|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
753-1479 |
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: 994.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 753 ELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLpepvfSIKLKEWVQKLMMTLRHPSLPLLE 832
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 833 LQEIMTSVAGRIPAPVEKSVRRVMAQYASNitsvLCQFPSQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSG 912
Cdd:pfam08326 76 WQEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 913 IRGYMKTVVLDLLRRYLRVEHHFQQA--HYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGP---DP 987
Cdd:pfam08326 152 LKGHEYSVFASLLEEYYDVEKLFSGGnvREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 988 SLSDELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCPENLKKLIL 1059
Cdd:pfam08326 232 NVAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELID 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1060 SETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCVVEFQFMLPSSHPNRMTVPISITNPDLLR 1139
Cdd:pfam08326 312 SKYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSPP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1140 H------STELFMDSGFSPLCQRMGAMVAFRRFEDFTRNFDEVISCFANVPKDTPLfseartslyseddcKSLREEPIHI 1213
Cdd:pfam08326 392 FkriasvSDLSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESGE--------------SNSSDEPINV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1214 LNVSIQCADHLE-DEALVPILRTFVQSKKNILVDYGLRRITFLIAQE-KEFPKFFTFRARDEFAEDRIYRHLEPALAFQL 1291
Cdd:pfam08326 458 LNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKdGQYPKYFTFRGPDNYEEDPIIRHIEPALAFQL 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1292 ELNRMRNFDLTAVPCANHKMHLYLGAAKVKEgvevTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAf 1371
Cdd:pfam08326 538 ELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRDDIPTAEYLISEAERLLNDILDALEVA- 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1372 NNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGSRLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLD 1451
Cdd:pfam08326 613 SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGPPIPLRLVITNVSGYVVK 692
|
730 740
....*....|....*....|....*...
gi 767974036 1452 ISLYKEVTDSRsGNIMFHSFGnKQGPQH 1479
Cdd:pfam08326 693 VELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1571-2119 |
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: 616.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1571 QEYPEGRDVIVIGNDITFRIGSFGPGEDLLYLRASEMARAEgIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGF 1650
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1651 KylyLTPQDYTRISSlnsvhckhieegGESRYMITDIIGKDDGLGVENLRGSGMIAGESSLAYEEIVTISLVTCRAIGIG 1730
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1731 AYLVRLGQRVIQVEN-SHIILTGASALNKVLGrEVYTSNNQLGGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNH 1809
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1810 S---PVPIITPTDPIDRE---IEFLPS--RAPYDPRWMLAGRphptlkgtwqsgfFDHGSFKEIMAPWAQTVVTGRARLG 1881
Cdd:pfam01039 224 NnrePVPIVPTKDPPDRDaplVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1882 GIPVGVIAVETRtvevavpadpanldseakiiQQAGqVWFPDSAYKTAQAVKDFNREKLPLMIFANWRGFSGGMKDMYDQ 1961
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1962 VLKFGAYIVDGLRQYKQPILIYIPPyaELRGGSWVVIDATINPLCIeMYADKESRGGVLEPEGTVEIKFRKKDLIKSMRR 2041
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767974036 2042 IDPAYKKlmeqlgepdlsdkdrkdlEGRLKAREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARtFLYW 2119
Cdd:pfam01039 427 KDLAATR------------------KQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
51-577 |
1.68e-131 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 421.35 E-value: 1.68e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 51 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 130
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 131 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 210
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 211 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSE---IPGSP-IFLMKLA 286
Cdd:COG4770 135 -----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREakaAFGDDrVYLEKYI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 287 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 366
Cdd:COG4770 204 ERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 367 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 445
Cdd:COG4770 284 FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPfTQEDIKL-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 446 SENPDEGFKPSSGTVQELNFRSSknvwgyFSVAATGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRG 519
Cdd:COG4770 341 AEDPARGFLPSPGTITRLRPPGG------PGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 767974036 520 dFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDimlgvvcgALNVADAM 577
Cdd:COG4770 415 -VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE--------ELALAAAM 463
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
51-557 |
1.66e-111 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 363.35 E-value: 1.66e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 51 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 130
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 131 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPwsGSgltvewteddlqqg 210
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 211 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP-IFLMKLA 286
Cdd:PRK08591 135 -----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 287 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 366
Cdd:PRK08591 204 ENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 367 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 445
Cdd:PRK08591 284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 446 SENPDEGFKPSSGTVQelnfrssknvwGYFsvaATGGLH--------------EFADSQFGHCFSWGENREEAISNMVVA 511
Cdd:PRK08591 341 AEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 767974036 512 LKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQA 557
Cdd:PRK08591 407 LSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
53-548 |
1.06e-85 |
|
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: 307.52 E-value: 1.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 53 KVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEY-IKMADHYVPVpggpnnNNYANVEL 125
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 126 IVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewted 205
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 206 dlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGS----PIF 281
Cdd:TIGR01235 135 ----------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 282 LMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLY 361
Cdd:TIGR01235 199 VEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 362 SQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLK-------DIRLlygespwgvtpisfetpsnppl 434
Cdd:TIGR01235 279 DNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQlgvpnqeDIRT---------------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 435 aRGHVIAARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSVAATGG-------LHEFADSQFGHCFSWGENREEAISN 507
Cdd:TIGR01235 337 -NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAK 409
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 767974036 508 MVVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 548
Cdd:TIGR01235 410 MDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
211-404 |
1.01e-54 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 190.21 E-value: 1.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 211 KRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSP----IFLMKLA 286
Cdd:pfam02786 10 KEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 287 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQD-G 365
Cdd:pfam02786 90 KGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsG 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 767974036 366 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL 404
Cdd:pfam02786 170 EYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
442-548 |
1.04e-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: 125.99 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 442 ARITSENPDEGFKPSSGTVQELNFRSSKNVwgYFSVAATGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 519
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 767974036 520 dFRTTVEYLINLLETESFQNNDIDTGWLD 548
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1558-1889 |
7.69e-26 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 114.35 E-value: 7.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1558 EVGM-VAFKMRFKTQEYP-----------EGRDVIVIGNDITFRIGSFGP--GEDLLylRASEMARAEGIPKIYVAANSG 1623
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPgdgvvtgigtvDGRPVVVVANDFTVKGGSLGPmtAKKIL--RAQDIALENGLPVIYLVDSGG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1624 ARIGMaeeikhmfhvawvdpedphkgfkylyltpqdytrisslnsvhckhieeggesrymitdiigkddglGVENLRGSG 1703
Cdd:COG4799 129 ARLQE------------------------------------------------------------------GVESFAGYG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1704 MIAGESSLAYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVE-NSHIILTGASALNKVLGREVytSNNQLGGVQiMHY--N 1780
Cdd:COG4799 143 RIFYRNARSSGGIPQISVIMGPCAAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1781 GVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDP--IDREI-EFLP--SRAPYDPRWMLAGrphptlkgtwqsg 1855
Cdd:COG4799 220 GVADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPParDPEELyGIVPedPRKPYDMREVIAR------------- 286
|
330 340 350
....*....|....*....|....*....|....
gi 767974036 1856 FFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIA 1889
Cdd:COG4799 287 LVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA 320
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
686-752 |
1.14e-15 |
|
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: 73.40 E-value: 1.14e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767974036 686 TVLRSPSAGKL-----TQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRP-GAVLEAGCVVARL 752
Cdd:pfam00364 1 TEIKSPMIGESvregvVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
687-752 |
7.71e-14 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 68.21 E-value: 7.71e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767974036 687 VLRSPSAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIK-RPGAVLEAGCVVARL 752
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1708-1970 |
3.45e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 45.57 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1708 ESSLAYEEIVTISLVTCRAIGIGAYLVRLG-QRVIQVENSHIILTGASALNKVLGREVytSNNQLGGVQImH--YNGVSH 1784
Cdd:PLN02820 198 QARMSSAGIPQIALVLGSCTAGGAYVPAMAdESVIVKGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-HckVSGVSD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1785 ITVPDDFEGV---YTILEWL-----SYMPKDNHSPVPII-TPTDPID--REIEFLPSRAPYDPRWMLAGrphptlkgtwq 1853
Cdd:PLN02820 275 HFAQDELHALaigRNIVKNLhlaakQGMENTLGSKNPEYkEPLYDVKelRGIVPADHKQSFDVRSVIAR----------- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1854 sgFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAvetrtvevavpadpanldseakiiqqAGQVWFPDSAYKTAQAVK 1933
Cdd:PLN02820 344 --IVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALKGAHFIE 395
|
250 260 270
....*....|....*....|....*....|....*..
gi 767974036 1934 DFNREKLPLMIFANWRGFSGGMKDMYDQVLKFGAYIV 1970
Cdd:PLN02820 396 LCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMV 432
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
693-753 |
1.28e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 39.39 E-value: 1.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767974036 693 AGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRP-GAVLEAGCVVARLE 753
Cdd:PRK08225 9 AGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQeGDFVNEGDVLLEIE 70
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
753-1479 |
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: 994.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 753 ELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLpepvfSIKLKEWVQKLMMTLRHPSLPLLE 832
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 833 LQEIMTSVAGRIPAPVEKSVRRVMAQYASNitsvLCQFPSQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSG 912
Cdd:pfam08326 76 WQEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 913 IRGYMKTVVLDLLRRYLRVEHHFQQA--HYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGP---DP 987
Cdd:pfam08326 152 LKGHEYSVFASLLEEYYDVEKLFSGGnvREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 988 SLSDELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCPENLKKLIL 1059
Cdd:pfam08326 232 NVAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELID 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1060 SETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCVVEFQFMLPSSHPNRMTVPISITNPDLLR 1139
Cdd:pfam08326 312 SKYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSPP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1140 H------STELFMDSGFSPLCQRMGAMVAFRRFEDFTRNFDEVISCFANVPKDTPLfseartslyseddcKSLREEPIHI 1213
Cdd:pfam08326 392 FkriasvSDLSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESGE--------------SNSSDEPINV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1214 LNVSIQCADHLE-DEALVPILRTFVQSKKNILVDYGLRRITFLIAQE-KEFPKFFTFRARDEFAEDRIYRHLEPALAFQL 1291
Cdd:pfam08326 458 LNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKdGQYPKYFTFRGPDNYEEDPIIRHIEPALAFQL 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1292 ELNRMRNFDLTAVPCANHKMHLYLGAAKVKEgvevTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAf 1371
Cdd:pfam08326 538 ELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRDDIPTAEYLISEAERLLNDILDALEVA- 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1372 NNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGSRLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLD 1451
Cdd:pfam08326 613 SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGPPIPLRLVITNVSGYVVK 692
|
730 740
....*....|....*....|....*...
gi 767974036 1452 ISLYKEVTDSRsGNIMFHSFGnKQGPQH 1479
Cdd:pfam08326 693 VELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1571-2119 |
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: 616.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1571 QEYPEGRDVIVIGNDITFRIGSFGPGEDLLYLRASEMARAEgIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGF 1650
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1651 KylyLTPQDYTRISSlnsvhckhieegGESRYMITDIIGKDDGLGVENLRGSGMIAGESSLAYEEIVTISLVTCRAIGIG 1730
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1731 AYLVRLGQRVIQVEN-SHIILTGASALNKVLGrEVYTSNNQLGGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNH 1809
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1810 S---PVPIITPTDPIDRE---IEFLPS--RAPYDPRWMLAGRphptlkgtwqsgfFDHGSFKEIMAPWAQTVVTGRARLG 1881
Cdd:pfam01039 224 NnrePVPIVPTKDPPDRDaplVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1882 GIPVGVIAVETRtvevavpadpanldseakiiQQAGqVWFPDSAYKTAQAVKDFNREKLPLMIFANWRGFSGGMKDMYDQ 1961
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1962 VLKFGAYIVDGLRQYKQPILIYIPPyaELRGGSWVVIDATINPLCIeMYADKESRGGVLEPEGTVEIKFRKKDLIKSMRR 2041
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767974036 2042 IDPAYKKlmeqlgepdlsdkdrkdlEGRLKAREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARtFLYW 2119
Cdd:pfam01039 427 KDLAATR------------------KQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
51-577 |
1.68e-131 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 421.35 E-value: 1.68e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 51 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 130
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 131 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 210
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 211 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSE---IPGSP-IFLMKLA 286
Cdd:COG4770 135 -----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREakaAFGDDrVYLEKYI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 287 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 366
Cdd:COG4770 204 ERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 367 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 445
Cdd:COG4770 284 FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPfTQEDIKL-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 446 SENPDEGFKPSSGTVQELNFRSSknvwgyFSVAATGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRG 519
Cdd:COG4770 341 AEDPARGFLPSPGTITRLRPPGG------PGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 767974036 520 dFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDimlgvvcgALNVADAM 577
Cdd:COG4770 415 -VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE--------ELALAAAM 463
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
51-557 |
1.66e-111 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 363.35 E-value: 1.66e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 51 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 130
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 131 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPwsGSgltvewteddlqqg 210
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 211 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP-IFLMKLA 286
Cdd:PRK08591 135 -----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 287 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 366
Cdd:PRK08591 204 ENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 367 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 445
Cdd:PRK08591 284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 446 SENPDEGFKPSSGTVQelnfrssknvwGYFsvaATGGLH--------------EFADSQFGHCFSWGENREEAISNMVVA 511
Cdd:PRK08591 341 AEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 767974036 512 LKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQA 557
Cdd:PRK08591 407 LSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
49-548 |
1.75e-104 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 364.46 E-value: 1.75e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 49 RVIEKVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEYIkmadhyVPVPGGPNNNnYAN 122
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAA---------TELGIRTVAIYSEEDklslhrFKADEAYL------IGEGKHPVRA-YLD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 123 VELIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGltvew 202
Cdd:PRK12999 67 IDEIIRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGP----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 203 teddlqqgkrisvpedvydkgcVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP 279
Cdd:PRK12999 142 ----------------------IDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafGND 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 280 -IFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVE 358
Cdd:PRK12999 200 eVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 359 YLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRL-------KDIRLlygespwgvtpisfetpsn 431
Cdd:PRK12999 280 FLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATLHDLeigipsqEDIRL------------------- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 432 pplaRGHVIAARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSVAATGGLHeFADSQFGHCF--------SWGENREE 503
Cdd:PRK12999 341 ----RGYAIQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVRLDGGNA-FAGAEITPYYdsllvkltAWGRTFEQ 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 767974036 504 AISNMVVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 548
Cdd:PRK12999 410 AVARMRRALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFID 453
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
51-548 |
7.57e-102 |
|
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: 356.31 E-value: 7.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 51 IEKVLIANNG-IAavkcmrsIR--RWAYEMfrnerAIRFVVMVTPED------LKANAEY-IKMADHyvPVpggpnnNNY 120
Cdd:COG1038 4 IKKVLVANRGeIA-------IRvfRAATEL-----GIRTVAIYSEEDryslhrFKADEAYlIGEGKG--PV------DAY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 121 ANVELIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPwsGSgltv 200
Cdd:COG1038 64 LDIEEIIRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP--GT---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 201 ewteddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---G 277
Cdd:COG1038 138 ---------------------EGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 278 SP-IFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGT 356
Cdd:COG1038 197 DDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 357 VEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-------RLKDIRLlygespwgvtpisfetp 429
Cdd:COG1038 277 VEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSLDdpeigipSQEDIRL----------------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 430 snpplaRGHVIAARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSV---AATGglheFA--------DSQFGHCFSWG 498
Cdd:COG1038 340 ------NGYAIQCRITTEDPANNFMPDTGRITA--YRSA----GGFGIrldGGNA----YTgavitpyyDSLLVKVTAWG 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 767974036 499 ENREEAISNMVVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 548
Cdd:COG1038 404 RTFEEAIRKMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFID 452
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
52-548 |
1.18e-100 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 333.87 E-value: 1.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 52 EKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAK 131
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACR---------ELGIKTVAVYSEAD--KNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 132 RIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqgk 211
Cdd:PRK08654 72 KAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGT----------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 212 risvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSeIPGS-----PIFLMKLA 286
Cdd:PRK08654 135 ----------EEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTQS-IAQSafgdsTVFIEKYL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 287 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSqDGS 366
Cdd:PRK08654 204 EKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGN 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 367 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL-HRLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 445
Cdd:PRK08654 283 FYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELsFKQEDITI-----------------------RGHAIECRIN 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 446 SENPDEGFKPSSGTVQelNFRSSknvwGYFSVAATGGLH------EFADSQFGHCFSWGENREEAISNMVVALKELSIRG 519
Cdd:PRK08654 340 AEDPLNDFAPSPGKIK--RYRSP----GGPGVRVDSGVHmgyeipPYYDSMISKLIVWGRTREEAIARMRRALYEYVIVG 413
|
490 500
....*....|....*....|....*....
gi 767974036 520 dFRTTVEYLINLLETESFQNNDIDTGWLD 548
Cdd:PRK08654 414 -VKTNIPFHKAVMENENFVRGNLHTHFIE 441
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
51-550 |
1.28e-100 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 331.99 E-value: 1.28e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 51 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 130
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLG---------IRTVAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 131 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTvewteddlqqg 210
Cdd:PRK06111 71 KKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLE----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 211 krisvpedvydkgcvkDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP-IFLMKLA 286
Cdd:PRK06111 140 ----------------DAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAAnffGNGeMYIEKYI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 287 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 366
Cdd:PRK06111 204 EDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 367 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL-HRLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 445
Cdd:PRK06111 284 FYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR-----------------------SGHAIEVRIY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 446 SENPDEgFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTV 525
Cdd:PRK06111 341 AEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEG-IKTNI 418
|
490 500
....*....|....*....|....*.
gi 767974036 526 EYLINLLETESFQNNDIDTGWL-DYL 550
Cdd:PRK06111 419 PLLLQVLEDPVFKAGGYTTGFLtKQL 444
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
51-547 |
7.62e-92 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 306.64 E-value: 7.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 51 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 130
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACR---------EMGIETVAVYSEAD--KDALHVQLADEAVCIGPASSKDSYLNIQNIISAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 131 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 210
Cdd:PRK05586 71 VLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 211 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGS----PIFLMKLA 286
Cdd:PRK05586 135 -----------EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 287 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 366
Cdd:PRK05586 204 ENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 367 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARIT 445
Cdd:PRK05586 284 FYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSiKQEDIKI-----------------------NGHSIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 446 SENPDEGFKPSSGTVQELNFRSSKNVwgYFSVAATGG--LHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRT 523
Cdd:PRK05586 341 AEDPKNGFMPCPGKIEELYIPGGLGV--RVDSAVYSGytIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEG-VNT 417
|
490 500
....*....|....*....|....
gi 767974036 524 TVEYLINLLETESFQNNDIDTGWL 547
Cdd:PRK05586 418 NIDFQFIILEDEEFIKGTYDTSFI 441
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
51-557 |
1.92e-90 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 303.21 E-value: 1.92e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 51 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDLKANAeyIKMADHYVPVPGGPNNNNYANVELIVDIA 130
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAAR---------ELGMRTVAACSDADRDSLA--ARMADEAVHIGPSHAAKSYLNPAAILAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 131 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 210
Cdd:PRK12833 74 RQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGS---------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 211 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAED----FPILFRQVQSEIPGSPIFLMKLA 286
Cdd:PRK12833 138 -----------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQlaaeLPLAQREAQAAFGDGGVYLERFI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 287 QHARHLEVQILADQYgNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLY-SQDG 365
Cdd:PRK12833 207 ARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFdDARG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 366 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLH-RLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARI 444
Cdd:PRK12833 286 EFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRfAQGDIAL-----------------------RGAALECRI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 445 TSENPDEGFKPSSGTVQELNF------RSSKNVWGYFSVAAtgglheFADSQFGHCFSWGENREEAISNMVVALKELSIR 518
Cdd:PRK12833 343 NAEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYPGYRVPP------FYDSLLAKLIVHGEDRAAALARAARALRELRID 416
|
490 500 510
....*....|....*....|....*....|....*....
gi 767974036 519 GdFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQA 557
Cdd:PRK12833 417 G-MKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAA 454
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
51-548 |
1.15e-89 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 300.12 E-value: 1.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 51 IEKVLIANNGIAAVKCMRSIRrwayEMfrNERAIrfVVMVTPEDlkaNAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 130
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQ----EM--GKEAI--AIYSTADK---DALYLKYADAKICIGGAKSSESYLNIPAIISAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 131 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewteddlqqg 210
Cdd:PRK08462 73 EIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGS---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 211 krisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGS----PIFLMKLA 286
Cdd:PRK08462 137 -----------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAfgdgTMYMEKFI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 287 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGS 366
Cdd:PRK08462 206 NNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 367 FHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLlygespwgvtpisfetpsnpplaRGHVIAARITS 446
Cdd:PRK08462 286 FYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKL-----------------------KGHAIECRITA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 447 ENPdEGFKPSSGTVQEL------NFRSSKNVWGYFSVAAtgglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGd 520
Cdd:PRK08462 343 EDP-KKFYPSPGKITKWiapggrNVRMDSHAYAGYVVPP------YYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEG- 414
|
490 500
....*....|....*....|....*...
gi 767974036 521 FRTTVEYLINLLETESFQNNDIDTGWLD 548
Cdd:PRK08462 415 IKTTIPFHLEMMENADFINNKYDTKYLE 442
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
53-548 |
1.06e-85 |
|
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: 307.52 E-value: 1.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 53 KVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEY-IKMADHYVPVpggpnnNNYANVEL 125
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 126 IVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewted 205
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 206 dlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGS----PIF 281
Cdd:TIGR01235 135 ----------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 282 LMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLY 361
Cdd:TIGR01235 199 VEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 362 SQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLK-------DIRLlygespwgvtpisfetpsnppl 434
Cdd:TIGR01235 279 DNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQlgvpnqeDIRT---------------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 435 aRGHVIAARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSVAATGG-------LHEFADSQFGHCFSWGENREEAISN 507
Cdd:TIGR01235 337 -NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAK 409
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 767974036 508 MVVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 548
Cdd:TIGR01235 410 MDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
50-548 |
1.69e-85 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 289.31 E-value: 1.69e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 50 VIEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYV-----PVPGgpnnnnYANVE 124
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACA---------EMGIRSVAIYSEAD--RHALHVKRADEAYsigadPLAG------YLNPR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 125 LIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSgsgltvewte 204
Cdd:PRK07178 64 RLVNLAVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGS---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 205 ddlqqgkrisvpedvydKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIP---GSP-I 280
Cdd:PRK07178 134 -----------------EGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafGSAeV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 281 FLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYL 360
Cdd:PRK07178 197 FLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 361 YSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL-HRLKDIRLlygespwgvtpisfetpsnpplaRGHV 439
Cdd:PRK07178 277 LDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH-----------------------RGFA 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 440 IAARITSENPDEGFKPSSGTVQElnfrssknvwgYFSVAATG---------GLH--EFADSQFGHCFSWGENREEAISNM 508
Cdd:PRK07178 334 LQFRINAEDPKNDFLPSFGKITR-----------YYAPGGPGvrtdtaiytGYTipPYYDSMCAKLIVWALTWEEALDRG 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 767974036 509 VVALKELSIRGdFRTTVEYLINLLETESFQNNDIDTGWLD 548
Cdd:PRK07178 403 RRALDDMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVE 441
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
51-571 |
9.87e-68 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 237.79 E-value: 9.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 51 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNnYANVELIVDIA 130
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACR---------DLHIKSVAIYTEPD--RECLHVKIADEAYRIGTDPIKG-YLDVKRIVEIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 131 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPwsgsgltvewteddlqqg 210
Cdd:PRK08463 70 KACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVP------------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 211 krisvpedvydkGCVKDVDEGLEA----AERIGFPLMIKASEGGGGKGIRKAESAEDFPILF----RQVQSEIPGSPIFL 282
Cdd:PRK08463 132 ------------GTEKLNSESMEEikifARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFesckREALAYFNNDEVFM 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 283 MKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYS 362
Cdd:PRK08463 200 EKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 363 QDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLhrlkdirllygespwgvtpisfETPSNPPLARGHVIAA 442
Cdd:PRK08463 280 DYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEIL----------------------DLEQSDIKPRGFAIEA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 443 RITSENPDEGFKPSSGTVQEL------NFRSSKNVWGYFSVAAtgglheFADSQFGHCFSWGENREEAISNMVVALKELS 516
Cdd:PRK08463 338 RITAENVWKNFIPSPGKITEYypalgpSVRVDSHIYKDYTIPP------YYDSMLAKLIVKATSYDLAVNKLERALKEFV 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767974036 517 IRGdFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQA------EKPDIMLGVVCGAL 571
Cdd:PRK08463 412 IDG-IRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKtedrhqENKEEVIAAIAAAL 471
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
211-404 |
1.01e-54 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 190.21 E-value: 1.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 211 KRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSP----IFLMKLA 286
Cdd:pfam02786 10 KEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 287 QHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQD-G 365
Cdd:pfam02786 90 KGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsG 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 767974036 366 SFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPL 404
Cdd:pfam02786 170 EYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
51-169 |
2.89e-43 |
|
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: 153.41 E-value: 2.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 51 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELIVDIA 130
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELG---------IRTVAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAA 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 767974036 131 KRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEA 169
Cdd:pfam00289 70 KETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
123-403 |
4.26e-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: 147.33 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 123 VELIVDIAKRIPVQAVWAGWGHASEnpKLPELLCKNGVAflGPPSEAMWALGDKIASTVVAQTLQVPTlPWSGsgltvew 202
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVE--TAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 203 teddlqqgkrisvpedvydkgCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEI----PGS 278
Cdd:COG0439 74 ---------------------LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 279 PIFLMKLAQHaRHLEVQILADQyGNAVSlfgrdCSIQRRHQK---IVE---EAPATIAPlAIFEFMEQCAIRLAKTVGYV 352
Cdd:COG0439 133 EVLVEEFLEG-REYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPLPE-ELRAEIGELVARALRALGYR 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767974036 353 -SAGTVEYLYSQDGSFHFLELNPRLQVEH--PCTEMIADVNLPAAQLQIAMGVP 403
Cdd:COG0439 205 rGAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
442-548 |
1.04e-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: 125.99 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 442 ARITSENPDEGFKPSSGTVQELNFRSSKNVwgYFSVAATGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 519
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 767974036 520 dFRTTVEYLINLLETESFQNNDIDTGWLD 548
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
442-548 |
5.66e-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: 5.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 442 ARITSENPDEGFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 521
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*..
gi 767974036 522 RTTVEYLINLLETESFQNNDIDTGWLD 548
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLE 107
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1558-1889 |
7.69e-26 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 114.35 E-value: 7.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1558 EVGM-VAFKMRFKTQEYP-----------EGRDVIVIGNDITFRIGSFGP--GEDLLylRASEMARAEGIPKIYVAANSG 1623
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPgdgvvtgigtvDGRPVVVVANDFTVKGGSLGPmtAKKIL--RAQDIALENGLPVIYLVDSGG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1624 ARIGMaeeikhmfhvawvdpedphkgfkylyltpqdytrisslnsvhckhieeggesrymitdiigkddglGVENLRGSG 1703
Cdd:COG4799 129 ARLQE------------------------------------------------------------------GVESFAGYG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1704 MIAGESSLAYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVE-NSHIILTGASALNKVLGREVytSNNQLGGVQiMHY--N 1780
Cdd:COG4799 143 RIFYRNARSSGGIPQISVIMGPCAAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1781 GVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDP--IDREI-EFLP--SRAPYDPRWMLAGrphptlkgtwqsg 1855
Cdd:COG4799 220 GVADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPParDPEELyGIVPedPRKPYDMREVIAR------------- 286
|
330 340 350
....*....|....*....|....*....|....
gi 767974036 1856 FFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIA 1889
Cdd:COG4799 287 LVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA 320
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
686-752 |
1.14e-15 |
|
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: 73.40 E-value: 1.14e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767974036 686 TVLRSPSAGKL-----TQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRP-GAVLEAGCVVARL 752
Cdd:pfam00364 1 TEIKSPMIGESvregvVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
687-752 |
7.71e-14 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 68.21 E-value: 7.71e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767974036 687 VLRSPSAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIK-RPGAVLEAGCVVARL 752
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
105-404 |
5.46e-11 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 66.88 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 105 ADHYVPVPGgPNNNNYANVELIVDIAKRIPVQAVWA---GWGHA-SEN-PKLPEllcknGVAFLGPPSEAMWALGDKIAS 179
Cdd:COG3919 48 VDEVVVVPD-PGDDPEAFVDALLELAERHGPDVLIPtgdEYVELlSRHrDELEE-----HYRLPYPDADLLDRLLDKERF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 180 TVVAQTLQVPtlpwsgsgltvewteddlqqgkrisVPEDVYdkgcVKDVDEGLEAAERIGFPLMIKASEG--------GG 251
Cdd:COG3919 122 YELAEELGVP-------------------------VPKTVV----LDSADDLDALAEDLGFPVVVKPADSvgydelsfPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 252 GKGIRKAESAEDFPILFRQ---------VQSEIPG--SPIFLmklaqharhleVQILADQYGNAVSLFGrdcsiqrrHQK 320
Cdd:COG3919 173 KKKVFYVDDREELLALLRRiaaagyeliVQEYIPGddGEMRG-----------LTAYVDRDGEVVATFT--------GRK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 321 IVEeAPATIAPLAIFEF-----MEQCAIRLAKTVGYVSAGTVEYLY-SQDGSFHFLELNPRLQVEHPCTEmIADVNLPAA 394
Cdd:COG3919 234 LRH-YPPAGGNSAARESvddpeLEEAARRLLEALGYHGFANVEFKRdPRDGEYKLIEINPRFWRSLYLAT-AAGVNFPYL 311
|
330
....*....|
gi 767974036 395 QLQIAMGVPL 404
Cdd:COG3919 312 LYDDAVGRPL 321
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
199-430 |
1.40e-07 |
|
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: 57.32 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 199 TVEWTED-DLQQGKRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASE--GGGGKGIrkAESAEDFPILFRQVQSEI 275
Cdd:TIGR01369 121 AIKKAEDrELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSAS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 276 PGSPIFLMKLAQHARHLEVQILADQYGNAVSLfgrdCSIQR-----RH--QKIVeeapatIAP---LAIFEF--MEQCAI 343
Cdd:TIGR01369 199 PINQVLVEKSLAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHtgDSIV------VAPsqtLTDKEYqmLRDASI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 344 RLAKTVGYVSAGTVEY-LYSQDGSFHFLELNPRLQ---------VEHPctemIADVnlpAAQLqiAMGVPLHRLK-DIRl 412
Cdd:TIGR01369 269 KIIRELGIEGGCNVQFaLNPDSGRYYVIEVNPRVSrssalaskaTGYP----IAKV---AAKL--AVGYTLDELKnPVT- 338
|
250
....*....|....*...
gi 767974036 413 lygespwGVTPISFEtPS 430
Cdd:TIGR01369 339 -------GTTPASFE-PS 348
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
223-375 |
6.93e-07 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 54.78 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 223 GCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDfpiLFRQVQSEI---PGSPIFLMKLAQHARHLEVQILAD 299
Cdd:PLN02735 721 GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDK---LKTYLETAVevdPERPVLVDKYLSDATEIDVDALAD 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 300 QYGNAV-----------SLFGRD--CSIQRrhQKIVEEAPATIaplaifefmEQCAIRLAKTVGYVSAGTVEYLYSQDGS 366
Cdd:PLN02735 798 SEGNVViggimehieqaGVHSGDsaCSLPT--QTIPSSCLATI---------RDWTTKLAKRLNVCGLMNCQYAITPSGE 866
|
....*....
gi 767974036 367 FHFLELNPR 375
Cdd:PLN02735 867 VYIIEANPR 875
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
225-404 |
3.19e-06 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 52.69 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 225 VKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQILADqyGNA 304
Cdd:TIGR01369 690 ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 305 VSLFGrdcsIQrRHqkiVEEA-----------PATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSqDGSFHFLELN 373
Cdd:TIGR01369 768 VLIPG----IM-EH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVN 838
|
170 180 190
....*....|....*....|....*....|.
gi 767974036 374 PRLQVEHPCTEMIADVNLPAAQLQIAMGVPL 404
Cdd:TIGR01369 839 PRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
225-375 |
4.61e-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: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 225 VKDVDEGLEAAERIGFPLMIKASE--GGGGKGIrkAESAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQILADQYG 302
Cdd:COG0458 135 ATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGED 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 303 NAVSLfgrdCSIQrrHqkiVEEA------PATIAP-----LAIFEFMEQCAIRLAKTVGYVSAGTVEYLYsQDGSFHFLE 371
Cdd:COG0458 213 NVIIV----GIME--H---IEPAgvhsgdSICVAPpqtlsDKEYQRLRDATLKIARALGVVGLCNIQFAV-DDGRVYVIE 282
|
....
gi 767974036 372 LNPR 375
Cdd:COG0458 283 VNPR 286
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1708-1970 |
3.45e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 45.57 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1708 ESSLAYEEIVTISLVTCRAIGIGAYLVRLG-QRVIQVENSHIILTGASALNKVLGREVytSNNQLGGVQImH--YNGVSH 1784
Cdd:PLN02820 198 QARMSSAGIPQIALVLGSCTAGGAYVPAMAdESVIVKGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-HckVSGVSD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1785 ITVPDDFEGV---YTILEWL-----SYMPKDNHSPVPII-TPTDPID--REIEFLPSRAPYDPRWMLAGrphptlkgtwq 1853
Cdd:PLN02820 275 HFAQDELHALaigRNIVKNLhlaakQGMENTLGSKNPEYkEPLYDVKelRGIVPADHKQSFDVRSVIAR----------- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 1854 sgFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAvetrtvevavpadpanldseakiiqqAGQVWFPDSAYKTAQAVK 1933
Cdd:PLN02820 344 --IVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALKGAHFIE 395
|
250 260 270
....*....|....*....|....*....|....*..
gi 767974036 1934 DFNREKLPLMIFANWRGFSGGMKDMYDQVLKFGAYIV 1970
Cdd:PLN02820 396 LCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMV 432
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
693-753 |
1.28e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 39.39 E-value: 1.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767974036 693 AGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRP-GAVLEAGCVVARLE 753
Cdd:PRK08225 9 AGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQeGDFVNEGDVLLEIE 70
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
225-264 |
2.41e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 43.16 E-value: 2.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767974036 225 VKDVDEGLEAAERIGFPLMIKAS--EGGGGKGIrkAESAEDF 264
Cdd:PRK05294 149 AHSMEEALEVAEEIGYPVIIRPSftLGGTGGGI--AYNEEEL 188
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
213-375 |
2.75e-03 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 42.18 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 213 ISVPeDVYDKGCVKDVDEGLEAAErIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQ-----VQSEIPGSPIflmklaq 287
Cdd:PRK12767 124 IPTP-KSYLPESLEDFKAALAKGE-LQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYvpnliIQEFIEGQEY------- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 288 harhlEVQILADQYGNAVSLFGRdcsiqRRH--------QKIVEEAPAtiaplaIFEFMEqcaiRLAKTVGYVSAGTVEY 359
Cdd:PRK12767 195 -----TVDVLCDLNGEVISIVPR-----KRIevragetsKGVTVKDPE------LFKLAE----RLAEALGARGPLNIQC 254
|
170
....*....|....*.
gi 767974036 360 LYSqDGSFHFLELNPR 375
Cdd:PRK12767 255 FVT-DGEPYLFEINPR 269
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
686-753 |
3.28e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 38.46 E-value: 3.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767974036 686 TVLRSPSAGklTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRV-KYIKRPGAVLEAGCVVARLE 753
Cdd:PRK07051 13 TFYRRPSPD--APPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVvEFLVEDGEPVEAGQVLARIE 79
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
233-377 |
9.08e-03 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 39.29 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767974036 233 EAAERIGFPLMIKASEGGGGKGIRKAE--SAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQIlADQY-GNAVSLF- 308
Cdd:pfam02655 25 EELLREEKKYVVKPRDGCGGEGVRKVEngREDEAFIENVLVQEFIEGEPLSVSLLSDGEKALPLSV-NRQYiDNGGSGFv 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767974036 309 ---GRDCSIQRRHQKIVEEApatiaplaifefmEQCAIRLAKTVGYVSagtVEYLYSqDGSFHFLELNPRLQ 377
Cdd:pfam02655 104 yagNVTPSRTELKEEIIELA-------------EEVVECLPGLRGYVG---VDLVLK-DNEPYVIEVNPRIT 158
|
|
| |
