|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
820-1598 |
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: 996.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 820 LDDPSRVQQAELYTGTLPSIQSVALRGEKLHRVFHSTLGHLVHIMNGYCLpepffSAKLKEWVERLMKTLRDPSLPLLEL 899
Cdd:pfam08326 2 LDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLEW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 900 QDIMTSVSGRIPPAVEKAIKKEMAQYASNitsvLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQKYRSGI 979
Cdd:pfam08326 77 QEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 980 RGHMKAVVMDLLRQYLRVEVQFQHG--HYDKCVFALREENKVDMANVLNYIFSHAQVTKKNCLVTMLIDQLCGR---DPT 1054
Cdd:pfam08326 153 KGHEYSVFASLLEEYYDVEKLFSGGnvREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVSN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1055 LTDELMAILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCIENLQKLILS 1126
Cdd:pfam08326 233 VAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELIDS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1127 ETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCIVEFQFMLPTSHPNRGNIPTLNRMSFSSnl 1206
Cdd:pfam08326 313 KYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSP-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1207 nhyGMVHVASVSD-VLLDTSFTPPCQRMGAMVSFRSFQEFTRNIKDVLSCFSDSPPstptfpeggnpvlyrEEDSKSIQD 1285
Cdd:pfam08326 391 ---PFKRIASVSDlSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPE---------------ESGESNSSD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1286 EPIHILNVAIKTDSDID-DDGLAAMFREFTQSKKSLLFDHGIRRLTFLVAQK-REFPKFFTFRARDKFEEDRIYRHLEPA 1363
Cdd:pfam08326 453 EPINVLNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKdGQYPKYFTFRGPDNYEEDPIIRHIEPA 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1364 LAFQLELNRMRNFALTAIPCANHKMHLYLGAARVevgtEVTDYRFFVRAIIRHSDLVTKEASFEYLHNEAERLLLEAMDE 1443
Cdd:pfam08326 533 LAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKE----NPTDKRFFVRAIIRPGRLRDDIPTAEYLISEAERLLNDILDA 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1444 LEVAfNNTTVRTDCNHIFLNFVPTVIMDPSKhsaipsiqtilkttlaemqpqtrtnqrlqhvslkaIEESVRSMVMRYGS 1523
Cdd:pfam08326 609 LEVA-SIGNSNSDLNHIFLNFVPVFNVDPED-----------------------------------VEEAVGGFLERFGK 652
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207175556 1524 RLWKLRVLQAELKINIRLTPTGKQIPIRLFLTNESGYYLDISLYKEVTDSRtgqvghkdRQIMFQAYGdKQGPLH 1598
Cdd:pfam08326 653 RLWRLRVTQAEIRIIIRDPETGPPIPLRLVITNVSGYVVKVELYREVKDDK--------GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1698-2252 |
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: 605.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1698 PEYPAGREIIVISNDITHKIGSFGPQEDVLFQQASEMARESgIPRIYIAANSGARIGLAEEIRHMFHVAWQDPVDPYKGF 1777
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1778 KylyLTPQDYKKVSAlnsvhcehvedeGESRYKITDIIGKEEGLGVENLRGSGMIAGESSLAYEDIITMNLVTCRAIGIG 1857
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1858 AYLVRLGQRTIQVEN-SHIILTGAGALNKVLGrEVYTSNNQLGGVQIMHNNGVTHTNVCDDFEGVYTLLHWLSYMPK--- 1933
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKpap 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1934 NMSSPVPILSAKDPIDRA---IEFVPT--KAPYDPRWMLAGRpnqnikgawvsgfFDQGSFLEIMQPWAQSVVVGRARLG 2008
Cdd:pfam01039 224 NNREPVPIVPTKDPPDRDaplVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 2009 GIPTGVVAVETRsvelsipadpanldseakiiQQAGqVWFPDSAFKTAQAIKDFNREGLPLIVFANWRGFSGGMKDMYDQ 2088
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 2089 VLKFGAYIVDGLREYRQPVLVYIPPqaELRGGSWVVIDPTINPRHMeMYADKDSRGGVLEPEGTVEIKFRKKDLVKTMRR 2168
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 2169 VDPvymglaerlgtpelsvseRKELESKLKEREEFLLPIYHQVAVQFADLHDTPGRMQEKGVITDILEWSTSRqFFYWRL 2248
Cdd:pfam01039 427 KDL------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPWRK 487
|
....
gi 1207175556 2249 RRLL 2252
Cdd:pfam01039 488 HGNI 491
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
118-627 |
1.96e-131 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 421.35 E-value: 1.96e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 118 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGTNNNNYANVELILDIA 197
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 198 KRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgtgltvewtendqkkg 277
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 278 iinvptelyeQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVP---GSP-IFVMQLAK 353
Cdd:COG4770 135 ----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 354 HARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSSF 433
Cdd:COG4770 205 RPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 434 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLH-RIKDIRvlygmqpwgdspidfdglsttpcPRGHVIAARITS 512
Cdd:COG4770 285 YFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPfTQEDIK-----------------------LRGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 513 ENPDEGFKPSSGTVQELNFRsnknvwGYFSVAAAGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRGd 586
Cdd:COG4770 342 EDPARGFLPSPGTITRLRPP------GGPGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG- 414
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1207175556 587 FRTTVEYLIKLLETESFQHNSIDTGWLDRLISEKMQAERPD 627
Cdd:COG4770 415 VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
118-623 |
6.00e-110 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 359.12 E-value: 6.00e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 118 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGTNNNNYANVELILDIA 197
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 198 KRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgtgltvewtendqkkg 277
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 278 iinvptelyeQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVP---GSPIFVMQ--LA 352
Cdd:PRK08591 135 ----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPGVYMEkyLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 353 KhARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSS 432
Cdd:PRK08591 205 N-PRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 433 FYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLH-RIKDIRVlygmqpwgdspidfdglsttpcpRGHVIAARIT 511
Cdd:PRK08591 284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 512 SENPDEGFKPSSGTVQelnfrsnknvwGYFsvaAAGGLH--------------EFADSQFGHCFSWGENREEAISNMVVA 577
Cdd:PRK08591 341 AEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1207175556 578 LKELSIRGdFRTTVEYLIKLLETESFQHNSIDTGWLDRLISEKMQA 623
Cdd:PRK08591 407 LSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
118-619 |
1.09e-101 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 335.19 E-value: 1.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 118 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGTNNNNYANVELILDIA 197
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACK---------ELGIKTVAVHSTAD--RDALHVLLADEAVCIGPAPSAKSYLNIPNIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 198 KRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgtgltvewtendqkkg 277
Cdd:TIGR00514 71 EITGADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 278 iinvptelyeQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVP---GSP-IFVMQLAK 353
Cdd:TIGR00514 135 ----------DGLVEDEEENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKaafGNDgVYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 354 HARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSSF 433
Cdd:TIGR00514 205 NPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 434 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLhrikdirvlygmqPWGDSPIDFdglsttpcpRGHVIAARITSE 513
Cdd:TIGR00514 285 YFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL-------------SLKQEDVVV---------RGHAIECRINAE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 514 NPDEGFKPSSGTVQE------LNFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 587
Cdd:TIGR00514 343 DPIKTFLPSPGRITRylppggPGVRWDSHVYSGYTVPP------YYDSMIGKLITYGKTREVAIARMKRALSEFIIDG-I 415
|
490 500 510
....*....|....*....|....*....|..
gi 1207175556 588 RTTVEYLIKLLETESFQHNSIDTGWLDRLISE 619
Cdd:TIGR00514 416 KTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
279-470 |
2.66e-59 |
|
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: 203.69 E-value: 2.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 279 INVPTELYEQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVPGSP----IFVMQLAKH 354
Cdd:pfam02786 12 AGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 355 ARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDS-SF 433
Cdd:pfam02786 92 PKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFSgEY 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207175556 434 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL 470
Cdd:pfam02786 172 YFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
508-614 |
2.05e-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: 122.52 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 508 ARITSENPDEGFKPSSGTVQELNFRSNKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 585
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 1207175556 586 dFRTTVEYLIKLLETESFQHNSIDTGWLD 614
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1685-2078 |
1.10e-21 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 101.64 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1685 EIGM-VAWRMTLRTPEYPA-----------GREIIVISNDITHKIGSFGPQ--EDVLfqQASEMARESGIPRIYIAANSG 1750
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPGdgvvtgigtvdGRPVVVVANDFTVKGGSLGPMtaKKIL--RAQDIALENGLPVIYLVDSGG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1751 ARIglaeeirhmfhvawQDPVDPYKGFkylyltpqdykkvsalnsvhcehvedeGESRYKitdiigkeeglgveNLRGSG 1830
Cdd:COG4799 129 ARL--------------QEGVESFAGY---------------------------GRIFYR--------------NARSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1831 MIAgesslayedIITMNLVTCraIGIGAYLVRLGQRTIQVE-NSHIILTGAGALNKVLGREVytSNNQLGGVQiMHN--N 1907
Cdd:COG4799 154 GIP---------QISVIMGPC--AAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1908 GVTHtNVCDD----FEGVYTLLhwlSYMPKNMSSPVPILSAKDPIDRAIE---FVPT--KAPYDPRWMLAGrpnqnikga 1978
Cdd:COG4799 220 GVAD-YLAEDeeeaLALARRLL---SYLPSNNLEDPPRAEPAPPARDPEElygIVPEdpRKPYDMREVIAR--------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1979 wvsgFFDQGSFLEIMQPWAQSVVVGRARLGGIPTGVVAvetrsvelsipADPANLdseakiiqqAGqVWFPDSAFKTAQA 2058
Cdd:COG4799 287 ----LVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA-----------NQPMVL---------AG-VLDIDAADKAARF 341
|
410 420
....*....|....*....|
gi 1207175556 2059 IKDFNREGLPLIVFANWRGF 2078
Cdd:COG4799 342 IRLCDAFNIPLVFLVDVPGF 361
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
753-818 |
3.60e-16 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 74.94 E-value: 3.60e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207175556 753 VLRSPSAGKLI-----QYTVEDGGHVFAGQCYAEIEVMKMVMTLTASESGCIHYVKR-AGAVLEPGCIIGKL 818
Cdd:pfam00364 2 EIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVpEGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
753-818 |
3.07e-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: 3.07e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207175556 753 VLRSPSAGKLIQYTVEDGGHVFAGQCYAEIEVMKMVMTLTASESGCIHYVK-RAGAVLEPGCIIGKL 818
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
749-812 |
6.58e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 42.05 E-value: 6.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207175556 749 NDPSVLRSPSAGKLIQYTVEDGGHVFAGQCYAEIEVMKMVMTLTASESGCI-HYVKRAGAVLEPG 812
Cdd:PRK12999 1074 GNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVkRVLVKAGDQVEAG 1138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
820-1598 |
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: 996.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 820 LDDPSRVQQAELYTGTLPSIQSVALRGEKLHRVFHSTLGHLVHIMNGYCLpepffSAKLKEWVERLMKTLRDPSLPLLEL 899
Cdd:pfam08326 2 LDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLEW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 900 QDIMTSVSGRIPPAVEKAIKKEMAQYASNitsvLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQKYRSGI 979
Cdd:pfam08326 77 QEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 980 RGHMKAVVMDLLRQYLRVEVQFQHG--HYDKCVFALREENKVDMANVLNYIFSHAQVTKKNCLVTMLIDQLCGR---DPT 1054
Cdd:pfam08326 153 KGHEYSVFASLLEEYYDVEKLFSGGnvREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVSN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1055 LTDELMAILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCIENLQKLILS 1126
Cdd:pfam08326 233 VAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELIDS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1127 ETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCIVEFQFMLPTSHPNRGNIPTLNRMSFSSnl 1206
Cdd:pfam08326 313 KYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSP-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1207 nhyGMVHVASVSD-VLLDTSFTPPCQRMGAMVSFRSFQEFTRNIKDVLSCFSDSPPstptfpeggnpvlyrEEDSKSIQD 1285
Cdd:pfam08326 391 ---PFKRIASVSDlSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPE---------------ESGESNSSD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1286 EPIHILNVAIKTDSDID-DDGLAAMFREFTQSKKSLLFDHGIRRLTFLVAQK-REFPKFFTFRARDKFEEDRIYRHLEPA 1363
Cdd:pfam08326 453 EPINVLNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKdGQYPKYFTFRGPDNYEEDPIIRHIEPA 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1364 LAFQLELNRMRNFALTAIPCANHKMHLYLGAARVevgtEVTDYRFFVRAIIRHSDLVTKEASFEYLHNEAERLLLEAMDE 1443
Cdd:pfam08326 533 LAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKE----NPTDKRFFVRAIIRPGRLRDDIPTAEYLISEAERLLNDILDA 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1444 LEVAfNNTTVRTDCNHIFLNFVPTVIMDPSKhsaipsiqtilkttlaemqpqtrtnqrlqhvslkaIEESVRSMVMRYGS 1523
Cdd:pfam08326 609 LEVA-SIGNSNSDLNHIFLNFVPVFNVDPED-----------------------------------VEEAVGGFLERFGK 652
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207175556 1524 RLWKLRVLQAELKINIRLTPTGKQIPIRLFLTNESGYYLDISLYKEVTDSRtgqvghkdRQIMFQAYGdKQGPLH 1598
Cdd:pfam08326 653 RLWRLRVTQAEIRIIIRDPETGPPIPLRLVITNVSGYVVKVELYREVKDDK--------GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1698-2252 |
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: 605.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1698 PEYPAGREIIVISNDITHKIGSFGPQEDVLFQQASEMARESgIPRIYIAANSGARIGLAEEIRHMFHVAWQDPVDPYKGF 1777
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1778 KylyLTPQDYKKVSAlnsvhcehvedeGESRYKITDIIGKEEGLGVENLRGSGMIAGESSLAYEDIITMNLVTCRAIGIG 1857
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1858 AYLVRLGQRTIQVEN-SHIILTGAGALNKVLGrEVYTSNNQLGGVQIMHNNGVTHTNVCDDFEGVYTLLHWLSYMPK--- 1933
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKpap 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1934 NMSSPVPILSAKDPIDRA---IEFVPT--KAPYDPRWMLAGRpnqnikgawvsgfFDQGSFLEIMQPWAQSVVVGRARLG 2008
Cdd:pfam01039 224 NNREPVPIVPTKDPPDRDaplVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 2009 GIPTGVVAVETRsvelsipadpanldseakiiQQAGqVWFPDSAFKTAQAIKDFNREGLPLIVFANWRGFSGGMKDMYDQ 2088
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 2089 VLKFGAYIVDGLREYRQPVLVYIPPqaELRGGSWVVIDPTINPRHMeMYADKDSRGGVLEPEGTVEIKFRKKDLVKTMRR 2168
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 2169 VDPvymglaerlgtpelsvseRKELESKLKEREEFLLPIYHQVAVQFADLHDTPGRMQEKGVITDILEWSTSRqFFYWRL 2248
Cdd:pfam01039 427 KDL------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPWRK 487
|
....
gi 1207175556 2249 RRLL 2252
Cdd:pfam01039 488 HGNI 491
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
118-627 |
1.96e-131 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 421.35 E-value: 1.96e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 118 IEKVLIANNGIAAVKCMRSIRrwayEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGTNNNNYANVELILDIA 197
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 198 KRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgtgltvewtendqkkg 277
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 278 iinvptelyeQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVP---GSP-IFVMQLAK 353
Cdd:COG4770 135 ----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 354 HARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSSF 433
Cdd:COG4770 205 RPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 434 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLH-RIKDIRvlygmqpwgdspidfdglsttpcPRGHVIAARITS 512
Cdd:COG4770 285 YFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPfTQEDIK-----------------------LRGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 513 ENPDEGFKPSSGTVQELNFRsnknvwGYFSVAAAGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRGd 586
Cdd:COG4770 342 EDPARGFLPSPGTITRLRPP------GGPGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG- 414
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1207175556 587 FRTTVEYLIKLLETESFQHNSIDTGWLDRLISEKMQAERPD 627
Cdd:COG4770 415 VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
118-623 |
6.00e-110 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 359.12 E-value: 6.00e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 118 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGTNNNNYANVELILDIA 197
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 198 KRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgtgltvewtendqkkg 277
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 278 iinvptelyeQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVP---GSPIFVMQ--LA 352
Cdd:PRK08591 135 ----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPGVYMEkyLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 353 KhARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSS 432
Cdd:PRK08591 205 N-PRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 433 FYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLH-RIKDIRVlygmqpwgdspidfdglsttpcpRGHVIAARIT 511
Cdd:PRK08591 284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSiKQEDIVF-----------------------RGHAIECRIN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 512 SENPDEGFKPSSGTVQelnfrsnknvwGYFsvaAAGGLH--------------EFADSQFGHCFSWGENREEAISNMVVA 577
Cdd:PRK08591 341 AEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1207175556 578 LKELSIRGdFRTTVEYLIKLLETESFQHNSIDTGWLDRLISEKMQA 623
Cdd:PRK08591 407 LSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
116-614 |
9.02e-103 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 359.45 E-value: 9.02e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 116 KVIEKVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEY-IKMADHyvPVPGgtnnnnYA 188
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAA---------TELGIRTVAIYSEEDklslhrFKADEAYlIGEGKH--PVRA------YL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 189 NVELILDIAKRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGTGltve 268
Cdd:PRK12999 66 DIDEIIRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGP---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 269 wtendqkkgiinvptelyeqgcVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVP---GSP 345
Cdd:PRK12999 142 ----------------------IDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafGND 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 346 -IFVMQLAKHARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVE 424
Cdd:PRK12999 200 eVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 425 YLYSQDSSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLHrikDIRVLYGMQpwgdspidfdglsTTPCPRGH 504
Cdd:PRK12999 280 FLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATLH---DLEIGIPSQ-------------EDIRLRGY 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 505 VIAARITSENPDEGFKPSSGTVQElnFRSNknvwGYFSV------AAAGGlhEFA---DSQFGHCFSWGENREEAISNMV 575
Cdd:PRK12999 344 AIQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVrldggnAFAGA--EITpyyDSLLVKLTAWGRTFEQAVARMR 415
|
490 500 510
....*....|....*....|....*....|....*....
gi 1207175556 576 VALKELSIRGdFRTTVEYLIKLLETESFQHNSIDTGWLD 614
Cdd:PRK12999 416 RALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFID 453
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
118-620 |
2.06e-102 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 337.39 E-value: 2.06e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 118 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVVMVTPEDlkANAEYIKMADHYVPVPGGTNNNNYANVELILDIA 197
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLG---------IRTVAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 198 KRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGTGLTvewtendqkkg 277
Cdd:PRK06111 71 KKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLE----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 278 iinvptelyeqgcvhDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVP---GSP-IFVMQLAK 353
Cdd:PRK06111 140 ---------------DAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAAnffGNGeMYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 354 HARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSSF 433
Cdd:PRK06111 205 DPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 434 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-HRIKDIRVlygmqpwgdspidfdglsttpcpRGHVIAARITS 512
Cdd:PRK06111 285 YFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR-----------------------SGHAIEVRIYA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 513 ENPDEgFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVE 592
Cdd:PRK06111 342 EDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEG-IKTNIP 419
|
490 500
....*....|....*....|....*...
gi 1207175556 593 YLIKLLETESFQHNSIDTGWLDRLISEK 620
Cdd:PRK06111 420 LLLQVLEDPVFKAGGYTTGFLTKQLVKK 447
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
118-619 |
1.09e-101 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 335.19 E-value: 1.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 118 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGTNNNNYANVELILDIA 197
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACK---------ELGIKTVAVHSTAD--RDALHVLLADEAVCIGPAPSAKSYLNIPNIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 198 KRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgtgltvewtendqkkg 277
Cdd:TIGR00514 71 EITGADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 278 iinvptelyeQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVP---GSP-IFVMQLAK 353
Cdd:TIGR00514 135 ----------DGLVEDEEENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKaafGNDgVYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 354 HARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSSF 433
Cdd:TIGR00514 205 NPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 434 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLhrikdirvlygmqPWGDSPIDFdglsttpcpRGHVIAARITSE 513
Cdd:TIGR00514 285 YFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL-------------SLKQEDVVV---------RGHAIECRINAE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 514 NPDEGFKPSSGTVQE------LNFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 587
Cdd:TIGR00514 343 DPIKTFLPSPGRITRylppggPGVRWDSHVYSGYTVPP------YYDSMIGKLITYGKTREVAIARMKRALSEFIIDG-I 415
|
490 500 510
....*....|....*....|....*....|..
gi 1207175556 588 RTTVEYLIKLLETESFQHNSIDTGWLDRLISE 619
Cdd:TIGR00514 416 KTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
119-622 |
2.89e-101 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 335.80 E-value: 2.89e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 119 EKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGTNNNNYANVELILDIAK 198
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACR---------ELGIKTVAVYSEAD--KNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 199 RIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgtgltvewtendqkkgi 278
Cdd:PRK08654 72 KAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGT----------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 279 invptelyeQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLY---RQVQAEVPGSP-IFVMQLAKH 354
Cdd:PRK08654 135 ---------EEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIestQSIAQSAFGDStVFIEKYLEK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 355 ARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSqDSSFY 434
Cdd:PRK08654 206 PRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 435 FLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-HRIKDIRVlygmqpwgdspidfdglsttpcpRGHVIAARITSE 513
Cdd:PRK08654 285 FLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELsFKQEDITI-----------------------RGHAIECRINAE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 514 NPDEGFKPSSGTVQelnfrsnknvwGYFSVAAAG-----GLH------EFADSQFGHCFSWGENREEAISNMVVALKELS 582
Cdd:PRK08654 342 DPLNDFAPSPGKIK-----------RYRSPGGPGvrvdsGVHmgyeipPYYDSMISKLIVWGRTREEAIARMRRALYEYV 410
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1207175556 583 IRGdFRTTVEYLIKLLETESFQHNSIDTGWLD--RLISEKMQ 622
Cdd:PRK08654 411 IVG-VKTNIPFHKAVMENENFVRGNLHTHFIEeeTTILEEMK 451
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
116-614 |
2.72e-99 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 348.99 E-value: 2.72e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 116 KVIEKVLIANNG-IAavkcmrsIR--RWAYEMfrnerAIRFVVMVTPED------LKANAEY-IKMADHyvPVpggtnnN 185
Cdd:COG1038 2 KKIKKVLVANRGeIA-------IRvfRAATEL-----GIRTVAIYSEEDryslhrFKADEAYlIGEGKG--PV------D 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 186 NYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGTGl 265
Cdd:COG1038 62 AYLDIEEIIRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP--GTE- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 266 tvewtendqkkgiinvptelyeqGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVP--- 342
Cdd:COG1038 139 -----------------------GPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaaf 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 343 GSP-IFVMQLAKHARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAG 421
Cdd:COG1038 196 GDDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 422 TVEYLYSQDSSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLH----RIK---DIRVlygmqpwgdspidfdg 494
Cdd:COG1038 276 TVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSLDdpeiGIPsqeDIRL---------------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 495 lsttpcpRGHVIAARITSENPDEGFKPSSGTVQElnFRSnknvwgyfsvaaAGGlhefadsqFG------HCFS------ 562
Cdd:COG1038 340 -------NGYAIQCRITTEDPANNFMPDTGRITA--YRS------------AGG--------FGirldggNAYTgavitp 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207175556 563 -----------WGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQHNSIDTGWLD 614
Cdd:COG1038 391 yydsllvkvtaWGRTFEEAIRKMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFID 452
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
118-615 |
9.27e-95 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 315.15 E-value: 9.27e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 118 IEKVLIANNGIAAVKCMRSIRrwayEMfrNERAIrfVVMVTPEDlkaNAEYIKMADHYVPVPGGTNNNNYANVELILDIA 197
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQ----EM--GKEAI--AIYSTADK---DALYLKYADAKICIGGAKSSESYLNIPAIISAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 198 KRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgtgltvewtendqkkg 277
Cdd:PRK08462 73 EIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGS---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 278 iinvptelyeQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVPGS----PIFVMQLAK 353
Cdd:PRK08462 137 ----------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAfgdgTMYMEKFIN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 354 HARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSSF 433
Cdd:PRK08462 207 NPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 434 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLHRIKDIRVlygmqpwgdspidfdglsttpcpRGHVIAARITSE 513
Cdd:PRK08462 287 YFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKL-----------------------KGHAIECRITAE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 514 NPdEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 587
Cdd:PRK08462 344 DP-KKFYPSPGKITKWiapggrNVRMDSHAYAGYVVPP------YYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEG-I 415
|
490 500
....*....|....*....|....*...
gi 1207175556 588 RTTVEYLIKLLETESFQHNSIDTGWLDR 615
Cdd:PRK08462 416 KTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
118-615 |
7.65e-94 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 312.42 E-value: 7.65e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 118 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGTNNNNYANVELILDIA 197
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACR---------EMGIETVAVYSEAD--KDALHVQLADEAVCIGPASSKDSYLNIQNIISAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 198 KRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgtgltvewtendqkkg 277
Cdd:PRK05586 71 VLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 278 iinvptelyeQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVPGS----PIFVMQLAK 353
Cdd:PRK05586 135 ----------EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 354 HARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSSF 433
Cdd:PRK05586 205 NPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 434 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLH-RIKDIRVlygmqpwgdspidfdglsttpcpRGHVIAARITS 512
Cdd:PRK05586 285 YFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSiKQEDIKI-----------------------NGHSIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 513 ENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVE 592
Cdd:PRK05586 342 EDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEG-VNTNID 420
|
490 500
....*....|....*....|...
gi 1207175556 593 YLIKLLETESFQHNSIDTGWLDR 615
Cdd:PRK05586 421 FQFIILEDEEFIKGTYDTSFIEK 443
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
118-629 |
3.32e-90 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 302.83 E-value: 3.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 118 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDLKANAeyIKMADHYVPVPGGTNNNNYANVELILDIA 197
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAAR---------ELGMRTVAACSDADRDSLA--ARMADEAVHIGPSHAAKSYLNPAAILAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 198 KRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgtgltvewtendqkkg 277
Cdd:PRK12833 74 RQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGS---------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 278 iinvptelyeQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAED----FPNLYRQVQAEVPGSPIFVMQLAK 353
Cdd:PRK12833 138 ----------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQlaaeLPLAQREAQAAFGDGGVYLERFIA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 354 HARHLEVQILADQYgNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSS- 432
Cdd:PRK12833 208 RARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGe 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 433 FYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLH-RIKDIRVlygmqpwgdspidfdglsttpcpRGHVIAARIT 511
Cdd:PRK12833 287 FYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRfAQGDIAL-----------------------RGAALECRIN 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 512 SENPDEGFKPSSGTVQELNF------RSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRG 585
Cdd:PRK12833 344 AEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYPGYRVPP------FYDSLLAKLIVHGEDRAAALARAARALRELRIDG 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1207175556 586 dFRTTVEYLIKLLETESFQHNSIDTGWLdrlisEKMQAERPDTM 629
Cdd:PRK12833 418 -MKTTAPLHRALLADADVRAGRFHTNFL-----EAWLAEWRAAL 455
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
119-616 |
4.30e-89 |
|
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including characterized members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae. The allophanate hydrolase domain of the yeast enzyme is not included in this model and is represented by an adjacent gene in Oleomonas sagaranensis. The fusion of urea carboxylase and allophanate hydrolase is designated urea amidolyase. The enzyme from Oleomonas sagaranensis was shown to be highly active on acetamide and formamide as well as urea. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 274264 [Multi-domain] Cd Length: 1201 Bit Score: 318.90 E-value: 4.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 119 EKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVVMVTPEDlkANAEYIKMADHYVPVPGGTNNNNYANVELILDIAK 198
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRMG---------IRSVAVYSDAD--AASQHVLDADEAVCLGGAPAAESYLDIDKILAAAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 199 RIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGTGLtvewtendqkkgi 278
Cdd:TIGR02712 71 KTGAQAIHPGYGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLP--GTGL------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 279 invptelyeqgcVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAED----FPNLYRQVQAEVPGSPIFVMQLAKH 354
Cdd:TIGR02712 136 ------------LSSLDEALEAAKEIGYPVMLKSTAGGGGIGMQKCDSAAElaeaFETVKRLGESFFGDAGVFLERFVEN 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 355 ARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLY-SQDSSF 433
Cdd:TIGR02712 204 ARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEETPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYdEARDEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 434 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAmgiplhrikdirvlygmqpwGDSPIDFDGLSTTPCPRGHVIAARITSE 513
Cdd:TIGR02712 284 YFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIA--------------------AGELPDFASLNISLTPRGAAIEARVYAE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 514 NPDEGFKPSSGTVQELNFRSNKNVWGYfsVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVEY 593
Cdd:TIGR02712 344 NPAKNFQPSPGLLTDVQFPDDVRVDTW--VETGTEVSPEYDPMLAKIIVHGSDREDAILKLHQALAETRVYG-IETNLDY 420
|
490 500
....*....|....*....|...
gi 1207175556 594 LIKLLETESFQHNSIDTGWLDRL 616
Cdd:TIGR02712 421 LRSILSSETFRSAQVSTRTLNSF 443
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
120-634 |
2.82e-86 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 309.45 E-value: 2.82e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 120 KVLIANNGIAAVKCMRSIrrwayemfrNERAIRFVVMVTPED------LKANAEY-IKMADHYVPVpggtnnNNYANVEL 192
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 193 ILDIAKRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGTgltvewten 272
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVP--GT--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 273 dqkkgiinvptelyeQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVPGS----PIFV 348
Cdd:TIGR01235 135 ---------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVYV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 349 MQLAKHARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYS 428
Cdd:TIGR01235 200 EKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 429 QDSSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLHRIKdirVLYGMQpwgdspidfDGLSTtpcpRGHVIAA 508
Cdd:TIGR01235 280 NDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQ---LGVPNQ---------EDIRT----NGYAIQC 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 509 RITSENPDEGFKPSSGTVQElnFRSNknvwGYFSVAAAGG-------LHEFADSQFGHCFSWGENREEAISNMVVALKEL 581
Cdd:TIGR01235 344 RVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAKMDRALREF 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207175556 582 SIRGdFRTTVEYLIKLLETESFQHNSIDTGWLD------RLISEKMQAERPDTMLGVVS 634
Cdd:TIGR01235 418 RIRG-VKTNIPFLENVLGHPKFLDGSYDTRFIDttpelfQFVKSQDRATKLLTYLADVT 475
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
117-614 |
1.50e-84 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 286.61 E-value: 1.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 117 VIEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYV-----PVPGgtnnnnYANVE 191
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACA---------EMGIRSVAIYSEAD--RHALHVKRADEAYsigadPLAG------YLNPR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 192 LILDIAKRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgtgltvewte 271
Cdd:PRK07178 64 RLVNLAVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGS---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 272 ndqkkgiinvptelyeQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVP---GSP-IF 347
Cdd:PRK07178 134 ----------------EGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafGSAeVF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 348 VMQLAKHARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLY 427
Cdd:PRK07178 198 LEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 428 SQDSSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-HRIKDIRVlygmqpwgdspidfdglsttpcpRGHVI 506
Cdd:PRK07178 278 DADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH-----------------------RGFAL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 507 AARITSENPDEGFKPSSGTVQElnfrsnknvwgYFSVAAAG---------GLH--EFADSQFGHCFSWGENREEAISNMV 575
Cdd:PRK07178 335 QFRINAEDPKNDFLPSFGKITR-----------YYAPGGPGvrtdtaiytGYTipPYYDSMCAKLIVWALTWEEALDRGR 403
|
490 500 510
....*....|....*....|....*....|....*....
gi 1207175556 576 VALKELSIRGdFRTTVEYLIKLLETESFQHNSIDTGWLD 614
Cdd:PRK07178 404 RALDDMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVE 441
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
118-637 |
3.72e-73 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 253.58 E-value: 3.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 118 IEKVLIANNGIAAVKCMRSIRrwayemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVpGGTNNNNYANVELILDIA 197
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACR---------DLHIKSVAIYTEPD--RECLHVKIADEAYRI-GTDPIKGYLDVKRIVEIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 198 KRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGTgltvewtendqkkg 277
Cdd:PRK08463 70 KACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVP--GT-------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 278 iinvptelyEQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLY----RQVQAEVPGSPIFVMQLAK 353
Cdd:PRK08463 134 ---------EKLNSESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFesckREALAYFNNDEVFMEKYVV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 354 HARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSSF 433
Cdd:PRK08463 205 NPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 434 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLH-RIKDIRvlygmqpwgdspidfdglsttpcPRGHVIAARITS 512
Cdd:PRK08463 285 YFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDlEQSDIK-----------------------PRGFAIEARITA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 513 ENPDEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGd 586
Cdd:PRK08463 342 ENVWKNFIPSPGKITEYypalgpSVRVDSHIYKDYTIPP------YYDSMLAKLIVKATSYDLAVNKLERALKEFVIDG- 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207175556 587 FRTTVEYLIKLLETESFQHNSIDTGWLDRLISEKMQA------ERPDTMLGVVSGAL 637
Cdd:PRK08463 415 IRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKtedrhqENKEEVIAAIAAAL 471
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
279-470 |
2.66e-59 |
|
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: 203.69 E-value: 2.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 279 INVPTELYEQGCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVPGSP----IFVMQLAKH 354
Cdd:pfam02786 12 AGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 355 ARHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDS-SF 433
Cdd:pfam02786 92 PKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFSgEY 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207175556 434 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL 470
Cdd:pfam02786 172 YFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
118-236 |
2.67e-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: 2.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 118 IEKVLIANNGIAAVKCMRSIRRWAyemfrneraIRFVVMVTPEDlkANAEYIKMADHYVPVPGGTNNNNYANVELILDIA 197
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELG---------IRTVAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAA 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207175556 198 KRIPVQAVWAGWGHASENPKLPELLHKNGIAFMGPPSQA 236
Cdd:pfam00289 70 KETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
190-469 |
1.02e-39 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 149.25 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 190 VELILDIAKRIPVQAVWAGWGHASEnpKLPELLHKNGIAfmGPPSQAMWALGDKIASSIVAQTAGIPTlPWSGtgltvew 269
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVE--TAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 270 tendqkkgiinvptelyeqgCVHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEV----PGSP 345
Cdd:COG0439 74 --------------------LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNGE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 346 IFVMQLAkHARHLEVQILADQyGNAISlfgrdCSVQRRHQK---IIE---EAPATIaTSDVFEDMEKCAVKLAKMVGYV- 418
Cdd:COG0439 134 VLVEEFL-EGREYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPL-PEELRAEIGELVARALRALGYRr 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1207175556 419 SAGTVEYLYSQDSSFYFLELNPRLQVEH--PCTEMVADVNLPAAQLQIAMGIP 469
Cdd:COG0439 206 GAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
508-614 |
2.05e-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: 122.52 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 508 ARITSENPDEGFKPSSGTVQELNFRSNKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 585
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 1207175556 586 dFRTTVEYLIKLLETESFQHNSIDTGWLD 614
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
508-615 |
1.46e-29 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 114.51 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 508 ARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 587
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*...
gi 1207175556 588 RTTVEYLIKLLETESFQHNSIDTGWLDR 615
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1685-2078 |
1.10e-21 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 101.64 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1685 EIGM-VAWRMTLRTPEYPA-----------GREIIVISNDITHKIGSFGPQ--EDVLfqQASEMARESGIPRIYIAANSG 1750
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPGdgvvtgigtvdGRPVVVVANDFTVKGGSLGPMtaKKIL--RAQDIALENGLPVIYLVDSGG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1751 ARIglaeeirhmfhvawQDPVDPYKGFkylyltpqdykkvsalnsvhcehvedeGESRYKitdiigkeeglgveNLRGSG 1830
Cdd:COG4799 129 ARL--------------QEGVESFAGY---------------------------GRIFYR--------------NARSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1831 MIAgesslayedIITMNLVTCraIGIGAYLVRLGQRTIQVE-NSHIILTGAGALNKVLGREVytSNNQLGGVQiMHN--N 1907
Cdd:COG4799 154 GIP---------QISVIMGPC--AAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1908 GVTHtNVCDD----FEGVYTLLhwlSYMPKNMSSPVPILSAKDPIDRAIE---FVPT--KAPYDPRWMLAGrpnqnikga 1978
Cdd:COG4799 220 GVAD-YLAEDeeeaLALARRLL---SYLPSNNLEDPPRAEPAPPARDPEElygIVPEdpRKPYDMREVIAR--------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 1979 wvsgFFDQGSFLEIMQPWAQSVVVGRARLGGIPTGVVAvetrsvelsipADPANLdseakiiqqAGqVWFPDSAFKTAQA 2058
Cdd:COG4799 287 ----LVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA-----------NQPMVL---------AG-VLDIDAADKAARF 341
|
410 420
....*....|....*....|
gi 1207175556 2059 IKDFNREGLPLIVFANWRGF 2078
Cdd:COG4799 342 IRLCDAFNIPLVFLVDVPGF 361
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
753-818 |
3.60e-16 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 74.94 E-value: 3.60e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207175556 753 VLRSPSAGKLI-----QYTVEDGGHVFAGQCYAEIEVMKMVMTLTASESGCIHYVKR-AGAVLEPGCIIGKL 818
Cdd:pfam00364 2 EIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVpEGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
753-818 |
3.07e-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: 3.07e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207175556 753 VLRSPSAGKLIQYTVEDGGHVFAGQCYAEIEVMKMVMTLTASESGCIHYVK-RAGAVLEPGCIIGKL 818
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
172-470 |
4.11e-11 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 67.26 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 172 ADHYVPVPGGTNNNNyANVELILDIAKRIPVQAVWA---GWGHA-SEN-PKLPEllhknGIAFMGPPSQAMWALGDKIAS 246
Cdd:COG3919 48 VDEVVVVPDPGDDPE-AFVDALLELAERHGPDVLIPtgdEYVELlSRHrDELEE-----HYRLPYPDADLLDRLLDKERF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 247 SIVAQTAGIPtlpwsgtgltvewtendqkkgiinVPTELYeqgcVHDVEAGLKAAEQVGFPVMVKASEG--------GGG 318
Cdd:COG3919 122 YELAEELGVP------------------------VPKTVV----LDSADDLDALAEDLGFPVVVKPADSvgydelsfPGK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 319 KGIRKVNCAEDFPNLYRQ---------VQAEVPG--SPIFVmqlakharhleVQILADQYGNAISLFGRdcsvQRRHQKI 387
Cdd:COG3919 174 KKVFYVDDREELLALLRRiaaagyeliVQEYIPGddGEMRG-----------LTAYVDRDGEVVATFTG----RKLRHYP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 388 IEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLY-SQDSSFYFLELNPRLQVEHPCTEmVADVNLPAAQLQIAM 466
Cdd:COG3919 239 PAGGNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRdPRDGEYKLIEINPRFWRSLYLAT-AAGVNFPYLLYDDAV 317
|
....
gi 1207175556 467 GIPL 470
Cdd:COG3919 318 GRPL 321
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
279-442 |
1.71e-07 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 56.93 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 279 INVPTElyEQGCVHDVEAGLKAAEQVGFPVMVKASE--GGGGKGIrkVNCAEDFPNLYRQVQAEVPGSPIFVMQLAKHAR 356
Cdd:TIGR01369 138 IGEPVP--ESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSASPINQVLVEKSLAGWK 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 357 HLEVQILADQYGNAISLfgrdCSVQR-----RHQ-KIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQD 430
Cdd:TIGR01369 214 EIEYEVMRDSNDNCITV----CNMENfdpmgVHTgDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPD 289
|
170
....*....|...
gi 1207175556 431 S-SFYFLELNPRL 442
Cdd:TIGR01369 290 SgRYYVIEVNPRV 302
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
291-470 |
2.96e-07 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 56.16 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 291 VHDVEAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEVPGSPIFVMQLAKHARHLEVQILADqyGNA 370
Cdd:TIGR01369 690 ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 371 ISLFGrdcsvQRRHqkiIEEA-----------PATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDsSFYFLELN 439
Cdd:TIGR01369 768 VLIPG-----IMEH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDG-EVYVIEVN 838
|
170 180 190
....*....|....*....|....*....|.
gi 1207175556 440 PRLQVEHPCTEMVADVNLPAAQLQIAMGIPL 470
Cdd:TIGR01369 839 PRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
214-331 |
2.99e-06 |
|
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: 51.65 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 214 ENPKLPELLHKNGIAFMGPPSQAMwALG-DKIASSIVAQTAGIPTLPWsgtgltvewtendqkkgiinvptELYEQGCVH 292
Cdd:COG1181 67 EDGTIQGLLELLGIPYTGSGVLAS-ALAmDKALTKRVLAAAGLPTPPY-----------------------VVLRRGELA 122
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207175556 293 DVEAglkAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFP 331
Cdd:COG1181 123 DLEA---IEEELGLPLFVKPAREGSSVGVSKVKNAEELA 158
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
222-459 |
3.41e-06 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 51.19 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 222 LHKNGIAFMGPPsQAMWALGDKIASSIVAQTAGIPTlpwsgtgltvewtendQKKGIInvptelyeqgcvHDVEAGLKAA 301
Cdd:TIGR00768 69 LESLGVPVINSS-DAILNAGDKFLSHQLLAKAGIPL----------------PRTGLA------------GSPEEALKLI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 302 EQVGFPVMVKASEGGGGKG---IRKVNCAEDFPNLYRQVQAevPGSPIFVMQLAKHARHLEV-------QILADQYGNAI 371
Cdd:TIGR00768 120 EEIGFPVVLKPVFGSWGRGvslARDRQAAESLLEHFEQLNG--PQNLFLVQEYIKKPGGRDIrvfvvgdEVVAAIYRITS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 372 SLFGRDCSVQRRHQKIieeapatiatsDVFEDMEKCAVKLAKMVGYVSAGtVEYLYSQDsSFYFLELNPRLQVEHpcTEM 451
Cdd:TIGR00768 198 GHWRSNLARGGKAEPC-----------SLTEEIEELAIKAAKALGLDVAG-VDLLESED-GLLVNEVNANPEFKN--SVK 262
|
....*...
gi 1207175556 452 VADVNLPA 459
Cdd:TIGR00768 263 TTGVNIAG 270
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
295-441 |
4.01e-06 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 52.47 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 295 EAGLKAAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNlYRQVQAEV-PGSPIFVMQLAKHARHLEVQILADQYGNAI-- 371
Cdd:PLN02735 727 ADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKT-YLETAVEVdPERPVLVDKYLSDATEIDVDALADSEGNVVig 805
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207175556 372 ---------SLFGRDCSVQRRHQKIIEEAPATIATSdvfedmekcAVKLAKMVGYVSAGTVEYLYSQDSSFYFLELNPR 441
Cdd:PLN02735 806 gimehieqaGVHSGDSACSLPTQTIPSSCLATIRDW---------TTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR 875
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
300-468 |
5.28e-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: 51.07 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 300 AAEQVGFPVMVKASEGGGGKGIRKVNCAE-DFPNLYrqVQAEVPGSPIFVMQLA--KHARHLEV--QILAD------QYG 368
Cdd:COG2232 133 EPPPDPGPWLVKPIGGAGGWHIRPADSEApPAPGRY--FQRYVEGTPASVLFLAdgSDARVLGFnrQLIGPagerpfRYG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 369 NAISLFGRDCSVQRRhqkiieeapatiatsdvfedMEKCAVKLAKMVGYVSAGTVEYLYSqDSSFYFLELNPRLQVEHPC 448
Cdd:COG2232 211 GNIGPLALPPALAEE--------------------MRAIAEALVAALGLVGLNGVDFILD-GDGPYVLEVNPRPQASLDL 269
|
170 180
....*....|....*....|
gi 1207175556 449 TEMVADVNLPAAQLQIAMGI 468
Cdd:COG2232 270 YEDATGGNLFDAHLRACRGE 289
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
291-441 |
2.35e-05 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 49.49 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 291 VHDVEAGLKAAEQVGFPVMVKASE--GGGGKGIrkVNCAEDFPNLYRQVQAEVPGSPIFVMQLAKHARHLEVQILADQYG 368
Cdd:COG0458 135 ATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGED 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 369 NAISLfgrdCSVQrrHqkiIEEA-----------PATIATSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYsQDSSFYFLE 437
Cdd:COG0458 213 NVIIV----GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAV-DDGRVYVIE 282
|
....
gi 1207175556 438 LNPR 441
Cdd:COG0458 283 VNPR 286
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
220-460 |
3.54e-05 |
|
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: 48.01 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 220 ELLHKNGIAFMGPPsQAMWALGDKIASSIVAQTAGIPTlPwsgtgltvewtendqkkgiinvPTELyeqgcVHDVEAGLK 299
Cdd:COG0189 75 RQLEAAGVPVVNDP-EAIRRARDKLFTLQLLARAGIPV-P----------------------PTLV-----TRDPDDLRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 300 AAEQVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQVQAEvpGSPIFVMQ---LAKHARHLEVQILADQYgnaislFGr 376
Cdd:COG0189 126 FLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTEL--GSEPVLVQefiPEEDGRDIRVLVVGGEP------VA- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 377 dcSVQRR----HQKIIEEAPATIATSDVFEDMEKCAVKLAKMVGYVSAGtVEYLYSQDsSFYFLELNPRLQVEHpcTEMV 452
Cdd:COG0189 197 --AIRRIpaegEFRTNLARGGRAEPVELTDEERELALRAAPALGLDFAG-VDLIEDDD-GPLVLEVNVTPGFRG--LERA 270
|
....*...
gi 1207175556 453 ADVNLPAA 460
Cdd:COG0189 271 TGVDIAEA 278
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
239-335 |
5.16e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 44.72 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 239 ALG-DKIASSIVAQTAGIPTLPWSgtgltvewtendqkkgiinvptelyeqgCVHDVEAGLKAAEQVGFPVMVKASEGGG 317
Cdd:PRK01372 94 ALAmDKLRTKLVWQAAGLPTPPWI----------------------------VLTREEDLLAAIDKLGLPLVVKPAREGS 145
|
90
....*....|....*...
gi 1207175556 318 GKGIRKVNCAEDFPNLYR 335
Cdd:PRK01372 146 SVGVSKVKEEDELQAALE 163
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
265-441 |
7.34e-04 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 44.10 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 265 LTVEW-TENDqkkgiINVPTElYEQGCVHDVEAGLKAAEqVGFPVMVKASEGGGGKGIRKVNCAEDFPNLYRQ-----VQ 338
Cdd:PRK12767 114 LTYEFlKENG-----IPTPKS-YLPESLEDFKAALAKGE-LQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYvpnliIQ 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 339 AEVPGSPIfvmqlakharhlEVQILADQYGNAISLFGRdcsvqRRHQKIIEEAPATIatSDVFEDMEKCAVKLAKMVGYV 418
Cdd:PRK12767 187 EFIEGQEY------------TVDVLCDLNGEVISIVPR-----KRIEVRAGETSKGV--TVKDPELFKLAERLAEALGAR 247
|
170 180
....*....|....*....|...
gi 1207175556 419 SAGTVEYLYSqDSSFYFLELNPR 441
Cdd:PRK12767 248 GPLNIQCFVT-DGEPYLFEINPR 269
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
280-441 |
2.16e-03 |
|
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: 41.09 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 280 NVPTELYEQgcVHDVEAGLKAAEQVGFPVMVKASEGG-GGKGIRKVNCAEDFPnlyrQVQAEVPGSPIFVMQLAKHARHL 358
Cdd:pfam02222 4 GLPTPRFMA--AESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLP----QAWEELGDGPVIVEEFVPFDREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 359 EVQILADQYGNAISlfgrdCS-VQRRHQK---IIEEAPATIaTSDVFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSSFY 434
Cdd:pfam02222 78 SVLVVRSVDGETAF-----YPvVETIQEDgicRLSVAPARV-PQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLL 151
|
....*..
gi 1207175556 435 FLELNPR 441
Cdd:pfam02222 152 INELAPR 158
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
307-443 |
2.43e-03 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 40.83 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 307 PVMVKASEGGGGKGIRKVN-----CAEDFPNLyrqVQAEVPGSPIFVMQLAKHARHLEVQIlADQY-GNAISLFGRD-CS 379
Cdd:pfam02655 33 KYVVKPRDGCGGEGVRKVEngredEAFIENVL---VQEFIEGEPLSVSLLSDGEKALPLSV-NRQYiDNGGSGFVYAgNV 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207175556 380 VQRRH---QKIIEEApatiatsdvfEDMEKCAVKLAKMVGyvsagtVEYLYSqDSSFYFLELNPRLQ 443
Cdd:pfam02655 109 TPSRTelkEEIIELA----------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 ... |
251-440 |
3.87e-03 |
|
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: 41.15 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 251 QTAGIPTLPWSGTgLTVEWTENDQKKgiinvptelyeqgCVHDVEAglkaaeqVGFPVMVKASEGGGGKGIRKVNCAE-- 328
Cdd:pfam07478 3 KAAGLPVVPFVTF-TRADWKLNPKEW-------------CAQVEEA-------LGYPVFVKPARLGSSVGVSKVESREel 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207175556 329 -DFPNLYRQVQAEVpgspifVMQLAKHARHLEVQILADQYGNAISLfGR---DCSVQRRHQKIIEEA-----PATIATSd 399
Cdd:pfam07478 62 qAAIEEAFQYDEKV------LVEEGIEGREIECAVLGNEDPEVSPV-GEivpSGGFYDYEAKYIDDSaqivvPADLEEE- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207175556 400 VFEDMEKCAVKLAKMVGYVSAGTVEYLYSQDSSFYFLELNP 440
Cdd:pfam07478 134 QEEQIQELALKAYKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
749-812 |
6.58e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 42.05 E-value: 6.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207175556 749 NDPSVLRSPSAGKLIQYTVEDGGHVFAGQCYAEIEVMKMVMTLTASESGCI-HYVKRAGAVLEPG 812
Cdd:PRK12999 1074 GNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVkRVLVKAGDQVEAG 1138
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