|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
819-1568 |
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: 1009.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 819 LDNPSKVQQAELHTGSLPQIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLpdpffSSKVKDWVERLMKTLRDPSLPLLEL 898
Cdd:pfam08326 2 LDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLEW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 899 QDIMTSVSGRIPLNVEKSIKKEMAQYASNitsvLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGI 978
Cdd:pfam08326 77 QEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 979 RGHMKAVVMDLLRQYLRVETQFQ--NGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGR---DPT 1053
Cdd:pfam08326 153 KGHEYSVFASLLEEYYDVEKLFSggNVREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVSN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1054 LTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCIENLQKLILS 1125
Cdd:pfam08326 233 VAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELIDS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1126 ETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRMSFASnl 1205
Cdd:pfam08326 313 KYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSP-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1206 nhyGMTHVASVSD-VLLDNAFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFCDSPPQSPTFPESghtslydedkvprDEP 1284
Cdd:pfam08326 391 ---PFKRIASVSDlSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESGESNSS-------------DEP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1285 IHILNVAIKTDGDIE-DDRLAAMFREFTQQNKATLVEHGIRRLTFLVAQKDfrkqvncevdqrfhREFPKFFTFRARDKF 1363
Cdd:pfam08326 455 INVLNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKD--------------GQYPKYFTFRGPDNY 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1364 EEDRIYRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVgtevTDYRFFVRAIIRHSDLVTKEASFEYLQN 1443
Cdd:pfam08326 521 EEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRDDIPTAEYLIS 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1444 EGERLLLEAMDELEVAfNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTTTGK 1523
Cdd:pfam08326 597 EAERLLNDILDALEVA-SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGP 675
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1958660710 1524 AIPIRLFLTNESGYYLDISLYKEVTDSRtAQIMFQAYGdKQGPLH 1568
Cdd:pfam08326 676 PIPLRLVITNVSGYVVKVELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1668-2216 |
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: 611.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1668 PEYPDGRDVIVIGNDITYRIGSFGPQEDLLFLRASELARAEgIPRIYVAANSGARIGLAEEIRHMFHVAWVDSEDPYKGY 1747
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1748 KylyLTPQDYKRVSAlnsvhcehvedeGESRYKITDIIGKEEGLGAENLRGSGMIAGESSLAYDEIITISLVTCRAIGIG 1827
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1828 AYLVRLGQRTIQVEN-SHLILTGAGALNKVLGrEVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKNVH 1906
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1907 S---SVPLLNSKDPIDR---IIEFVPT--KAPYDPRWMLAGRphptqkgqwlsgfFDYGSFSEIMQPWAQTVVVGRARLG 1978
Cdd:pfam01039 224 NnrePVPIVPTKDPPDRdapLVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1979 GIPVGVVAVETRtvelsvpadpanldseakiiQQAGqVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQ 2058
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 2059 VLKFGAYIVDGLRECSQPVMVYIPPqaELRGGSWVVIDPTINPRHMeMYADRESRGSVLEPEGTVEIKFRKKDLVKTMRR 2138
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958660710 2139 VDPvyirlaerlgtpelspteRKELESKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVINDILDWKTSRtFFYW 2216
Cdd:pfam01039 427 KDL------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
117-626 |
7.79e-134 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 428.28 E-value: 7.79e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 117 IEKVLIANNGIAAVKCMRSIRrwsyEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGANNNNYANVELILDIA 196
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 197 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 276
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 277 ilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 352
Cdd:COG4770 135 ----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 353 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 432
Cdd:COG4770 205 RPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 433 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRmmygvspwgdapidfensahvpcPRGHVIAARITS 511
Cdd:COG4770 285 YFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLpFTQEDIK-----------------------LRGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 512 ENPDEGFKPSSGTVQELNFRsnknvwGYFSVAAAGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRGd 585
Cdd:COG4770 342 EDPARGFLPSPGTITRLRPP------GGPGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG- 414
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1958660710 586 FRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQAERPD 626
Cdd:COG4770 415 VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
117-622 |
1.89e-112 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 366.05 E-value: 1.89e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 117 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGANNNNYANVELILDIA 196
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 197 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSglrvdwqendfskr 276
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 277 ilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSPIFVM-RLAK 352
Cdd:PRK08591 135 ----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPGVYMeKYLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 353 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 432
Cdd:PRK08591 205 NPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 433 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspwgdapidfensahvpcpRGHVIAARITS 511
Cdd:PRK08591 285 YFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLsIKQEDIVF-----------------------RGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 512 ENPDEGFKPSSGTVQelnfrsnknvwGYFsvaAAGGLH--------------EFADSQFGHCFSWGENREEAISNMVVAL 577
Cdd:PRK08591 342 EDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRAL 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1958660710 578 KELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQA 622
Cdd:PRK08591 408 SEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
117-618 |
1.54e-101 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 334.81 E-value: 1.54e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 117 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGANNNNYANVELILDIA 196
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACK---------ELGIKTVAVHSTAD--RDALHVLLADEAVCIGPAPSAKSYLNIPNIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 197 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 276
Cdd:TIGR00514 71 EITGADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 277 ilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 352
Cdd:TIGR00514 135 ----------DGLVEDEEENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKaafGNDgVYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 353 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 432
Cdd:TIGR00514 205 NPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 433 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspwgdapidfensahvpcpRGHVIAARITS 511
Cdd:TIGR00514 285 YFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPLsLKQEDVVV-----------------------RGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 512 ENPDEGFKPSSGTVQE------LNFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGd 585
Cdd:TIGR00514 342 EDPIKTFLPSPGRITRylppggPGVRWDSHVYSGYTVPP------YYDSMIGKLITYGKTREVAIARMKRALSEFIIDG- 414
|
490 500 510
....*....|....*....|....*....|...
gi 1958660710 586 FRTTVEYLIKLLETESFQLNRIDTGWLDRLIAE 618
Cdd:TIGR00514 415 IKTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
288-469 |
8.83e-62 |
|
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: 210.62 E-value: 8.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 288 GYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSP----IFVMRLAKQSRHLEVQILA 363
Cdd:pfam02786 22 GPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 364 DQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQD-GSFYFLELNPRLQ 442
Cdd:pfam02786 102 DAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsGEYYFIEMNTRLQ 181
|
170 180
....*....|....*....|....*..
gi 1958660710 443 VEHPCTEMVADVNLPAAQLQIAMGIPL 469
Cdd:pfam02786 182 VEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
507-613 |
2.99e-32 |
|
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: 122.14 E-value: 2.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 507 ARITSENPDEGFKPSSGTVQELNFRSNKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 584
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 1958660710 585 dFRTTVEYLIKLLETESFQLNRIDTGWLD 613
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1655-1986 |
5.14e-21 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 99.33 E-value: 5.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1655 EIGM-VAWKMSLKSPEYP-----------DGRDVIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVAANSGAR 1722
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPgdgvvtgigtvDGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1723 IGLAEEIRHMFhvawvdsedpykgykylyltpqdykrvsalnsvhcehvedeGESRYKitdiigkeeglgaeNLRGSGMI 1802
Cdd:COG4799 131 LQEGVESFAGY-----------------------------------------GRIFYR--------------NARSSGGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1803 AgesslaydeiiTISLVTCRAIGIGAYLVRLGQRTIQVE-NSHLILTGAGALNKVLGREVytSNNQLGGIQiMHN--NGV 1879
Cdd:COG4799 156 P-----------QISVIMGPCAAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvSGV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1880 THCTVCDDFEGVFTVLHWLSYMPKNVHSSVPLLNSKDP---IDRIIEFVPT--KAPYDPRWMLAGrphptqkgqwlsgFF 1954
Cdd:COG4799 222 ADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPPardPEELYGIVPEdpRKPYDMREVIAR-------------LV 288
|
330 340 350
....*....|....*....|....*....|..
gi 1958660710 1955 DYGSFSEIMQPWAQTVVVGRARLGGIPVGVVA 1986
Cdd:COG4799 289 DGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA 320
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
752-817 |
2.07e-17 |
|
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: 78.41 E-value: 2.07e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958660710 752 VMRSPSAGKLI-----QYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRP-GAALDPGCVIAKM 817
Cdd:pfam00364 2 EIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
754-817 |
8.95e-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: 67.83 E-value: 8.95e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958660710 754 RSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVK-RPGAALDPGCVIAKM 817
Cdd:cd06850 3 TAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1805-2067 |
4.28e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 45.57 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1805 ESSLAYDEIITISLVTCRAIGIGAYLVRLGQRTIQV-ENSHLILTGAGALNKVLGREVytSNNQLGGIQImhnngvtHCT 1883
Cdd:PLN02820 198 QARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVkGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-------HCK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1884 ---VCDDF-----------EGVFTVLHWLSYMPKNVHSSVPLLNSKDPIDRIIEF---VPT--KAPYDPRWMLAGrphpt 1944
Cdd:PLN02820 269 vsgVSDHFaqdelhalaigRNIVKNLHLAAKQGMENTLGSKNPEYKEPLYDVKELrgiVPAdhKQSFDVRSVIAR----- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1945 qkgqwlsgFFDYGSFSEIMQPWAQTVVVGRARLGGIPVGVVAvetrtvelsvpadpanldseakiiqqAGQVWFPDSAFK 2024
Cdd:PLN02820 344 --------IVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALK 389
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958660710 2025 TYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIV 2067
Cdd:PLN02820 390 GAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMV 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
819-1568 |
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: 1009.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 819 LDNPSKVQQAELHTGSLPQIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLpdpffSSKVKDWVERLMKTLRDPSLPLLEL 898
Cdd:pfam08326 2 LDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLEW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 899 QDIMTSVSGRIPLNVEKSIKKEMAQYASNitsvLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGI 978
Cdd:pfam08326 77 QEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 979 RGHMKAVVMDLLRQYLRVETQFQ--NGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGR---DPT 1053
Cdd:pfam08326 153 KGHEYSVFASLLEEYYDVEKLFSggNVREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVSN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1054 LTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCIENLQKLILS 1125
Cdd:pfam08326 233 VAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELIDS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1126 ETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRMSFASnl 1205
Cdd:pfam08326 313 KYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSP-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1206 nhyGMTHVASVSD-VLLDNAFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFCDSPPQSPTFPESghtslydedkvprDEP 1284
Cdd:pfam08326 391 ---PFKRIASVSDlSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESGESNSS-------------DEP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1285 IHILNVAIKTDGDIE-DDRLAAMFREFTQQNKATLVEHGIRRLTFLVAQKDfrkqvncevdqrfhREFPKFFTFRARDKF 1363
Cdd:pfam08326 455 INVLNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKD--------------GQYPKYFTFRGPDNY 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1364 EEDRIYRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVgtevTDYRFFVRAIIRHSDLVTKEASFEYLQN 1443
Cdd:pfam08326 521 EEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRDDIPTAEYLIS 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1444 EGERLLLEAMDELEVAfNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTTTGK 1523
Cdd:pfam08326 597 EAERLLNDILDALEVA-SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGP 675
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1958660710 1524 AIPIRLFLTNESGYYLDISLYKEVTDSRtAQIMFQAYGdKQGPLH 1568
Cdd:pfam08326 676 PIPLRLVITNVSGYVVKVELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1668-2216 |
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: 611.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1668 PEYPDGRDVIVIGNDITYRIGSFGPQEDLLFLRASELARAEgIPRIYVAANSGARIGLAEEIRHMFHVAWVDSEDPYKGY 1747
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1748 KylyLTPQDYKRVSAlnsvhcehvedeGESRYKITDIIGKEEGLGAENLRGSGMIAGESSLAYDEIITISLVTCRAIGIG 1827
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1828 AYLVRLGQRTIQVEN-SHLILTGAGALNKVLGrEVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKNVH 1906
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1907 S---SVPLLNSKDPIDR---IIEFVPT--KAPYDPRWMLAGRphptqkgqwlsgfFDYGSFSEIMQPWAQTVVVGRARLG 1978
Cdd:pfam01039 224 NnrePVPIVPTKDPPDRdapLVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1979 GIPVGVVAVETRtvelsvpadpanldseakiiQQAGqVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQ 2058
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 2059 VLKFGAYIVDGLRECSQPVMVYIPPqaELRGGSWVVIDPTINPRHMeMYADRESRGSVLEPEGTVEIKFRKKDLVKTMRR 2138
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958660710 2139 VDPvyirlaerlgtpelspteRKELESKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVINDILDWKTSRtFFYW 2216
Cdd:pfam01039 427 KDL------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
117-626 |
7.79e-134 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 428.28 E-value: 7.79e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 117 IEKVLIANNGIAAVKCMRSIRrwsyEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGANNNNYANVELILDIA 196
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 197 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 276
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 277 ilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 352
Cdd:COG4770 135 ----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 353 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 432
Cdd:COG4770 205 RPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 433 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRmmygvspwgdapidfensahvpcPRGHVIAARITS 511
Cdd:COG4770 285 YFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLpFTQEDIK-----------------------LRGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 512 ENPDEGFKPSSGTVQELNFRsnknvwGYFSVAAAGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRGd 585
Cdd:COG4770 342 EDPARGFLPSPGTITRLRPP------GGPGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG- 414
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1958660710 586 FRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQAERPD 626
Cdd:COG4770 415 VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
117-622 |
1.89e-112 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 366.05 E-value: 1.89e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 117 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGANNNNYANVELILDIA 196
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 197 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSglrvdwqendfskr 276
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 277 ilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSPIFVM-RLAK 352
Cdd:PRK08591 135 ----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPGVYMeKYLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 353 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 432
Cdd:PRK08591 205 NPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 433 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspwgdapidfensahvpcpRGHVIAARITS 511
Cdd:PRK08591 285 YFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLsIKQEDIVF-----------------------RGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 512 ENPDEGFKPSSGTVQelnfrsnknvwGYFsvaAAGGLH--------------EFADSQFGHCFSWGENREEAISNMVVAL 577
Cdd:PRK08591 342 EDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRAL 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1958660710 578 KELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQA 622
Cdd:PRK08591 408 SEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
118-621 |
1.01e-103 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 342.73 E-value: 1.01e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 118 EKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGANNNNYANVELILDIAK 197
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACR---------ELGIKTVAVYSEAD--KNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 198 RIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGlrvdwqendfskri 277
Cdd:PRK08654 72 KAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEG-------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 278 lnvpqdlyekgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLF---RQVQAEVPGSP-IFVMRLAKQ 353
Cdd:PRK08654 138 ------------IEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIestQSIAQSAFGDStVFIEKYLEK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 354 SRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSqDGSFY 433
Cdd:PRK08654 206 PRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 434 FLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspwgdapidfensahvpcpRGHVIAARITSE 512
Cdd:PRK08654 285 FLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELsFKQEDITI-----------------------RGHAIECRINAE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 513 NPDEGFKPSSGTVQelnfrsnknvwGYFSVAAAG-----GLH------EFADSQFGHCFSWGENREEAISNMVVALKELS 581
Cdd:PRK08654 342 DPLNDFAPSPGKIK-----------RYRSPGGPGvrvdsGVHmgyeipPYYDSMISKLIVWGRTREEAIARMRRALYEYV 410
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1958660710 582 IRGdFRTTVEYLIKLLETESFQLNRIDTGWLD--RLIAEKVQ 621
Cdd:PRK08654 411 IVG-VKTNIPFHKAVMENENFVRGNLHTHFIEeeTTILEEMK 451
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
115-613 |
4.80e-103 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 360.22 E-value: 4.80e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 115 KVIEKVLIANNGIAAVKCMRSIrrwsyemfrNERAIRFVVMVTPED------LKANAEYI-----KMADHYVpvpggann 183
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAA---------TELGIRTVAIYSEEDklslhrFKADEAYLigegkHPVRAYL-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 184 nnyaNVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSG 263
Cdd:PRK12999 66 ----DIDEIIRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 264 lrvdwqendfskrilnvpqdlyekgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP-- 341
Cdd:PRK12999 142 --------------------------IDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaa 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 342 -GSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSA 419
Cdd:PRK12999 196 fGNDeVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 420 GTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLfrikdirmmygvspwGDAPIDFENSAHVpC 499
Cdd:PRK12999 276 GTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATL---------------HDLEIGIPSQEDI-R 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 500 PRGHVIAARITSENPDEGFKPSSGTVQElnFRSNknvwGYFSV------AAAGGlhEFA---DSQFGHCFSWGENREEAI 570
Cdd:PRK12999 340 LRGYAIQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVrldggnAFAGA--EITpyyDSLLVKLTAWGRTFEQAV 411
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1958660710 571 SNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD 613
Cdd:PRK12999 412 ARMRRALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFID 453
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
117-618 |
1.54e-101 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 334.81 E-value: 1.54e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 117 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGANNNNYANVELILDIA 196
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACK---------ELGIKTVAVHSTAD--RDALHVLLADEAVCIGPAPSAKSYLNIPNIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 197 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 276
Cdd:TIGR00514 71 EITGADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 277 ilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 352
Cdd:TIGR00514 135 ----------DGLVEDEEENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKaafGNDgVYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 353 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 432
Cdd:TIGR00514 205 NPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 433 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspwgdapidfensahvpcpRGHVIAARITS 511
Cdd:TIGR00514 285 YFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPLsLKQEDVVV-----------------------RGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 512 ENPDEGFKPSSGTVQE------LNFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGd 585
Cdd:TIGR00514 342 EDPIKTFLPSPGRITRylppggPGVRWDSHVYSGYTVPP------YYDSMIGKLITYGKTREVAIARMKRALSEFIIDG- 414
|
490 500 510
....*....|....*....|....*....|...
gi 1958660710 586 FRTTVEYLIKLLETESFQLNRIDTGWLDRLIAE 618
Cdd:TIGR00514 415 IKTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
117-614 |
2.87e-101 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 333.92 E-value: 2.87e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 117 IEKVLIANNGIAAVKCMRSIRRWsyemfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGANNNNYANVELILDIA 196
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKL---------GIRTVAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 197 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGLrvdwqendfskr 276
Cdd:PRK06111 71 KKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNL------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 277 ilnvpqdlyekgyvKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 352
Cdd:PRK06111 139 --------------EDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAAnffGNGeMYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 353 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 432
Cdd:PRK06111 205 DPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 433 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspwgdapidfensahvpcpRGHVIAARITS 511
Cdd:PRK06111 285 YFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR-----------------------SGHAIEVRIYA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 512 ENPDEgFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVE 591
Cdd:PRK06111 342 EDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEG-IKTNIP 419
|
490 500
....*....|....*....|...
gi 1958660710 592 YLIKLLETESFQLNRIDTGWLDR 614
Cdd:PRK06111 420 LLLQVLEDPVFKAGGYTTGFLTK 442
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
115-613 |
1.41e-98 |
|
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: 346.68 E-value: 1.41e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 115 KVIEKVLIANNG-IAavkcmrsIRrwsyeMFR--NERAIRFVVMVTPED------LKANAEY-IKMADHyvPVpggannN 184
Cdd:COG1038 2 KKIKKVLVANRGeIA-------IR-----VFRaaTELGIRTVAIYSEEDryslhrFKADEAYlIGEGKG--PV------D 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 185 NYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSgl 264
Cdd:COG1038 62 AYLDIEEIIRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP--GT-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 265 rvdwqendfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP--- 341
Cdd:COG1038 138 ----------------------EGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaaf 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 342 GSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAG 420
Cdd:COG1038 196 GDDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 421 TVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLfrikdirmmygvspwGDAPIDFENSAHVPCp 500
Cdd:COG1038 276 TVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSL---------------DDPEIGIPSQEDIRL- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 501 RGHVIAARITSENPDEGFKPSSGTVQElnFRSnknvwgyfsvaaAGGlhefadsqFG------HCFS------------- 561
Cdd:COG1038 340 NGYAIQCRITTEDPANNFMPDTGRITA--YRS------------AGG--------FGirldggNAYTgavitpyydsllv 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958660710 562 ----WGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD 613
Cdd:COG1038 398 kvtaWGRTFEEAIRKMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFID 452
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
117-622 |
3.21e-94 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 314.39 E-value: 3.21e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 117 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDLKANAeyIKMADHYVPVPGGANNNNYANVELILDIA 196
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAAR---------ELGMRTVAACSDADRDSLA--ARMADEAVHIGPSHAAKSYLNPAAILAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 197 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 276
Cdd:PRK12833 74 RQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGS---------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 277 ilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 352
Cdd:PRK12833 138 ----------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQaafGDGgVYLERFIA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 353 QSRHLEVQILADQYgNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLY-SQDGS 431
Cdd:PRK12833 208 RARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFdDARGE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 432 FYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspwgdapidfensahvpcpRGHVIAARIT 510
Cdd:PRK12833 287 FYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLrFAQGDIAL-----------------------RGAALECRIN 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 511 SENPDEGFKPSSGTVQELNF------RSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRG 584
Cdd:PRK12833 344 AEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYPGYRVPP------FYDSLLAKLIVHGEDRAAALARAARALRELRIDG 417
|
490 500 510
....*....|....*....|....*....|....*...
gi 1958660710 585 dFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQA 622
Cdd:PRK12833 418 -MKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAA 454
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
117-614 |
2.51e-93 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 310.91 E-value: 2.51e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 117 IEKVLIANNGIAAVKCMRSIRrwsyEMfrNERAIrfVVMVTPEDlkaNAEYIKMADHYVPVPGGANNNNYANVELILDIA 196
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQ----EM--GKEAI--AIYSTADK---DALYLKYADAKICIGGAKSSESYLNIPAIISAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 197 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 276
Cdd:PRK08462 73 EIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGS---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 277 ilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGS----PIFVMRLAK 352
Cdd:PRK08462 137 ----------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAfgdgTMYMEKFIN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 353 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 432
Cdd:PRK08462 207 NPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 433 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLFRIKDIRMmygvspwgdapidfensahvpcpRGHVIAARITSE 512
Cdd:PRK08462 287 YFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKL-----------------------KGHAIECRITAE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 513 NPdEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 586
Cdd:PRK08462 344 DP-KKFYPSPGKITKWiapggrNVRMDSHAYAGYVVPP------YYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEG-I 415
|
490 500
....*....|....*....|....*...
gi 1958660710 587 RTTVEYLIKLLETESFQLNRIDTGWLDR 614
Cdd:PRK08462 416 KTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
117-614 |
3.06e-92 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 307.79 E-value: 3.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 117 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGANNNNYANVELILDIA 196
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACR---------EMGIETVAVYSEAD--KDALHVQLADEAVCIGPASSKDSYLNIQNIISAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 197 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 276
Cdd:PRK05586 71 VLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 277 ilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGS----PIFVMRLAK 352
Cdd:PRK05586 135 ----------EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 353 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 432
Cdd:PRK05586 205 NPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 433 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspwgdapidfensahvpcpRGHVIAARITS 511
Cdd:PRK05586 285 YFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLsIKQEDIKI-----------------------NGHSIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 512 ENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVE 591
Cdd:PRK05586 342 EDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEG-VNTNID 420
|
490 500
....*....|....*....|...
gi 1958660710 592 YLIKLLETESFQLNRIDTGWLDR 614
Cdd:PRK05586 421 FQFIILEDEEFIKGTYDTSFIEK 443
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
118-615 |
9.31e-89 |
|
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including characterized members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae. The allophanate hydrolase domain of the yeast enzyme is not included in this model and is represented by an adjacent gene in Oleomonas sagaranensis. The fusion of urea carboxylase and allophanate hydrolase is designated urea amidolyase. The enzyme from Oleomonas sagaranensis was shown to be highly active on acetamide and formamide as well as urea. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 274264 [Multi-domain] Cd Length: 1201 Bit Score: 317.74 E-value: 9.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 118 EKVLIANNGIAAVKCMRSIRRWsyemfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGANNNNYANVELILDIAK 197
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRM---------GIRSVAVYSDAD--AASQHVLDADEAVCLGGAPAAESYLDIDKILAAAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 198 RIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSGLrvdwqendfskri 277
Cdd:TIGR02712 71 KTGAQAIHPGYGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLP--GTGL------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 278 lnvpqdlyekgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLF----RQVQAEVPGSPIFVMRLAKQ 353
Cdd:TIGR02712 136 ------------LSSLDEALEAAKEIGYPVMLKSTAGGGGIGMQKCDSAAELAEAFetvkRLGESFFGDAGVFLERFVEN 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 354 SRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLY-SQDGSF 432
Cdd:TIGR02712 204 ARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEETPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYdEARDEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 433 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAmgiplfrikdirmmygvspwGDAPIDFENSAHVPCPRGHVIAARITSE 512
Cdd:TIGR02712 284 YFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIA--------------------AGELPDFASLNISLTPRGAAIEARVYAE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 513 NPDEGFKPSSGTVQELNFRSNKNVWGYfsVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVEY 592
Cdd:TIGR02712 344 NPAKNFQPSPGLLTDVQFPDDVRVDTW--VETGTEVSPEYDPMLAKIIVHGSDREDAILKLHQALAETRVYG-IETNLDY 420
|
490 500
....*....|....*....|...
gi 1958660710 593 LIKLLETESFQLNRIDTGWLDRL 615
Cdd:TIGR02712 421 LRSILSSETFRSAQVSTRTLNSF 443
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
119-613 |
3.22e-86 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 309.06 E-value: 3.22e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 119 KVLIANNGIAAVKCMRSIrrwsyemfrNERAIRFVVMVTPED------LKANAEY-IKMADHYVPVpggannNNYANVEL 191
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 192 ILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqen 271
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 272 dfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGS----PIFV 347
Cdd:TIGR01235 135 ---------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVYV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 348 MRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYS 427
Cdd:TIGR01235 200 EKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 428 QDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-------FRIKDIRMmygvspwgdapidfensahvpcp 500
Cdd:TIGR01235 280 NDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLptpqlgvPNQEDIRT----------------------- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 501 RGHVIAARITSENPDEGFKPSSGTVQElnFRSNknvwGYFSVAAAGG-------LHEFADSQFGHCFSWGENREEAISNM 573
Cdd:TIGR01235 337 NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAKM 410
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1958660710 574 VVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD 613
Cdd:TIGR01235 411 DRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
116-613 |
1.32e-85 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 289.69 E-value: 1.32e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 116 VIEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPV---PGGANNNNYANVELi 192
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACA---------EMGIRSVAIYSEAD--RHALHVKRADEAYSIgadPLAGYLNPRRLVNL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 193 ldiAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqend 272
Cdd:PRK07178 69 ---AVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGS------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 273 fskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVM 348
Cdd:PRK07178 134 --------------EGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafGSAeVFLE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 349 RLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQ 428
Cdd:PRK07178 200 KCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 429 DGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspwgdapidfensahvpcpRGHVIAA 507
Cdd:PRK07178 280 DGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH-----------------------RGFALQF 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 508 RITSENPDEGFKPSSGTVQElnfrsnknvwgYFSVAAAG---------GLH--EFADSQFGHCFSWGENREEAISNMVVA 576
Cdd:PRK07178 337 RINAEDPKNDFLPSFGKITR-----------YYAPGGPGvrtdtaiytGYTipPYYDSMCAKLIVWALTWEEALDRGRRA 405
|
490 500 510
....*....|....*....|....*....|....*..
gi 1958660710 577 LKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD 613
Cdd:PRK07178 406 LDDMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVE 441
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
117-636 |
3.43e-69 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 242.03 E-value: 3.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 117 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVpGGANNNNYANVELILDIA 196
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACR---------DLHIKSVAIYTEPD--RECLHVKIADEAYRI-GTDPIKGYLDVKRIVEIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 197 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 276
Cdd:PRK08463 70 KACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGT---------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 277 ilnvpqdlyEKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLF----RQVQAEVPGSPIFVMRLAK 352
Cdd:PRK08463 134 ---------EKLNSESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFesckREALAYFNNDEVFMEKYVV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 353 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 432
Cdd:PRK08463 205 NPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 433 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMG-IPLFRIKDIRmmygvspwgdapidfensahvpcPRGHVIAARITS 511
Cdd:PRK08463 285 YFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGeILDLEQSDIK-----------------------PRGFAIEARITA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 512 ENPDEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGd 585
Cdd:PRK08463 342 ENVWKNFIPSPGKITEYypalgpSVRVDSHIYKDYTIPP------YYDSMLAKLIVKATSYDLAVNKLERALKEFVIDG- 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958660710 586 FRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQA------ERPDTMLGVVCGAL 636
Cdd:PRK08463 415 IRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKtedrhqENKEEVIAAIAAAL 471
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
288-469 |
8.83e-62 |
|
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: 210.62 E-value: 8.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 288 GYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSP----IFVMRLAKQSRHLEVQILA 363
Cdd:pfam02786 22 GPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 364 DQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQD-GSFYFLELNPRLQ 442
Cdd:pfam02786 102 DAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsGEYYFIEMNTRLQ 181
|
170 180
....*....|....*....|....*..
gi 1958660710 443 VEHPCTEMVADVNLPAAQLQIAMGIPL 469
Cdd:pfam02786 182 VEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
189-470 |
3.08e-43 |
|
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: 159.65 E-value: 3.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 189 VELILDIAKRIPVQAVWAGWGHASEnpKLPELLLKNGIAfmGPPSQAMWALGDKIASSIVAQTAGIPTlPWSGSglrvdw 268
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVE--TAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFAL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 269 qendfskrilnvpqdlyekgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEV----PGSP 344
Cdd:COG0439 75 ---------------------VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNGE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 345 IFVMRLAkQSRHLEVQILADQyGNAISlfgrdCSVQRRHQK---IIE---EAPAAIaTPAVFEHMEQCAVKLAKMVGYV- 417
Cdd:COG0439 134 VLVEEFL-EGREYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPL-PEELRAEIGELVARALRALGYRr 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958660710 418 SAGTVEYLYSQDGSFYFLELNPRLQVEH--PCTEMVADVNLPAAQLQIAMGIPLF 470
Cdd:COG0439 206 GAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEPRI 260
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
117-235 |
5.04e-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: 133.00 E-value: 5.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 117 IEKVLIANNGIAAVKCMRSIRRWsyemfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGANNNNYANVELILDIA 196
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACREL---------GIRTVAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAA 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958660710 197 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQA 235
Cdd:pfam00289 70 KETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
507-613 |
2.99e-32 |
|
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: 122.14 E-value: 2.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 507 ARITSENPDEGFKPSSGTVQELNFRSNKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 584
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 1958660710 585 dFRTTVEYLIKLLETESFQLNRIDTGWLD 613
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
507-614 |
1.33e-29 |
|
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: 114.51 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 507 ARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 586
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*...
gi 1958660710 587 RTTVEYLIKLLETESFQLNRIDTGWLDR 614
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1655-1986 |
5.14e-21 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 99.33 E-value: 5.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1655 EIGM-VAWKMSLKSPEYP-----------DGRDVIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVAANSGAR 1722
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPgdgvvtgigtvDGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1723 IGLAEEIRHMFhvawvdsedpykgykylyltpqdykrvsalnsvhcehvedeGESRYKitdiigkeeglgaeNLRGSGMI 1802
Cdd:COG4799 131 LQEGVESFAGY-----------------------------------------GRIFYR--------------NARSSGGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1803 AgesslaydeiiTISLVTCRAIGIGAYLVRLGQRTIQVE-NSHLILTGAGALNKVLGREVytSNNQLGGIQiMHN--NGV 1879
Cdd:COG4799 156 P-----------QISVIMGPCAAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvSGV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1880 THCTVCDDFEGVFTVLHWLSYMPKNVHSSVPLLNSKDP---IDRIIEFVPT--KAPYDPRWMLAGrphptqkgqwlsgFF 1954
Cdd:COG4799 222 ADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPPardPEELYGIVPEdpRKPYDMREVIAR-------------LV 288
|
330 340 350
....*....|....*....|....*....|..
gi 1958660710 1955 DYGSFSEIMQPWAQTVVVGRARLGGIPVGVVA 1986
Cdd:COG4799 289 DGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA 320
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
752-817 |
2.07e-17 |
|
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: 78.41 E-value: 2.07e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958660710 752 VMRSPSAGKLI-----QYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRP-GAALDPGCVIAKM 817
Cdd:pfam00364 2 EIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
754-817 |
8.95e-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: 67.83 E-value: 8.95e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958660710 754 RSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVK-RPGAALDPGCVIAKM 817
Cdd:cd06850 3 TAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
189-476 |
1.45e-12 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 71.88 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 189 VELILDIAKRIPVQAVWA---GWGHA-SEN-PKLPElllknGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTlPWSGsg 263
Cdd:COG3919 65 VDALLELAERHGPDVLIPtgdEYVELlSRHrDELEE-----HYRLPYPDADLLDRLLDKERFYELAEELGVPV-PKTV-- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 264 lrvdwqendfskrilnvpqdlyekgYVKDVDDGLKAAEEVGYPVMIKASEG--------GGGKGIRKVNNADDFPNLFRQ 335
Cdd:COG3919 137 -------------------------VLDSADDLDALAEDLGFPVVVKPADSvgydelsfPGKKKVFYVDDREELLALLRR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 336 ---------VQAEVPGSpifvmrlakQSRHLEVQILADQYGNAISLFGrdcsvqrrHQKIIEeAPAAIATPAVFEH---- 402
Cdd:COG3919 192 iaaagyeliVQEYIPGD---------DGEMRGLTAYVDRDGEVVATFT--------GRKLRH-YPPAGGNSAARESvddp 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958660710 403 -MEQCAVKLAKMVGYVSAGTVEYLY-SQDGSFYFLELNPRLQVEHPCTEmVADVNLPAAQLQIAMGIPLFRIKDIR 476
Cdd:COG3919 254 eLEEAARRLLEALGYHGFANVEFKRdPRDGEYKLIEINPRFWRSLYLAT-AAGVNFPYLLYDDAVGRPLEPVPAYR 328
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
273-470 |
4.54e-09 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 61.94 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 273 FSKRI--LNVPQDlyEKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRL 350
Cdd:TIGR01369 673 FSELLdeLGIPQP--KWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKY 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 351 AKQSRHLEVQILADqyGNAISLFGrdcsvQRRHqkiIEEA-----------PAAIATPAVFEHMEQCAVKLAKMVGYVSA 419
Cdd:TIGR01369 751 LEDAVEVDVDAVSD--GEEVLIPG-----IMEH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGL 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958660710 420 GTVEYLYSqDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLF 470
Cdd:TIGR01369 821 MNIQFAVK-DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLE 870
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
288-440 |
9.80e-09 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 60.95 E-value: 9.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 288 GYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDfpnLFRQVQAEV---PGSPIFVMRLAKQSRHLEVQILAD 364
Cdd:PLN02735 721 GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDK---LKTYLETAVevdPERPVLVDKYLSDATEIDVDALAD 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 365 QYGNAISlfgrdCSVQRRhqkiIEEA-----------PAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFY 433
Cdd:PLN02735 798 SEGNVVI-----GGIMEH----IEQAgvhsgdsacslPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVY 868
|
....*..
gi 1958660710 434 FLELNPR 440
Cdd:PLN02735 869 IIEANPR 875
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
289-440 |
1.26e-07 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 53.41 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 289 YVKDVDDGLKAAEEVGYPVMIKASEGG-GGKGIRKVNNADDFPnlfrQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYG 367
Cdd:pfam02222 12 AAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLP----QAWEELGDGPVIVEEFVPFDRELSVLVVRSVDG 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958660710 368 NAISlfgrdCS-VQRRHQK---IIEEAPAAIaTPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPR 440
Cdd:pfam02222 88 ETAF-----YPvVETIQEDgicRLSVAPARV-PQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLINELAPR 158
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
288-440 |
2.87e-07 |
|
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: 55.65 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 288 GYVKDVDDGLKAAEEVGYPVMIKASE--GGGGKGIrkVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEVQILADQ 365
Cdd:COG0458 133 GTATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 366 YGNAISLfgrdCSVQrrHqkiIEEA-----------PAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYsQDGSFYF 434
Cdd:COG0458 211 EDNVIIV----GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAV-DDGRVYV 280
|
....*.
gi 1958660710 435 LELNPR 440
Cdd:COG0458 281 IEVNPR 286
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
273-441 |
4.84e-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: 55.39 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 273 FSKRILNVPQDLYEKGYVKDVDDGLKAAEEVGYPVMIKASE--GGGGKGIrkVNNADDFPNLFRQVQAEVPGSPIFVMRL 350
Cdd:TIGR01369 131 FREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSASPINQVLVEKS 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 351 AKQSRHLEVQILADQYGNAISLfgrdCSVQR-----RHQ-KIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEY 424
Cdd:TIGR01369 209 LAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHTgDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQF 284
|
170
....*....|....*...
gi 1958660710 425 -LYSQDGSFYFLELNPRL 441
Cdd:TIGR01369 285 aLNPDSGRYYVIEVNPRV 302
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
299-467 |
2.37e-06 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 52.23 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 299 AAEEVGYPVMIKASEGGGGKGIRKVNNAD-DFPNLFrqVQAEVPGSPIfvmrlakqSrhleVQILADqygnaislfGRDC 377
Cdd:COG2232 133 EPPPDPGPWLVKPIGGAGGWHIRPADSEApPAPGRY--FQRYVEGTPA--------S----VLFLAD---------GSDA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 378 SVQRRHQKIIEEAPAA------IATPAVFEH-----MEQCAVKLAKMVGYVSAGTVEYLYSQDGsFYFLELNPRLQVEHP 446
Cdd:COG2232 190 RVLGFNRQLIGPAGERpfryggNIGPLALPPalaeeMRAIAEALVAALGLVGLNGVDFILDGDG-PYVLEVNPRPQASLD 268
|
170 180
....*....|....*....|.
gi 1958660710 447 CTEMVADVNLPAAQLQIAMGI 467
Cdd:COG2232 269 LYEDATGGNLFDAHLRACRGE 289
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
273-440 |
8.73e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 50.27 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 273 FSKRILNVPQDlYEKGYVKDVDDGLkAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQ-----VQAEVPGSPIfv 347
Cdd:PRK12767 119 LKENGIPTPKS-YLPESLEDFKAAL-AKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYvpnliIQEFIEGQEY-- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 348 mrlakqsrhlEVQILADQYGNAISLFGRdcsvqRRHQKIIEEAPAAIAT--PAVFEHMEQCAVKLakmvGYVSAGTVEYL 425
Cdd:PRK12767 195 ----------TVDVLCDLNGEVISIVPR-----KRIEVRAGETSKGVTVkdPELFKLAERLAEAL----GARGPLNIQCF 255
|
170
....*....|....*
gi 1958660710 426 YSqDGSFYFLELNPR 440
Cdd:PRK12767 256 VT-DGEPYLFEINPR 269
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
238-334 |
1.32e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 49.34 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 238 ALG-DKIASSIVAQTAGIPTLPWsgsglrvdwqendfskRILNVPQDLYEkgyvkdvddglkAAEEVGYPVMIKASEGGG 316
Cdd:PRK01372 94 ALAmDKLRTKLVWQAAGLPTPPW----------------IVLTREEDLLA------------AIDKLGLPLVVKPAREGS 145
|
90
....*....|....*...
gi 1958660710 317 GKGIRKVNNADDFPNLFR 334
Cdd:PRK01372 146 SVGVSKVKEEDELQAALE 163
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
300-442 |
1.97e-05 |
|
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: 46.99 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 300 AEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQ--VQAEVPGSPIFVMRLAKQSRHLEVQIlADQY-GNAISLFGRD 376
Cdd:pfam02655 27 LLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIENvlVQEFIEGEPLSVSLLSDGEKALPLSV-NRQYiDNGGSGFVYA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 377 -CSVQRRH---QKIIEEAPAAIAtpavfehmeqcavKLAKMVGYVSagtVEYLYSqDGSFYFLELNPRLQ 442
Cdd:pfam02655 106 gNVTPSRTelkEEIIELAEEVVE-------------CLPGLRGYVG---VDLVLK-DNEPYVIEVNPRIT 158
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
250-439 |
7.59e-05 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 46.16 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 250 QTAGIPTLPWSGSgLRVDWQENdfskrilnvPQDLYEKgyvkdvddglkAAEEVGYPVMIKASEGGGGKGIRKVNNAD-- 327
Cdd:pfam07478 3 KAAGLPVVPFVTF-TRADWKLN---------PKEWCAQ-----------VEEALGYPVFVKPARLGSSVGVSKVESREel 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 328 -DFPNLFRQVQAEVpgspifVMRLAKQSRHLEVQILADQYGNAISLfGR---DCSVQRRHQKIIEEA-----PAAIaTPA 398
Cdd:pfam07478 62 qAAIEEAFQYDEKV------LVEEGIEGREIECAVLGNEDPEVSPV-GEivpSGGFYDYEAKYIDDSaqivvPADL-EEE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958660710 399 VFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNP 439
Cdd:pfam07478 134 QEEQIQELALKAYKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
278-440 |
1.22e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 47.66 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 278 LNVPQDLYEKgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRqvQAEVPGSPIFVMRL--AKQsr 355
Cdd:PRK12815 681 LGLPHVPGLT--ATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLA--ENASQLYPILIDQFidGKE-- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 356 hLEVQILADqyGNAISLFGrdcsvqrrhqkI---IEEA-----------PAAIATPAVFEHMEQCAVKLAKMVGYVSAGT 421
Cdd:PRK12815 755 -YEVDAISD--GEDVTIPG-----------IiehIEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMN 820
|
170
....*....|....*....
gi 1958660710 422 VEYLYsQDGSFYFLELNPR 440
Cdd:PRK12815 821 IQFVL-ANDEIYVLEVNPR 838
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
290-440 |
3.35e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 45.53 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 290 VKDVDDGLKAAEEVGYPVMIKASEGG-GGKGIRKVNNADDFPNLFRQVQAE-------VPgspiFVMrlakqsrhlEVQI 361
Cdd:PRK06019 121 VDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEAAWALLGSVpcileefVP----FER---------EVSV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 362 LAdqygnAISLFGRDCS---VQRRHQKII---EEAPAAIaTPAVFEHMEQCAVKLAKMVGYVsaGT--VEYLYSQDGSFY 433
Cdd:PRK06019 188 IV-----ARGRDGEVVFyplVENVHRNGIlrtSIAPARI-SAELQAQAEEIASRIAEELDYV--GVlaVEFFVTGDGELL 259
|
....*..
gi 1958660710 434 FLELNPR 440
Cdd:PRK06019 260 VNEIAPR 266
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
232-459 |
3.58e-04 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 44.93 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 232 PSQAMWALGDKIASSIVAQTAGIPTlpwsgsglrvdwqendfskrilnvPQDLYekgyVKDVDDGLKAAEEVGYPVMIKA 311
Cdd:COG0189 87 DPEAIRRARDKLFTLQLLARAGIPV------------------------PPTLV----TRDPDDLRAFLEELGGPVVLKP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 312 SEGGGGKGIRKVNNADDFPNLFRQVQaEVPGSPIFVMRLAKQSRHLEVQILadqygnaisLFGRDC--SVQRRHQK---I 386
Cdd:COG0189 139 LDGSGGRGVFLVEDEDALESILEALT-ELGSEPVLVQEFIPEEDGRDIRVL---------VVGGEPvaAIRRIPAEgefR 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958660710 387 IEEAPAAIATPAVF-EHMEQCAVKLAKMVGYVSAGtVEYLYSQDGsFYFLELNPRLQVEHpcTEMVADVNLPAA 459
Cdd:COG0189 209 TNLARGGRAEPVELtDEERELALRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVTPGFRG--LERATGVDIAEA 278
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1805-2067 |
4.28e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 45.57 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1805 ESSLAYDEIITISLVTCRAIGIGAYLVRLGQRTIQV-ENSHLILTGAGALNKVLGREVytSNNQLGGIQImhnngvtHCT 1883
Cdd:PLN02820 198 QARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVkGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-------HCK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1884 ---VCDDF-----------EGVFTVLHWLSYMPKNVHSSVPLLNSKDPIDRIIEF---VPT--KAPYDPRWMLAGrphpt 1944
Cdd:PLN02820 269 vsgVSDHFaqdelhalaigRNIVKNLHLAAKQGMENTLGSKNPEYKEPLYDVKELrgiVPAdhKQSFDVRSVIAR----- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660710 1945 qkgqwlsgFFDYGSFSEIMQPWAQTVVVGRARLGGIPVGVVAvetrtvelsvpadpanldseakiiqqAGQVWFPDSAFK 2024
Cdd:PLN02820 344 --------IVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALK 389
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958660710 2025 TYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIV 2067
Cdd:PLN02820 390 GAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMV 432
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
269-320 |
6.30e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.15 E-value: 6.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958660710 269 QENDFSKRILN-----VPqdlyeKGY-VKDVDDGLKAAEEVGYPVMIKASEGGGGKGI 320
Cdd:PRK14016 213 CDKELTKRLLAaagvpVP-----EGRvVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGV 265
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
288-329 |
2.18e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 43.55 E-value: 2.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1958660710 288 GYVKDVDDGLKAAEEVGYPVMIKAS--EGGGGKGIrkVNNADDF 329
Cdd:PRK05294 147 GIAHSMEEALEVAEEIGYPVIIRPSftLGGTGGGI--AYNEEEL 188
|
|
| |
