKgTSQMFLGGppvVKA---ATGEEV--TAEELGGAD-VHArvSGVADYLAEDEEEALALARRLLSYLPSNNL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 1933 SPVPVIAISDP--IEREI-DFVP--SKVPYDPRWMLAGrphptlkgtwqsgFFDQGSFLEIMKPWAQTVVVGRARLGGLP 2007
Cdd:COG4799 249 EDPPRAEPAPParDPEELyGIVPedPRKPYDMREVIAR-------------LVDGGSFFEFKPLYGPNIVTGFARIDGRP 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024460499 2008 VGVIAvetrtvevtipadpANPdseakiIQQAGqVWFPDSAFKTAQAIRDFNREHLPLMIFANWRGF 2074
Cdd:COG4799 316 VGIVA--------------NQP------MVLAG-VLDIDAADKAARFIRLCDAFNIPLVFLVDVPGF 361
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
809-875 |
2.69e-12 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 64.16 E-value: 2.69e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024460499 809 TVLRSPSAGKL-----LQYTVDDGGHVAEGSVFAEIEVMKIIMTLTVEEAGRVHYVKRP-GALLEAGCVIAQL 875
Cdd:pfam00364 1 TEIKSPMIGESvregvVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
810-875 |
3.64e-12 |
|
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: 63.59 E-value: 3.64e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024460499 810 VLRSPSAGKLLQYTVDDGGHVAEGSVFAEIEVMKIIMTLTVEEAGRVHYVK-RPGALLEAGCVIAQL 875
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
282-527 |
1.17e-07 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 56.48 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 282 GIAFLGPPSDAMWALGDKVASTIVAQTVQIPtlpwsgsglvaqwseedqkgqqmisIPlETYgqgCVKDVEEGLEVAKRI 361
Cdd:COG3919 101 HYRLPYPDADLLDRLLDKERFYELAEELGVP-------------------------VP-KTV---VLDSADDLDALAEDL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 362 GYPLMIKAAEGGGGKG--------IRKVEAAEEFGACFRQVqAEAPGSPIflmklaqharhleVQ--------------V 419
Cdd:COG3919 152 GFPVVVKPADSVGYDElsfpgkkkVFYVDDREELLALLRRI-AAAGYELI-------------VQeyipgddgemrgltA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 420 LADEYGNAISLFGrdcsiqrrHQKIIEeAPITIAAPAVIEV-----MEKCAVRLAQMVGYVSTGTVEYLY-SEDGSFHFL 493
Cdd:COG3919 218 YVDRDGEVVATFT--------GRKLRH-YPPAGGNSAARESvddpeLEEAARRLLEALGYHGFANVEFKRdPRDGEYKLI 288
|
250 260 270
....*....|....*....|....*....|....
gi 2024460499 494 ELNPRLQVEHPCTEmIADVNLPAAQLQIAMGIPL 527
Cdd:COG3919 289 EINPRFWRSLYLAT-AAGVNFPYLLYDDAVGRPL 321
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
809-876 |
1.07e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 42.69 E-value: 1.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024460499 809 TVLRSPSAGKllQYTVDDGGHVAEGSVFAEIEVMKIIMTLTVEEAGRV-HYVKRPGALLEAGCVIAQLE 876
Cdd:PRK07051 13 TFYRRPSPDA--PPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVvEFLVEDGEPVEAGQVLARIE 79
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
299-498 |
4.03e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 45.92 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 299 KVASTIVAQTVQIPTLPWSGSGLVAQW--------SEEDQKGQQMI--SIPLETYGQGCVKDVEEGLEVAKRIGYPLMIK 368
Cdd:PLN02735 664 KLALPIQKYLDKNPPPSASGNGNVKIWgtspdsidAAEDRERFNAIlnELKIEQPKGGIARSEADALAIAKRIGYPVVVR 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 369 AAEGGGGKGIRKVEAAEEFGACFRQVQAEAPGSPIFLMKLAQHARHLEVQVLADEYGNAISlfgrdCSIQRRhqkiIEEA 448
Cdd:PLN02735 744 PSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEGNVVI-----GGIMEH----IEQA 814
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024460499 449 -----------PITIAAPAVIEVMEKCAVRLAQMVGYVSTGTVEYLYSEDGSFHFLELNPR 498
Cdd:PLN02735 815 gvhsgdsacslPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR 875
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
348-498 |
9.16e-04 |
|
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: 44.60 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 348 VKDVEEGLEVAKRIGYPLMIKAAEGGGGKGIRKVEAAEEFGACFRQVQAEAPGSPIFLMKLAQHARHLEVQVLADeyGNA 427
Cdd:TIGR01369 690 ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 428 ISLFGrdcsIQrRHqkiIEEAPI-----TIAAPA------VIEVMEKCAVRLAQMVGYVSTGTVEYLYSeDGSFHFLELN 496
Cdd:TIGR01369 768 VLIPG----IM-EH---IEEAGVhsgdsTCVLPPqtlsaeIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVN 838
|
..
gi 2024460499 497 PR 498
Cdd:TIGR01369 839 PR 840
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
348-498 |
2.17e-03 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 43.33 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 348 VKDVEEGLEVAKRIGYPLMIKAA--------EGgggkgirkVEAAEEFGACFRQVQAEAPGSPIFLMKLAQHARHLEVQV 419
Cdd:COG0458 135 ATSVEEALAIAEEIGYPVIVRPSyvlggrgmGI--------VYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDV 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024460499 420 LADEYGNAISLfgrdCSIQrrHqkiIEEAPI-----TIAAPA------VIEVMEKCAVRLAQMVGYVSTGTVEYLYSeDG 488
Cdd:COG0458 207 VRDGEDNVIIV----GIME--H---IEPAGVhsgdsICVAPPqtlsdkEYQRLRDATLKIARALGVVGLCNIQFAVD-DG 276
|
170
....*....|
gi 2024460499 489 SFHFLELNPR 498
Cdd:COG0458 277 RVYVIEVNPR 286
|
|
| |
