|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
857-1598 |
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: 1008.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 857 LDNPSKVQQAELHTGSLPRIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLpdpffSSKVKDWVERLMKTLRDPSLPLLEL 936
Cdd:pfam08326 2 LDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLEW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 937 QDIMTSVSGRIPPNVEKSIKKEMAQYASNitsvLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGI 1016
Cdd:pfam08326 77 QEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1017 RGHMKAVVMDLLRQYLRVETQFQ--NGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGR---DPT 1091
Cdd:pfam08326 153 KGHEYSVFASLLEEYYDVEKLFSggNVREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVSN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1092 LTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCIENLQKLILS 1163
Cdd:pfam08326 233 VAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELIDS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1164 ETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRMS---FSSNLNHYGM 1240
Cdd:pfam08326 313 KYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGsplSPSSDSSPPF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1241 THVASVSD-VLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSPPQSPTFPEaghtslydedkvpRDEPIHILN 1319
Cdd:pfam08326 393 KRIASVSDlSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESGESNS-------------SDEPINVLN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1320 VAIKTDCDIE-DDRLAAMFREFTQQNKATLVDHGIRRLTFLVAQKDfrkqvnyevdrrfhREFPKFFTFRARDKFEEDRI 1398
Cdd:pfam08326 460 VAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKD--------------GQYPKYFTFRGPDNYEEDPI 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1399 YRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVgtevTDYRFFVRAIIRHSDLVTKEASFEYLQNEGERL 1478
Cdd:pfam08326 526 IRHIEPALAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRDDIPTAEYLISEAERL 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1479 LLEAMDELEVAfNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTPTGKAIPIR 1558
Cdd:pfam08326 602 LNDILDALEVA-SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGPPIPLR 680
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 578830806 1559 LFLTNESGYYLDISLYKEVTDSRtAQIMFQAYGdKQGPLH 1598
Cdd:pfam08326 681 LVITNVSGYVVKVELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1698-2246 |
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: 615.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1698 PEYPEGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEgIPRIYVSANSGARIGLAEEIRHMFHVAWVDPEDPYKGY 1777
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1778 RylyLTPQDYKRVSAlnsvhcehvedeGESRYKITDIIGKEEGIGPENLRGSGMIAGESSLAYNEIITISLVTCRAIGIG 1857
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1858 AYLVRLGQRTIQVEN-SHLILTGAGALNKVLGrEVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVH 1936
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1937 S---SVPLLNSKDPIDR---IIEFVPT--KTPYDPRWMLAGRphptqkgqwlsgfFDYGSFSEIMQPWAQTVVVGRARLG 2008
Cdd:pfam01039 224 NnrePVPIVPTKDPPDRdapLVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 2009 GIPVGVVAVETRtvelsipadpanldseakiiQQAGqVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQ 2088
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 2089 VLKFGAYIVDGLRECCQPVLVYIPPqaELRGGSWVVIDSSINPRHMeMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRR 2168
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578830806 2169 VDPvyihlaerlgtpelstaeRKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRtFFYW 2246
Cdd:pfam01039 427 KDL------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
155-664 |
5.58e-139 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 442.92 E-value: 5.58e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 155 IEKVLIANNGIAAVKCMRSIRrwsyEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 234
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 235 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 314
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 315 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 390
Cdd:COG4770 135 ----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 391 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 470
Cdd:COG4770 205 RPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 471 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRmmygvspwgdspidfedsahvpcPRGHVIAARITS 549
Cdd:COG4770 285 YFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLpFTQEDIK-----------------------LRGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 550 ENPDEGFKPSSGTVQELNF------------RSNKNVWGYFsvaaagglhefaDSQFGHCFSWGENREEAISNMVVALKE 617
Cdd:COG4770 342 EDPARGFLPSPGTITRLRPpggpgvrvdsgvYEGYEIPPYY------------DSMIAKLIVWGPDREEAIARMRRALAE 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 578830806 618 LSIRGdFRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQAERPD 664
Cdd:COG4770 410 FVIEG-VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
155-660 |
3.02e-116 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 377.22 E-value: 3.02e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 155 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 234
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 235 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSglrvdwqendfskr 314
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 315 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSPIFVM-RLAK 390
Cdd:PRK08591 135 ----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPGVYMeKYLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 391 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 470
Cdd:PRK08591 205 NPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 471 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARITS 549
Cdd:PRK08591 285 YFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLsIKQEDIVF-----------------------RGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 550 ENPDEGFKPSSGTVQelnfrsnknvwGYFsvaAAGGLH--------------EFADSQFGHCFSWGENREEAISNMVVAL 615
Cdd:PRK08591 342 EDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRAL 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 578830806 616 KELSIRGdFRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQA 660
Cdd:PRK08591 408 SEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
155-656 |
2.71e-105 |
|
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: 345.59 E-value: 2.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 155 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 234
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACK---------ELGIKTVAVHSTAD--RDALHVLLADEAVCIGPAPSAKSYLNIPNIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 235 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 314
Cdd:TIGR00514 71 EITGADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 315 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 390
Cdd:TIGR00514 135 ----------DGLVEDEEENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKaafGNDgVYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 391 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 470
Cdd:TIGR00514 205 NPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 471 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLyrikdirmmygvsPWGDSPIDFedsahvpcpRGHVIAARITSE 550
Cdd:TIGR00514 285 YFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL-------------SLKQEDVVV---------RGHAIECRINAE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 551 NPDEGFKPSSGTVQE------LNFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 624
Cdd:TIGR00514 343 DPIKTFLPSPGRITRylppggPGVRWDSHVYSGYTVPP------YYDSMIGKLITYGKTREVAIARMKRALSEFIIDG-I 415
|
490 500 510
....*....|....*....|....*....|..
gi 578830806 625 RTTVEYLIKLLETESFQMNRIDTGWLDRLIAE 656
Cdd:TIGR00514 416 KTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
316-507 |
1.24e-61 |
|
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: 210.24 E-value: 1.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 316 LNVPQELYEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSP----IFVMRLAKQ 391
Cdd:pfam02786 12 AGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 392 SRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQD-GSF 470
Cdd:pfam02786 92 PKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsGEY 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 578830806 471 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL 507
Cdd:pfam02786 172 YFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
545-651 |
1.61e-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: 122.91 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 545 ARITSENPDEGFKPSSGTVQELNFRSNKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 622
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 578830806 623 dFRTTVEYLIKLLETESFQMNRIDTGWLD 651
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1685-2016 |
2.22e-19 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 94.32 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1685 EIGM-VAWKMTFKSPEYP-----------EGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGAR 1752
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPgdgvvtgigtvDGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1753 IGLAEEIRHMFhvawvdpedpykgyrylyltpqdykrvsalnsvhcehvedeGESRYKitdiigkeegigpeNLRGSGMI 1832
Cdd:COG4799 131 LQEGVESFAGY-----------------------------------------GRIFYR--------------NARSSGGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1833 AgesslayneiiTISLVTCRAIGIGAYLVRLGQRTIQVE-NSHLILTGAGALNKVLGREVytSNNQLGGIQiMHN--NGV 1909
Cdd:COG4799 156 P-----------QISVIMGPCAAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvSGV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1910 THCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDP---IDRIIEFVPT--KTPYDPRWMLAGrphptqkgqwlsgFF 1984
Cdd:COG4799 222 ADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPPardPEELYGIVPEdpRKPYDMREVIAR-------------LV 288
|
330 340 350
....*....|....*....|....*....|..
gi 578830806 1985 DYGSFSEIMQPWAQTVVVGRARLGGIPVGVVA 2016
Cdd:COG4799 289 DGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA 320
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
790-855 |
1.92e-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: 78.80 E-value: 1.92e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578830806 790 VMRSPSAGKLI-----QYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRP-GAALDPGCVLAKM 855
Cdd:pfam00364 2 EIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
792-855 |
2.63e-14 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 69.37 E-value: 2.63e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578830806 792 RSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVK-RPGAALDPGCVLAKM 855
Cdd:cd06850 3 TAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1844-2097 |
4.81e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 45.18 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1844 ITISLVTCRAiGiGAYLVRLGQRTIQV-ENSHLILTGAGALNKVLGREVytSNNQLGGIQImhnngvtHCT---VCDDF- 1918
Cdd:PLN02820 209 IALVLGSCTA-G-GAYVPAMADESVIVkGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-------HCKvsgVSDHFa 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1919 ----------EGVFTVLHWLSYMPKSVHSSVPLLNSKDPIDRIIEF---VPT--KTPYDPRWMLAGrphptqkgqwlsgF 1983
Cdd:PLN02820 278 qdelhalaigRNIVKNLHLAAKQGMENTLGSKNPEYKEPLYDVKELrgiVPAdhKQSFDVRSVIAR-------------I 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1984 FDYGSFSEIMQPWAQTVVVGRARLGGIPVGVVAvetrtvelsipadpanldseakiiqqAGQVWFPDSAFKTYQAIKDFN 2063
Cdd:PLN02820 345 VDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALKGAHFIELCA 398
|
250 260 270
....*....|....*....|....*....|....
gi 578830806 2064 REGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIV 2097
Cdd:PLN02820 399 QRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMV 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 ... |
857-1598 |
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: 1008.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 857 LDNPSKVQQAELHTGSLPRIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLpdpffSSKVKDWVERLMKTLRDPSLPLLEL 936
Cdd:pfam08326 2 LDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLEW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 937 QDIMTSVSGRIPPNVEKSIKKEMAQYASNitsvLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGI 1016
Cdd:pfam08326 77 QEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1017 RGHMKAVVMDLLRQYLRVETQFQ--NGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGR---DPT 1091
Cdd:pfam08326 153 KGHEYSVFASLLEEYYDVEKLFSggNVREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVSN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1092 LTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCIENLQKLILS 1163
Cdd:pfam08326 233 VAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELIDS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1164 ETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRMS---FSSNLNHYGM 1240
Cdd:pfam08326 313 KYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGsplSPSSDSSPPF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1241 THVASVSD-VLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSPPQSPTFPEaghtslydedkvpRDEPIHILN 1319
Cdd:pfam08326 393 KRIASVSDlSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESGESNS-------------SDEPINVLN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1320 VAIKTDCDIE-DDRLAAMFREFTQQNKATLVDHGIRRLTFLVAQKDfrkqvnyevdrrfhREFPKFFTFRARDKFEEDRI 1398
Cdd:pfam08326 460 VAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKD--------------GQYPKYFTFRGPDNYEEDPI 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1399 YRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVgtevTDYRFFVRAIIRHSDLVTKEASFEYLQNEGERL 1478
Cdd:pfam08326 526 IRHIEPALAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRDDIPTAEYLISEAERL 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1479 LLEAMDELEVAfNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTPTGKAIPIR 1558
Cdd:pfam08326 602 LNDILDALEVA-SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGPPIPLR 680
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 578830806 1559 LFLTNESGYYLDISLYKEVTDSRtAQIMFQAYGdKQGPLH 1598
Cdd:pfam08326 681 LVITNVSGYVVKVELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1698-2246 |
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: 615.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1698 PEYPEGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEgIPRIYVSANSGARIGLAEEIRHMFHVAWVDPEDPYKGY 1777
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1778 RylyLTPQDYKRVSAlnsvhcehvedeGESRYKITDIIGKEEGIGPENLRGSGMIAGESSLAYNEIITISLVTCRAIGIG 1857
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1858 AYLVRLGQRTIQVEN-SHLILTGAGALNKVLGrEVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVH 1936
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1937 S---SVPLLNSKDPIDR---IIEFVPT--KTPYDPRWMLAGRphptqkgqwlsgfFDYGSFSEIMQPWAQTVVVGRARLG 2008
Cdd:pfam01039 224 NnrePVPIVPTKDPPDRdapLVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 2009 GIPVGVVAVETRtvelsipadpanldseakiiQQAGqVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQ 2088
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 2089 VLKFGAYIVDGLRECCQPVLVYIPPqaELRGGSWVVIDSSINPRHMeMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRR 2168
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578830806 2169 VDPvyihlaerlgtpelstaeRKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRtFFYW 2246
Cdd:pfam01039 427 KDL------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
155-664 |
5.58e-139 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 442.92 E-value: 5.58e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 155 IEKVLIANNGIAAVKCMRSIRrwsyEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 234
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 235 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 314
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 315 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 390
Cdd:COG4770 135 ----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 391 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 470
Cdd:COG4770 205 RPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 471 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRmmygvspwgdspidfedsahvpcPRGHVIAARITS 549
Cdd:COG4770 285 YFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLpFTQEDIK-----------------------LRGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 550 ENPDEGFKPSSGTVQELNF------------RSNKNVWGYFsvaaagglhefaDSQFGHCFSWGENREEAISNMVVALKE 617
Cdd:COG4770 342 EDPARGFLPSPGTITRLRPpggpgvrvdsgvYEGYEIPPYY------------DSMIAKLIVWGPDREEAIARMRRALAE 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 578830806 618 LSIRGdFRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQAERPD 664
Cdd:COG4770 410 FVIEG-VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
155-660 |
3.02e-116 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 377.22 E-value: 3.02e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 155 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 234
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 235 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSglrvdwqendfskr 314
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 315 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSPIFVM-RLAK 390
Cdd:PRK08591 135 ----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPGVYMeKYLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 391 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 470
Cdd:PRK08591 205 NPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 471 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARITS 549
Cdd:PRK08591 285 YFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLsIKQEDIVF-----------------------RGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 550 ENPDEGFKPSSGTVQelnfrsnknvwGYFsvaAAGGLH--------------EFADSQFGHCFSWGENREEAISNMVVAL 615
Cdd:PRK08591 342 EDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRAL 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 578830806 616 KELSIRGdFRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQA 660
Cdd:PRK08591 408 SEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
156-659 |
6.78e-107 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 351.98 E-value: 6.78e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 156 EKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIAK 235
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACR---------ELGIKTVAVYSEAD--KNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 236 RIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGlrvdwqendfskri 315
Cdd:PRK08654 72 KAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEG-------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 316 lnvpqelyekgyVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLF---RQVQAEVPGSP-IFVMRLAKQ 391
Cdd:PRK08654 138 ------------IEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIestQSIAQSAFGDStVFIEKYLEK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 392 SRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSqDGSFY 471
Cdd:PRK08654 206 PRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 472 FLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARITSE 550
Cdd:PRK08654 285 FLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELsFKQEDITI-----------------------RGHAIECRINAE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 551 NPDEGFKPSSGTVQelnfrsnknvwGYFSVAAAG-----GLH------EFADSQFGHCFSWGENREEAISNMVVALKELS 619
Cdd:PRK08654 342 DPLNDFAPSPGKIK-----------RYRSPGGPGvrvdsGVHmgyeipPYYDSMISKLIVWGRTREEAIARMRRALYEYV 410
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 578830806 620 IRGdFRTTVEYLIKLLETESFQMNRIDTGWLD--RLIAEKVQ 659
Cdd:PRK08654 411 IVG-VKTNIPFHKAVMENENFVRGNLHTHFIEeeTTILEEMK 451
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
155-656 |
2.71e-105 |
|
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: 345.59 E-value: 2.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 155 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 234
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACK---------ELGIKTVAVHSTAD--RDALHVLLADEAVCIGPAPSAKSYLNIPNIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 235 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 314
Cdd:TIGR00514 71 EITGADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 315 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 390
Cdd:TIGR00514 135 ----------DGLVEDEEENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKaafGNDgVYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 391 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 470
Cdd:TIGR00514 205 NPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 471 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLyrikdirmmygvsPWGDSPIDFedsahvpcpRGHVIAARITSE 550
Cdd:TIGR00514 285 YFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL-------------SLKQEDVVV---------RGHAIECRINAE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 551 NPDEGFKPSSGTVQE------LNFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 624
Cdd:TIGR00514 343 DPIKTFLPSPGRITRylppggPGVRWDSHVYSGYTVPP------YYDSMIGKLITYGKTREVAIARMKRALSEFIIDG-I 415
|
490 500 510
....*....|....*....|....*....|..
gi 578830806 625 RTTVEYLIKLLETESFQMNRIDTGWLDRLIAE 656
Cdd:TIGR00514 416 KTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
153-651 |
4.89e-105 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 366.39 E-value: 4.89e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 153 KVIEKVLIANNGIAAVKCMRSIrrwsyemfrNERAIRFVVMVTPED------LKANAEYIkmadhyVPVPGGPNNNnYAN 226
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAA---------TELGIRTVAIYSEEDklslhrFKADEAYL------IGEGKHPVRA-YLD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 227 VELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGlrvdw 306
Cdd:PRK12999 67 IDEIIRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGP----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 307 qendfskrilnvpqelyekgyVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP- 382
Cdd:PRK12999 142 ---------------------IDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafGNDe 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 383 IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEY 462
Cdd:PRK12999 201 VYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 463 LYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLyrikdirmmygvspwgDSPIDFEDSAHVPCPRGHV 542
Cdd:PRK12999 281 LVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATL----------------HDLEIGIPSQEDIRLRGYA 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 543 IAARITSENPDEGFKPSSGTVQElnFRSNknvwGYFSV------AAAGGlhEFA---DSQFGHCFSWGENREEAISNMVV 613
Cdd:PRK12999 345 IQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVrldggnAFAGA--EITpyyDSLLVKLTAWGRTFEQAVARMRR 416
|
490 500 510
....*....|....*....|....*....|....*...
gi 578830806 614 ALKELSIRGdFRTTVEYLIKLLETESFQMNRIDTGWLD 651
Cdd:PRK12999 417 ALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFID 453
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
155-652 |
8.49e-105 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 343.93 E-value: 8.49e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 155 IEKVLIANNGIAAVKCMRSIRRWsyemfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 234
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKL---------GIRTVAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 235 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGLrvdwqendfskr 314
Cdd:PRK06111 71 KKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNL------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 315 ilnvpqelyekgyvKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 390
Cdd:PRK06111 139 --------------EDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAAnffGNGeMYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 391 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 470
Cdd:PRK06111 205 DPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 471 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARITS 549
Cdd:PRK06111 285 YFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR-----------------------SGHAIEVRIYA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 550 ENPDEgFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVE 629
Cdd:PRK06111 342 EDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEG-IKTNIP 419
|
490 500
....*....|....*....|...
gi 578830806 630 YLIKLLETESFQMNRIDTGWLDR 652
Cdd:PRK06111 420 LLLQVLEDPVFKAGGYTTGFLTK 442
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
153-651 |
2.54e-100 |
|
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: 352.07 E-value: 2.54e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 153 KVIEKVLIANNG-IAavkcmrsIRrwsyeMFR--NERAIRFVVMVTPED------LKANAEY-IKMADHyvPVpggpnnN 222
Cdd:COG1038 2 KKIKKVLVANRGeIA-------IR-----VFRaaTELGIRTVAIYSEEDryslhrFKADEAYlIGEGKG--PV------D 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 223 NYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSgl 302
Cdd:COG1038 62 AYLDIEEIIRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP--GT-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 303 rvdwqendfskrilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP--- 379
Cdd:COG1038 138 ----------------------EGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaaf 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 380 GSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAG 458
Cdd:COG1038 196 GDDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 459 TVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLyrikdirmmygvspwGDSPIDFEDSAHVPCp 538
Cdd:COG1038 276 TVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSL---------------DDPEIGIPSQEDIRL- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 539 RGHVIAARITSENPDEGFKPSSGTVQElnFRSnknvwgyfsvaaAGGlhefadsqFG------HCFS------------- 599
Cdd:COG1038 340 NGYAIQCRITTEDPANNFMPDTGRITA--YRS------------AGG--------FGirldggNAYTgavitpyydsllv 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 578830806 600 ----WGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQMNRIDTGWLD 651
Cdd:COG1038 398 kvtaWGRTFEEAIRKMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFID 452
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
155-652 |
1.39e-96 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 320.15 E-value: 1.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 155 IEKVLIANNGIAAVKCMRSIRrwsyEMfrNERAIrfVVMVTPEDlkaNAEYIKMADHYVPVPGGPNNNNYANVELILDIA 234
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQ----EM--GKEAI--AIYSTADK---DALYLKYADAKICIGGAKSSESYLNIPAIISAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 235 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 314
Cdd:PRK08462 73 EIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGS---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 315 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGS----PIFVMRLAK 390
Cdd:PRK08462 137 ----------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAfgdgTMYMEKFIN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 391 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 470
Cdd:PRK08462 207 NPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 471 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARITSE 550
Cdd:PRK08462 287 YFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKL-----------------------KGHAIECRITAE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 551 NPdEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 624
Cdd:PRK08462 344 DP-KKFYPSPGKITKWiapggrNVRMDSHAYAGYVVPP------YYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEG-I 415
|
490 500
....*....|....*....|....*...
gi 578830806 625 RTTVEYLIKLLETESFQMNRIDTGWLDR 652
Cdd:PRK08462 416 KTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
155-660 |
4.65e-96 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 319.39 E-value: 4.65e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 155 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDLKANAeyIKMADHYVPVPGGPNNNNYANVELILDIA 234
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAAR---------ELGMRTVAACSDADRDSLA--ARMADEAVHIGPSHAAKSYLNPAAILAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 235 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 314
Cdd:PRK12833 74 RQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGS---------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 315 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 390
Cdd:PRK12833 138 ----------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQaafGDGgVYLERFIA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 391 QSRHLEVQILADQYgNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLY-SQDGS 469
Cdd:PRK12833 208 RARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFdDARGE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 470 FYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARIT 548
Cdd:PRK12833 287 FYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLrFAQGDIAL-----------------------RGAALECRIN 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 549 SENPDEGFKPSSGTVQELNF------RSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRG 622
Cdd:PRK12833 344 AEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYPGYRVPP------FYDSLLAKLIVHGEDRAAALARAARALRELRIDG 417
|
490 500 510
....*....|....*....|....*....|....*...
gi 578830806 623 dFRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQA 660
Cdd:PRK12833 418 -MKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAA 454
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
155-652 |
1.55e-95 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 317.42 E-value: 1.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 155 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 234
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACR---------EMGIETVAVYSEAD--KDALHVQLADEAVCIGPASSKDSYLNIQNIISAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 235 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 314
Cdd:PRK05586 71 VLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 315 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGS----PIFVMRLAK 390
Cdd:PRK05586 135 ----------EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 391 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 470
Cdd:PRK05586 205 NPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 471 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARITS 549
Cdd:PRK05586 285 YFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLsIKQEDIKI-----------------------NGHSIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 550 ENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVE 629
Cdd:PRK05586 342 EDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEG-VNTNID 420
|
490 500
....*....|....*....|...
gi 578830806 630 YLIKLLETESFQMNRIDTGWLDR 652
Cdd:PRK05586 421 FQFIILEDEEFIKGTYDTSFIEK 443
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
156-653 |
5.12e-92 |
|
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: 327.76 E-value: 5.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 156 EKVLIANNGIAAVKCMRSIRRWsyemfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIAK 235
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRM---------GIRSVAVYSDAD--AASQHVLDADEAVCLGGAPAAESYLDIDKILAAAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 236 RIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSGLrvdwqendfskri 315
Cdd:TIGR02712 71 KTGAQAIHPGYGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLP--GTGL------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 316 lnvpqelyekgyVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLF----RQVQAEVPGSPIFVMRLAKQ 391
Cdd:TIGR02712 136 ------------LSSLDEALEAAKEIGYPVMLKSTAGGGGIGMQKCDSAAELAEAFetvkRLGESFFGDAGVFLERFVEN 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 392 SRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLY-SQDGSF 470
Cdd:TIGR02712 204 ARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEETPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYdEARDEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 471 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAmgiplyrikdirmmygvspwGDSPIDFEDSAHVPCPRGHVIAARITSE 550
Cdd:TIGR02712 284 YFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIA--------------------AGELPDFASLNISLTPRGAAIEARVYAE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 551 NPDEGFKPSSGTVQELNFRSNKNVWGYfsVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVEY 630
Cdd:TIGR02712 344 NPAKNFQPSPGLLTDVQFPDDVRVDTW--VETGTEVSPEYDPMLAKIIVHGSDREDAILKLHQALAETRVYG-IETNLDY 420
|
490 500
....*....|....*....|...
gi 578830806 631 LIKLLETESFQMNRIDTGWLDRL 653
Cdd:TIGR02712 421 LRSILSSETFRSAQVSTRTLNSF 443
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
154-651 |
4.09e-89 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 299.71 E-value: 4.09e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 154 VIEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYV-----PVPGgpnnnnYANVE 228
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACA---------EMGIRSVAIYSEAD--RHALHVKRADEAYsigadPLAG------YLNPR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 229 LILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqe 308
Cdd:PRK07178 64 RLVNLAVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGS---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 309 ndfskrilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IF 384
Cdd:PRK07178 134 ----------------EGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafGSAeVF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 385 VMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLY 464
Cdd:PRK07178 198 LEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 465 SQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVI 543
Cdd:PRK07178 278 DADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH-----------------------RGFAL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 544 AARITSENPDEGFKPSSGTVQElnfrsnknvwgYFSVAAAG---------GLH--EFADSQFGHCFSWGENREEAISNMV 612
Cdd:PRK07178 335 QFRINAEDPKNDFLPSFGKITR-----------YYAPGGPGvrtdtaiytGYTipPYYDSMCAKLIVWALTWEEALDRGR 403
|
490 500 510
....*....|....*....|....*....|....*....
gi 578830806 613 VALKELSIRGdFRTTVEYLIKLLETESFQMNRIDTGWLD 651
Cdd:PRK07178 404 RALDDMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVE 441
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
157-651 |
9.63e-88 |
|
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: 313.69 E-value: 9.63e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 157 KVLIANNGIAAVKCMRSIrrwsyemfrNERAIRFVVMVTPED------LKANAEY-IKMADHYVPVpggpnnNNYANVEL 229
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 230 ILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqen 309
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 310 dfskrilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGS----PIFV 385
Cdd:TIGR01235 135 ---------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVYV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 386 MRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYS 465
Cdd:TIGR01235 200 EKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 466 QDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLyrikdirmmygvsPWGDSPIDFEDSAHVpcpRGHVIAA 545
Cdd:TIGR01235 280 NDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASL-------------PTPQLGVPNQEDIRT---NGYAIQC 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 546 RITSENPDEGFKPSSGTVQElnFRSNknvwGYFSVAAAGG-------LHEFADSQFGHCFSWGENREEAISNMVVALKEL 618
Cdd:TIGR01235 344 RVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAKMDRALREF 417
|
490 500 510
....*....|....*....|....*....|...
gi 578830806 619 SIRGdFRTTVEYLIKLLETESFQMNRIDTGWLD 651
Cdd:TIGR01235 418 RIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
155-674 |
1.77e-71 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 248.96 E-value: 1.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 155 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNnYANVELILDIA 234
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACR---------DLHIKSVAIYTEPD--RECLHVKIADEAYRIGTDPIKG-YLDVKRIVEIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 235 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 314
Cdd:PRK08463 70 KACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGT---------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 315 ilnvpqelyEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLF----RQVQAEVPGSPIFVMRLAK 390
Cdd:PRK08463 134 ---------EKLNSESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFesckREALAYFNNDEVFMEKYVV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 391 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 470
Cdd:PRK08463 205 NPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 471 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMG-IPLYRIKDIRmmygvspwgdspidfedsahvpcPRGHVIAARITS 549
Cdd:PRK08463 285 YFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGeILDLEQSDIK-----------------------PRGFAIEARITA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 550 ENPDEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGd 623
Cdd:PRK08463 342 ENVWKNFIPSPGKITEYypalgpSVRVDSHIYKDYTIPP------YYDSMLAKLIVKATSYDLAVNKLERALKEFVIDG- 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 578830806 624 FRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQA------ERPDTMLGVVCGAL 674
Cdd:PRK08463 415 IRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKtedrhqENKEEVIAAIAAAL 471
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
316-507 |
1.24e-61 |
|
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: 210.24 E-value: 1.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 316 LNVPQELYEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSP----IFVMRLAKQ 391
Cdd:pfam02786 12 AGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 392 SRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQD-GSF 470
Cdd:pfam02786 92 PKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsGEY 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 578830806 471 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL 507
Cdd:pfam02786 172 YFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
155-273 |
2.38e-43 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 153.80 E-value: 2.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 155 IEKVLIANNGIAAVKCMRSIRRWsyemfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 234
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACREL---------GIRTVAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAA 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 578830806 235 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQA 273
Cdd:pfam00289 70 KETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
227-506 |
6.18e-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: 158.50 E-value: 6.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 227 VELILDIAKRIPVQAVWAGWGHASEnpKLPELLLKNGIAfmGPPSQAMWALGDKIASSIVAQTAGIPTlPWSGSglrvdw 306
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVE--TAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFAL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 307 qendfskrilnvpqelyekgyVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEV----PGSP 382
Cdd:COG0439 75 ---------------------VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNGE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 383 IFVMRLAkQSRHLEVQILADQyGNAISlfgrdCSVQRRHQK---IIE---EAPATIaTPAVFEHMEQCAVKLAKMVGYV- 455
Cdd:COG0439 134 VLVEEFL-EGREYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPL-PEELRAEIGELVARALRALGYRr 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 578830806 456 SAGTVEYLYSQDGSFYFLELNPRLQVEH--PCTEMVADVNLPAAQLQIAMGIP 506
Cdd:COG0439 206 GAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
545-651 |
1.61e-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: 122.91 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 545 ARITSENPDEGFKPSSGTVQELNFRSNKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 622
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 578830806 623 dFRTTVEYLIKLLETESFQMNRIDTGWLD 651
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
545-652 |
5.48e-30 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 115.67 E-value: 5.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 545 ARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 624
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*...
gi 578830806 625 RTTVEYLIKLLETESFQMNRIDTGWLDR 652
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1685-2016 |
2.22e-19 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 94.32 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1685 EIGM-VAWKMTFKSPEYP-----------EGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGAR 1752
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPgdgvvtgigtvDGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1753 IGLAEEIRHMFhvawvdpedpykgyrylyltpqdykrvsalnsvhcehvedeGESRYKitdiigkeegigpeNLRGSGMI 1832
Cdd:COG4799 131 LQEGVESFAGY-----------------------------------------GRIFYR--------------NARSSGGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1833 AgesslayneiiTISLVTCRAIGIGAYLVRLGQRTIQVE-NSHLILTGAGALNKVLGREVytSNNQLGGIQiMHN--NGV 1909
Cdd:COG4799 156 P-----------QISVIMGPCAAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvSGV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1910 THCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDP---IDRIIEFVPT--KTPYDPRWMLAGrphptqkgqwlsgFF 1984
Cdd:COG4799 222 ADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPPardPEELYGIVPEdpRKPYDMREVIAR-------------LV 288
|
330 340 350
....*....|....*....|....*....|..
gi 578830806 1985 DYGSFSEIMQPWAQTVVVGRARLGGIPVGVVA 2016
Cdd:COG4799 289 DGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA 320
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
790-855 |
1.92e-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: 78.80 E-value: 1.92e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578830806 790 VMRSPSAGKLI-----QYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRP-GAALDPGCVLAKM 855
Cdd:pfam00364 2 EIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
792-855 |
2.63e-14 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 69.37 E-value: 2.63e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578830806 792 RSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVK-RPGAALDPGCVLAKM 855
Cdd:cd06850 3 TAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
209-514 |
2.89e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 77.28 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 209 ADHYVPVPGgPNNNNYANVELILDIAKRIPVQAVWA---GWGHA-SEN-PKLPElllknGIAFMGPPSQAMWALGDKIAS 283
Cdd:COG3919 48 VDEVVVVPD-PGDDPEAFVDALLELAERHGPDVLIPtgdEYVELlSRHrDELEE-----HYRLPYPDADLLDRLLDKERF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 284 SIVAQTAGIPtlpwsgsglrvdwqendfskrilnVPQELYekgyVKDVDDGLQAAEEVGYPVMIKASEG--------GGG 355
Cdd:COG3919 122 YELAEELGVP------------------------VPKTVV----LDSADDLDALAEDLGFPVVVKPADSvgydelsfPGK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 356 KGIRKVNNADDFPNLFRQ---------VQAEVPGSpifvmrlakQSRHLEVQILADQYGNAISLFGrdcsvqrrHQKIIE 426
Cdd:COG3919 174 KKVFYVDDREELLALLRRiaaagyeliVQEYIPGD---------DGEMRGLTAYVDRDGEVVATFT--------GRKLRH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 427 eAPATIATPAVFEH-----MEQCAVKLAKMVGYVSAGTVEYLY-SQDGSFYFLELNPRLQVEHPCTEmVADVNLPAAQLQ 500
Cdd:COG3919 237 -YPPAGGNSAARESvddpeLEEAARRLLEALGYHGFANVEFKRdPRDGEYKLIEINPRFWRSLYLAT-AAGVNFPYLLYD 314
|
330
....*....|....
gi 578830806 501 IAMGIPLYRIKDIR 514
Cdd:COG3919 315 DAVGRPLEPVPAYR 328
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
311-507 |
6.56e-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: 61.55 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 311 FSKRI--LNVPQElyEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRL 388
Cdd:TIGR01369 673 FSELLdeLGIPQP--KWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKY 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 389 AKQSRHLEVQILADqyGNAISLFGrdcsvQRRHqkiIEEA-----------PATIATPAVFEHMEQCAVKLAKMVGYVSA 457
Cdd:TIGR01369 751 LEDAVEVDVDAVSD--GEEVLIPG-----IMEH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGL 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578830806 458 GTVEYLYSqDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL 507
Cdd:TIGR01369 821 MNIQFAVK-DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
326-478 |
1.04e-08 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 60.95 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 326 GYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDfpnLFRQVQAEV---PGSPIFVMRLAKQSRHLEVQILAD 402
Cdd:PLN02735 721 GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDK---LKTYLETAVevdPERPVLVDKYLSDATEIDVDALAD 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 403 QYGNAI-----------SLFGRDCSVQRRHQKIIEEAPATI--ATPavfehmeqcavKLAKMVGYVSAGTVEYLYSQDGS 469
Cdd:PLN02735 798 SEGNVViggimehieqaGVHSGDSACSLPTQTIPSSCLATIrdWTT-----------KLAKRLNVCGLMNCQYAITPSGE 866
|
....*....
gi 578830806 470 FYFLELNPR 478
Cdd:PLN02735 867 VYIIEANPR 875
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
257-477 |
3.81e-08 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 57.42 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 257 ELLlknGIAFMGPPSQAMwALG-DKIASSIVAQTAGIPTLPWsgsglrvdwqendfskrilnvpqELYEKGYVKDVDdgl 335
Cdd:COG1181 76 ELL---GIPYTGSGVLAS-ALAmDKALTKRVLAAAGLPTPPY-----------------------VVLRRGELADLE--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 336 QAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNlfrqvqaevpgspifVMRLAKQSRHlevQILADQYgnaISlfGRD- 414
Cdd:COG1181 126 AIEEELGLPLFVKPAREGSSVGVSKVKNAEELAA---------------ALEEAFKYDD---KVLVEEF---ID--GREv 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 415 -CSV-QRRHQK---IIE----------EA-----------PATIaTPAVFEHMEQCAVKLAKMV---GYvsaGTVEYLYS 465
Cdd:COG1181 183 tVGVlGNGGPRalpPIEivpengfydyEAkytdggteyicPARL-PEELEERIQELALKAFRALgcrGY---ARVDFRLD 258
|
250
....*....|..
gi 578830806 466 QDGSFYFLELNP 477
Cdd:COG1181 259 EDGEPYLLEVNT 270
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
311-478 |
3.64e-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: 55.27 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 311 FSKRI--LNVPQElyEKGYVKDVDDGLQAAEEVGYPVMIKASE--GGGGKGIrkVNNADDFPNLFRQVQAEVPGSPIFVM 386
Cdd:COG0458 118 FKELLdkLGIPQP--KSGTATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLID 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 387 RLAKQSRHLEVQILADQYGNAISLfgrdCSVQrrHqkiIEEA-----------PATIATPAVFEHMEQCAVKLAKMVGYV 455
Cdd:COG0458 194 ESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVV 264
|
170 180
....*....|....*....|...
gi 578830806 456 SAGTVEYLYsQDGSFYFLELNPR 478
Cdd:COG0458 265 GLCNIQFAV-DDGRVYVIEVNPR 286
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
327-478 |
4.00e-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: 52.26 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 327 YVKDVDDGLQAAEEVGYPVMIKASEGG-GGKGIRKVNNADDFPnlfrQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYG 405
Cdd:pfam02222 12 AAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLP----QAWEELGDGPVIVEEFVPFDRELSVLVVRSVDG 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578830806 406 NAISlfgrdCS-VQRRHQK---IIEEAPATIaTPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPR 478
Cdd:pfam02222 88 ETAF-----YPvVETIQEDgicRLSVAPARV-PQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLINELAPR 158
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
316-479 |
1.24e-06 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 54.23 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 316 LNVPQElyEKGYVKDVDDGLQAAEEVGYPVMIKASE--GGGGKGIrkVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSR 393
Cdd:TIGR01369 138 IGEPVP--ESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSASPINQVLVEKSLAGWK 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 394 HLEVQILADQYGNAISLfgrdCSVQR-----RHQ-KIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEY-LYSQ 466
Cdd:TIGR01369 214 EIEYEVMRDSNDNCITV----CNMENfdpmgVHTgDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFaLNPD 289
|
170
....*....|...
gi 578830806 467 DGSFYFLELNPRL 479
Cdd:TIGR01369 290 SGRYYVIEVNPRV 302
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
337-505 |
3.72e-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: 51.84 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 337 AAEEVGYPVMIKASEGGGGKGIRKVNNAD-DFPNLFrqVQAEVPGSPIfvmrlakqSrhleVQILADqygnaislfGRDC 415
Cdd:COG2232 133 EPPPDPGPWLVKPIGGAGGWHIRPADSEApPAPGRY--FQRYVEGTPA--------S----VLFLAD---------GSDA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 416 SVQRRHQKIIEEAP------ATIATPAVFEH-----MEQCAVKLAKMVGYVSAGTVEYLYSQDGsFYFLELNPRLQVEHP 484
Cdd:COG2232 190 RVLGFNRQLIGPAGerpfryGGNIGPLALPPalaeeMRAIAEALVAALGLVGLNGVDFILDGDG-PYVLEVNPRPQASLD 268
|
170 180
....*....|....*....|.
gi 578830806 485 CTEMVADVNLPAAQLQIAMGI 505
Cdd:COG2232 269 LYEDATGGNLFDAHLRACRGE 289
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
311-478 |
9.49e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 50.27 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 311 FSKRILNVPQElYEKGYVKDVDDGLqAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQ-----VQAEVPGSPIfv 385
Cdd:PRK12767 119 LKENGIPTPKS-YLPESLEDFKAAL-AKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYvpnliIQEFIEGQEY-- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 386 mrlakqsrhlEVQILADQYGNAISLFGRdcsvqRRHQKIIEEA--PATIATPAVFEHMEQCAVKLakmvGYVSAGTVEYL 463
Cdd:PRK12767 195 ----------TVDVLCDLNGEVISIVPR-----KRIEVRAGETskGVTVKDPELFKLAERLAEAL----GARGPLNIQCF 255
|
170
....*....|....*
gi 578830806 464 YSqDGSFYFLELNPR 478
Cdd:PRK12767 256 VT-DGEPYLFEINPR 269
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
276-372 |
1.13e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 49.72 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 276 ALG-DKIASSIVAQTAGIPTLPWsgsglrvdwqendfskRILNvpqelyekgyvkDVDDGLQAAEEVGYPVMIKASEGGG 354
Cdd:PRK01372 94 ALAmDKLRTKLVWQAAGLPTPPW----------------IVLT------------REEDLLAAIDKLGLPLVVKPAREGS 145
|
90
....*....|....*...
gi 578830806 355 GKGIRKVNNADDFPNLFR 372
Cdd:PRK01372 146 SVGVSKVKEEDELQAALE 163
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
338-480 |
2.46e-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: 46.61 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 338 AEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQ--VQAEVPGSPIFVMRLAKQSRHLEVQIlADQY-GNAISLFGRD 414
Cdd:pfam02655 27 LLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIENvlVQEFIEGEPLSVSLLSDGEKALPLSV-NRQYiDNGGSGFVYA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 415 -CSVQRRH---QKIIEEApatiatpavfehmEQCAVKLAKMVGYVSagtVEYLYSqDGSFYFLELNPRLQ 480
Cdd:pfam02655 106 gNVTPSRTelkEEIIELA-------------EEVVECLPGLRGYVG---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 ... |
288-477 |
5.16e-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: 46.54 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 288 QTAGIPTLPWSGSgLRVDWQENdfskrilnvPQELYEkgyvkdvddglQAAEEVGYPVMIKASEGGGGKGIRKVNNAD-- 365
Cdd:pfam07478 3 KAAGLPVVPFVTF-TRADWKLN---------PKEWCA-----------QVEEALGYPVFVKPARLGSSVGVSKVESREel 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 366 -DFPNLFRQVQAEVpgspifVMRLAKQSRHLEVQILADQYGNAISLfGR---DCSVQRRHQKIIEEA-----PATIaTPA 436
Cdd:pfam07478 62 qAAIEEAFQYDEKV------LVEEGIEGREIECAVLGNEDPEVSPV-GEivpSGGFYDYEAKYIDDSaqivvPADL-EEE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578830806 437 VFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNP 477
Cdd:pfam07478 134 QEEQIQELALKAYKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
316-478 |
2.32e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 46.50 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 316 LNVPQELYEKgyVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRqvQAEVPGSPIFVMRL--AKQsr 393
Cdd:PRK12815 681 LGLPHVPGLT--ATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLA--ENASQLYPILIDQFidGKE-- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 394 hLEVQILADqyGNAISLFGrdcsvqrrhqkI---IEEA-----------PATIATPAVFEHMEQCAVKLAKMVGYVSAGT 459
Cdd:PRK12815 755 -YEVDAISD--GEDVTIPG-----------IiehIEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMN 820
|
170
....*....|....*....
gi 578830806 460 VEYLYsQDGSFYFLELNPR 478
Cdd:PRK12815 821 IQFVL-ANDEIYVLEVNPR 838
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
307-358 |
3.62e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.92 E-value: 3.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 578830806 307 QENDFSKRILN-----VPqelyeKGY-VKDVDDGLQAAEEVGYPVMIKASEGGGGKGI 358
Cdd:PRK14016 213 CDKELTKRLLAaagvpVP-----EGRvVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGV 265
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
270-497 |
3.76e-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: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 270 PSQAMWALGDKIASSIVAQTAGIPTlpwsgsglrvdwqendfskrilnvPQELYekgyVKDVDDGLQAAEEVGYPVMIKA 349
Cdd:COG0189 87 DPEAIRRARDKLFTLQLLARAGIPV------------------------PPTLV----TRDPDDLRAFLEELGGPVVLKP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 350 SEGGGGKGIRKVNNADDFPNLFRQ----------VQAEVP-------------GSPIFVMRlaKQSRHLEVQIladqygN 406
Cdd:COG0189 139 LDGSGGRGVFLVEDEDALESILEAltelgsepvlVQEFIPeedgrdirvlvvgGEPVAAIR--RIPAEGEFRT------N 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 407 aISLFGRdcsvqrrhqkiIEEAPATiatpavfEHMEQCAVKLAKMVGYVSAGtVEYLYSQDGsFYFLELNPRLQVEHpcT 486
Cdd:COG0189 211 -LARGGR-----------AEPVELT-------DEERELALRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVTPGFRG--L 267
|
250
....*....|.
gi 578830806 487 EMVADVNLPAA 497
Cdd:COG0189 268 ERATGVDIAEA 278
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1844-2097 |
4.81e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 45.18 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1844 ITISLVTCRAiGiGAYLVRLGQRTIQV-ENSHLILTGAGALNKVLGREVytSNNQLGGIQImhnngvtHCT---VCDDF- 1918
Cdd:PLN02820 209 IALVLGSCTA-G-GAYVPAMADESVIVkGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-------HCKvsgVSDHFa 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1919 ----------EGVFTVLHWLSYMPKSVHSSVPLLNSKDPIDRIIEF---VPT--KTPYDPRWMLAGrphptqkgqwlsgF 1983
Cdd:PLN02820 278 qdelhalaigRNIVKNLHLAAKQGMENTLGSKNPEYKEPLYDVKELrgiVPAdhKQSFDVRSVIAR-------------I 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 1984 FDYGSFSEIMQPWAQTVVVGRARLGGIPVGVVAvetrtvelsipadpanldseakiiqqAGQVWFPDSAFKTYQAIKDFN 2063
Cdd:PLN02820 345 VDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALKGAHFIELCA 398
|
250 260 270
....*....|....*....|....*....|....
gi 578830806 2064 REGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIV 2097
Cdd:PLN02820 399 QRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMV 432
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
328-478 |
5.15e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 44.76 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 328 VKDVDDGLQAAEEVGYPVMIKASEGG-GGKGIRKVNNADDFPNLFRQVQAE-------VPgspiFVMrlakqsrhlEVQI 399
Cdd:PRK06019 121 VDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEAAWALLGSVpcileefVP----FER---------EVSV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830806 400 LAdqygnAISLFGRDCS---VQRRHQKII---EEAPATIaTPAVFEHMEQCAVKLAKMVGYVsaGT--VEYLYSQDGSFY 471
Cdd:PRK06019 188 IV-----ARGRDGEVVFyplVENVHRNGIlrtSIAPARI-SAELQAQAEEIASRIAEELDYV--GVlaVEFFVTGDGELL 259
|
....*..
gi 578830806 472 FLELNPR 478
Cdd:PRK06019 260 VNEIAPR 266
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
326-367 |
2.62e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 43.16 E-value: 2.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 578830806 326 GYVKDVDDGLQAAEEVGYPVMIKAS--EGGGGKGIrkVNNADDF 367
Cdd:PRK05294 147 GIAHSMEEALEVAEEIGYPVIIRPSftLGGTGGGI--AYNEEEL 188
|
|
| |
