|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
687-1371 |
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: 680.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 687 TLDSPSKANESSLYRGELPVLGPPLIEGSRPNHKLRVLINRLENILNGYHENSGIETTLKELIKILRDGRLPYSEWDSQI 766
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDNQVIMNETLKDLIEVLRDPELPYLEWQEQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 767 STVRNRLPRQLNEGLGNLVKKSVS----FPAKELHKLMKRYLEENTN---DHVVYVALQPLLKISERYSEGLANHECEIF 839
Cdd:pfam08326 81 SALSGRIPAKLEASLRQLVERAHSrsaeFPAKQLRKILDKFLAELVLkadRDLFEATLAPLVDLVERYRNGLKGHEYSVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 840 LKLIKKYYAVEKIFENHDIHEERNLLNLRRKDLTNLKKILCISLSHANVVAKNKLVTAILHEYEPLCQDSSKMSLKFRAV 919
Cdd:pfam08326 161 ASLLEEYYDVEKLFSGGNVREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNCPNVSNVAKELRPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 920 IHDLASLESKWAKEVAVKARSVLLRGIFPPIKKRKEHIKTLLQLHIKDTGAENIHSRNIYSCMRDFGNLIHSNLIQLQDL 999
Cdd:pfam08326 241 LKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYGESGWKHREPSLEVLKELIDSKYTVFDVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1000 FFFFGHQDTALSSIASEIYARYAYGNYQLKSIKIHKGAPD-LLMSWQFsSLRNYLVNSDGESDEFTKLSKPP-----STS 1073
Cdd:pfam08326 321 PPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSpPIVSWQF-QLPSSHSSEFGSPLSPSSDSSPPfkriaSVS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1074 GKSSANS--------FGLLVNMRALESLEKTLDEVYEQIHIPEER----LSSGENSLIVNILspIRYR----SENDLIKT 1137
Cdd:pfam08326 400 DLSYLVNksedeplrTGAMVAFKSLDDLEEALPRALEEFPSEPEEsgesNSSDEPINVLNVA--IRDAegsdSDEELLER 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1138 LKIKLHENERGLSKLKVNRITFAFIAANAPAVKFYSFDGT-TYDEISQIRNMDPSYEAPLELGKMSNYKIRSLPTYDSSI 1216
Cdd:pfam08326 478 LEEILKENKEELLAAGVRRITFIIGRKDGQYPKYFTFRGPdNYEEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENRQI 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1217 RIFEGISKFTPLDKRFFVRKIINSFMYNDQKTTEENLKAEINAQVVYMLEHLGAVDI--SNSDLNHIFLSFNTVLNIPVH 1294
Cdd:pfam08326 558 HLYEAVGKENPTDKRFFVRAIIRPGRLRDDIPTAEYLISEAERLLNDILDALEVASIgnSNSDLNHIFLNFVPVFNVDPE 637
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323863 1295 RLEEIVSTILKTHETRLFQERITDVEICISVECLETKKPAPLRLLISNKSGYVVKIETYYEKIGKNGNLILEPCSEQ 1371
Cdd:pfam08326 638 DVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGPPIPLRLVITNVSGYVVKVELYREVKDDKGEWVFKSIGKP 714
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1469-2026 |
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: 608.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1469 PEYPEGRNMIVISNDITYNIGSFGPREDLFFDRVTNYARERgIPRIYLAANSGAKLGIAEELIPLFRVAWNDPSDPTKGF 1548
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1549 QYLylaPKDMQLLKDsgkgnsvvvehkmvyGEERYIIKAIVGFEEGLGVECLQGSGLIAGATSKAYRDIFTITAVTCRSV 1628
Cdd:pfam01039 80 KIL---RAMEIAIKT---------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1629 GIGSYLVRLGQRTIQVED-KPIILTGASAINKVLGtDIYTSNLQIGGTQIMYKNGIAHLTASNDMKAIEKIMTWLSYVPA 1707
Cdd:pfam01039 142 GGGAYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1708 KRDM---SPPLLETMDRWDRD---VDFKPAK-QVPYEARWLIEgkwdsnnnfqsGLFDKDSFFETLSGWAKGVIVGRARL 1780
Cdd:pfam01039 221 PAPNnrePVPIVPTKDPPDRDaplVSIVPDDpKKPYDVREVIA-----------GIVDEGEFFEIKPGYAKTVVTGFARL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1781 GGIPVGVIAVETKtieeiipadpanldssefsvKEAGqVWYPNSAFKTAQTINDFNYgEQLPLIILANWRGFSGGQRDMY 1860
Cdd:pfam01039 290 GGIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDA-FNLPLVILADVPGFLPGQRQEY 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1861 NEVLKYGSFIVDALVDYKQPILIYIPPfgELRGGSWVVIDPTINPEQMeMYADVESRGGVLEPDGVVSIKYRKEKMIETM 1940
Cdd:pfam01039 348 GGILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEM 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1941 IRLDstyghLRRTLTEKklslekqndltkrLKIRERQLIPIYNQISIQFADLHDRSTRMLVKGVIRNELEWKKsRRFLYW 2020
Cdd:pfam01039 425 RGKD-----LAATRKQK-------------IAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTK-PRFFPW 485
|
....*.
gi 6323863 2021 RLRRRL 2026
Cdd:pfam01039 486 RKHGNI 491
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
22-507 |
1.84e-129 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 415.18 E-value: 1.84e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 22 VMATPDdlhANSEYIRMADQYVQVPGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHASENPCLPELLAssQRKILFIGP 101
Cdd:COG4770 31 VYSDAD---RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGYGFLSENADFAEACE--DAGIVFIGP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 102 PGRAMRSLGDKISSTIVAQSAKIPCIPWSgshidtihidnktnfvsvpddvyvRGCCSSPEDALEKAKLIGFPVMIKASE 181
Cdd:COG4770 106 SPEAIRAMGDKIAAKKLMKAAGVPVVPGS------------------------DGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 182 GGGGKGIRRVDNEDDFIALYRQAVNETP---GSP-MFVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEE 257
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 258 APVTITKPETFQRMERAAIRLGELVGYVSAGTVEYLYSPkDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIP 337
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDA-DGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 338 mhmisdirklygLDPTGtsyidfknlKRPSPKGHCISCRITSEDPNEGFKPSTGKIHELNFRSSSNV---WGYFSvgnNG 414
Cdd:COG4770 321 ------------LPFTQ---------EDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVrvdSGVYE---GY 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 415 AIHSFSDSQFGHIFAVGNDRQDAKQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDDLILKNLSSDSKL 494
Cdd:COG4770 377 EIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG-VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
490
....*....|...
gi 6323863 495 DPTLAiicgAAMK 507
Cdd:COG4770 456 ELALA----AAMK 464
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
31-490 |
2.98e-105 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 345.25 E-value: 2.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 31 ANSEYIRMADQYVQVPGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHASENPCLPELLASSQrkILFIGPPGRAMRSLG 110
Cdd:PRK08591 37 RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPGYGFLSENADFAEICEDSG--FTFIGPSAETIRLMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 111 DKISSTIVAQSAKIPCIPwsGShidtihidnktnfvsvpddvyvRGCCSSPEDALEKAKLIGFPVMIKASEGGGGKGIRR 190
Cdd:PRK08591 115 DKVTAKATMKKAGVPVVP--GS----------------------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 191 VDNEDDFIALYRQAVNETP---GSPMFVM-KVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEAPVTITKPE 266
Cdd:PRK08591 171 VRTEAELEKAFSMARAEAKaafGNPGVYMeKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 267 TFQRMERAAIRLGELVGYVSAGTVEYLYSpKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPMHMI-SDIR 345
Cdd:PRK08591 251 LRRKIGEAAVKAAKAIGYRGAGTIEFLYE-KNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSIKqEDIV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 346 klygldptgtsyidfknlkrpsPKGHCISCRITSEDPNEGFKPSTGKI---HE---LNFRSSSNVW-GYfsvgnngAIHS 418
Cdd:PRK08591 330 ----------------------FRGHAIECRINAEDPAKNFMPSPGKItryHPpggPGVRVDSAVYtGY-------TIPP 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323863 419 FSDSQFGHIFAVGNDRQDAKQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDDLILKNLSS 490
Cdd:PRK08591 381 YYDSMIGKLIVHGETREEAIARMKRALSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
23-483 |
1.84e-90 |
|
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: 302.45 E-value: 1.84e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 23 MATPDDLHanseyIRMADQYVQVPGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHASENPCLPELLASSQrkILFIGPP 102
Cdd:TIGR00514 34 TADRDALH-----VLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPGYGFLSENANFAEQCERSG--FTFIGPS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 103 GRAMRSLGDKISSTIVAQSAKIPCIPWSGSHIDTIhidnktnfvsvpddvyvrgccsspEDALEKAKLIGFPVMIKASEG 182
Cdd:TIGR00514 107 AESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDE------------------------EENVRIAKRIGYPVIIKATAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 183 GGGKGIRRVDNEDDFIALYRQAVNETP---GSPMFVM-KVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEA 258
Cdd:TIGR00514 163 GGGRGMRVVREPDELVKSISMTRAEAKaafGNDGVYIeKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 259 PVTITKPETFQRMERAAIRLGELVGYVSAGTVEYLYSpKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPM 338
Cdd:TIGR00514 243 PSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLD-KNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 339 HMISDIRKLygldptgtsyidfknlkrpspKGHCISCRITSEDPNEGFKPSTGKIHE------LNFRSSSNVW-GYfsvg 411
Cdd:TIGR00514 322 SLKQEDVVV---------------------RGHAIECRINAEDPIKTFLPSPGRITRylppggPGVRWDSHVYsGY---- 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323863 412 nngAIHSFSDSQFGHIFAVGNDRQDAKQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDDL 483
Cdd:TIGR00514 377 ---TVPPYYDSMIGKLITYGKTREVAIARMKRALSEFIIDG-IKTTIPFHQRILEDENFQHGGTNIHYLEKK 444
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
111-338 |
7.88e-63 |
|
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: 213.71 E-value: 7.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 111 DKISSTIVAQSAKIPCIPWSGSHIDTIhidnktnfvsvpddvyvrgccsspEDALEKAKLIGFPVMIKASEGGGGKGIRR 190
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETE------------------------EEALAAAKEIGYPVIIKAAFGGGGLGMGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 191 VDNEDDFIALYRQAVNETP---GSPM-FVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEAPVTITKPE 266
Cdd:pfam02786 57 ARNEEELAELFALALAEAPaafGNPQvLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323863 267 TFQRMERAAIRLGELVGYVSAGTVEYLYSPKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPM 338
Cdd:pfam02786 137 ERQMLREAAVKIARHLGYVGAGTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
375-481 |
1.38e-30 |
|
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: 117.13 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 375 CRITSEDPNEGFKPSTGKIHELNFRSSSNVwgYFSVGNNG--AIHSFSDSQFGHIFAVGNDRQDAKQNMVLALKDFSIRG 452
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEgyEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 6323863 453 eFKTPIEYLIELLETRDFESNNISTGWLD 481
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
621-686 |
1.34e-21 |
|
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: 90.17 E-value: 1.34e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323863 621 QVISPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKL 686
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVkEILVKEGDQVEAGQLLVVI 67
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
620-686 |
1.54e-18 |
|
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: 81.49 E-value: 1.54e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323863 620 TQVISPTPGKLV-----KYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVIELLRQP-GSIIEAGDVIAKL 686
Cdd:pfam00364 1 TEIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1596-1852 |
1.13e-14 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 79.30 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1596 GVECLQGSGLIAGATSKAYRDIFTITAVTCRSVGIGSYLVRLGQRTIQVEDKPII-LTGASAINKVLGTDIytSNLQIGG 1674
Cdd:COG4799 134 GVESFAGYGRIFYRNARSSGGIPQISVIMGPCAAGGAYSPALSDFVIMVKGTSQMfLGGPPVVKAATGEEV--TAEELGG 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1675 TQI-MYKNGIAHLTASNDMKAIEKIMTWLSYVPAKRDMSPPLLETMD--RWDRDV-DFKPAKQ-VPYEARWLIEGkwdsn 1749
Cdd:COG4799 212 ADVhARVSGVADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPpaRDPEELyGIVPEDPrKPYDMREVIAR----- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1750 nnfqsgLFDKDSFFETLSGWAKGVIVGRARLGGIPVGVIAvetktieeiipADPANLdssefsvkeAGqVWYPNSAFKTA 1829
Cdd:COG4799 287 ------LVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA-----------NQPMVL---------AG-VLDIDAADKAA 339
|
250 260
....*....|....*....|....*.
gi 6323863 1830 QTI---NDFNygeqLPLIILANWRGF 1852
Cdd:COG4799 340 RFIrlcDAFN----IPLVFLVDVPGF 361
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
618-686 |
4.94e-12 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 71.71 E-value: 4.94e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 618 NPTQVISPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKL 686
Cdd:PRK12999 1075 NPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVkRVLVKAGDQVEAGDLLVEL 1144
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
618-686 |
5.19e-12 |
|
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: 71.65 E-value: 5.19e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 618 NPTQVISPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKL 686
Cdd:COG1038 1075 NPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVkEVLVKEGDQVEAGDLLIEL 1144
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
624-710 |
3.47e-04 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 45.49 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 624 SPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKLT--LDSPSKANESSLY 700
Cdd:TIGR01347 11 SITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLqEILFKEGDTVESGQVLAILEegNDATAAPPAKSGE 90
|
90
....*....|
gi 6323863 701 RGELPVLGPP 710
Cdd:TIGR01347 91 EKEETPAASA 100
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
687-1371 |
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: 680.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 687 TLDSPSKANESSLYRGELPVLGPPLIEGSRPNHKLRVLINRLENILNGYHENSGIETTLKELIKILRDGRLPYSEWDSQI 766
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDNQVIMNETLKDLIEVLRDPELPYLEWQEQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 767 STVRNRLPRQLNEGLGNLVKKSVS----FPAKELHKLMKRYLEENTN---DHVVYVALQPLLKISERYSEGLANHECEIF 839
Cdd:pfam08326 81 SALSGRIPAKLEASLRQLVERAHSrsaeFPAKQLRKILDKFLAELVLkadRDLFEATLAPLVDLVERYRNGLKGHEYSVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 840 LKLIKKYYAVEKIFENHDIHEERNLLNLRRKDLTNLKKILCISLSHANVVAKNKLVTAILHEYEPLCQDSSKMSLKFRAV 919
Cdd:pfam08326 161 ASLLEEYYDVEKLFSGGNVREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNCPNVSNVAKELRPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 920 IHDLASLESKWAKEVAVKARSVLLRGIFPPIKKRKEHIKTLLQLHIKDTGAENIHSRNIYSCMRDFGNLIHSNLIQLQDL 999
Cdd:pfam08326 241 LKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYGESGWKHREPSLEVLKELIDSKYTVFDVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1000 FFFFGHQDTALSSIASEIYARYAYGNYQLKSIKIHKGAPD-LLMSWQFsSLRNYLVNSDGESDEFTKLSKPP-----STS 1073
Cdd:pfam08326 321 PPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSpPIVSWQF-QLPSSHSSEFGSPLSPSSDSSPPfkriaSVS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1074 GKSSANS--------FGLLVNMRALESLEKTLDEVYEQIHIPEER----LSSGENSLIVNILspIRYR----SENDLIKT 1137
Cdd:pfam08326 400 DLSYLVNksedeplrTGAMVAFKSLDDLEEALPRALEEFPSEPEEsgesNSSDEPINVLNVA--IRDAegsdSDEELLER 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1138 LKIKLHENERGLSKLKVNRITFAFIAANAPAVKFYSFDGT-TYDEISQIRNMDPSYEAPLELGKMSNYKIRSLPTYDSSI 1216
Cdd:pfam08326 478 LEEILKENKEELLAAGVRRITFIIGRKDGQYPKYFTFRGPdNYEEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENRQI 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1217 RIFEGISKFTPLDKRFFVRKIINSFMYNDQKTTEENLKAEINAQVVYMLEHLGAVDI--SNSDLNHIFLSFNTVLNIPVH 1294
Cdd:pfam08326 558 HLYEAVGKENPTDKRFFVRAIIRPGRLRDDIPTAEYLISEAERLLNDILDALEVASIgnSNSDLNHIFLNFVPVFNVDPE 637
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323863 1295 RLEEIVSTILKTHETRLFQERITDVEICISVECLETKKPAPLRLLISNKSGYVVKIETYYEKIGKNGNLILEPCSEQ 1371
Cdd:pfam08326 638 DVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGPPIPLRLVITNVSGYVVKVELYREVKDDKGEWVFKSIGKP 714
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1469-2026 |
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: 608.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1469 PEYPEGRNMIVISNDITYNIGSFGPREDLFFDRVTNYARERgIPRIYLAANSGAKLGIAEELIPLFRVAWNDPSDPTKGF 1548
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1549 QYLylaPKDMQLLKDsgkgnsvvvehkmvyGEERYIIKAIVGFEEGLGVECLQGSGLIAGATSKAYRDIFTITAVTCRSV 1628
Cdd:pfam01039 80 KIL---RAMEIAIKT---------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1629 GIGSYLVRLGQRTIQVED-KPIILTGASAINKVLGtDIYTSNLQIGGTQIMYKNGIAHLTASNDMKAIEKIMTWLSYVPA 1707
Cdd:pfam01039 142 GGGAYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1708 KRDM---SPPLLETMDRWDRD---VDFKPAK-QVPYEARWLIEgkwdsnnnfqsGLFDKDSFFETLSGWAKGVIVGRARL 1780
Cdd:pfam01039 221 PAPNnrePVPIVPTKDPPDRDaplVSIVPDDpKKPYDVREVIA-----------GIVDEGEFFEIKPGYAKTVVTGFARL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1781 GGIPVGVIAVETKtieeiipadpanldssefsvKEAGqVWYPNSAFKTAQTINDFNYgEQLPLIILANWRGFSGGQRDMY 1860
Cdd:pfam01039 290 GGIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDA-FNLPLVILADVPGFLPGQRQEY 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1861 NEVLKYGSFIVDALVDYKQPILIYIPPfgELRGGSWVVIDPTINPEQMeMYADVESRGGVLEPDGVVSIKYRKEKMIETM 1940
Cdd:pfam01039 348 GGILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEM 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1941 IRLDstyghLRRTLTEKklslekqndltkrLKIRERQLIPIYNQISIQFADLHDRSTRMLVKGVIRNELEWKKsRRFLYW 2020
Cdd:pfam01039 425 RGKD-----LAATRKQK-------------IAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTK-PRFFPW 485
|
....*.
gi 6323863 2021 RLRRRL 2026
Cdd:pfam01039 486 RKHGNI 491
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
22-507 |
1.84e-129 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 415.18 E-value: 1.84e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 22 VMATPDdlhANSEYIRMADQYVQVPGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHASENPCLPELLAssQRKILFIGP 101
Cdd:COG4770 31 VYSDAD---RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGYGFLSENADFAEACE--DAGIVFIGP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 102 PGRAMRSLGDKISSTIVAQSAKIPCIPWSgshidtihidnktnfvsvpddvyvRGCCSSPEDALEKAKLIGFPVMIKASE 181
Cdd:COG4770 106 SPEAIRAMGDKIAAKKLMKAAGVPVVPGS------------------------DGPVQDAEEALAIAEEIGYPVLIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 182 GGGGKGIRRVDNEDDFIALYRQAVNETP---GSP-MFVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEE 257
Cdd:COG4770 162 GGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 258 APVTITKPETFQRMERAAIRLGELVGYVSAGTVEYLYSPkDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIP 337
Cdd:COG4770 242 APSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDA-DGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 338 mhmisdirklygLDPTGtsyidfknlKRPSPKGHCISCRITSEDPNEGFKPSTGKIHELNFRSSSNV---WGYFSvgnNG 414
Cdd:COG4770 321 ------------LPFTQ---------EDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVrvdSGVYE---GY 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 415 AIHSFSDSQFGHIFAVGNDRQDAKQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDDLILKNLSSDSKL 494
Cdd:COG4770 377 EIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG-VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
490
....*....|...
gi 6323863 495 DPTLAiicgAAMK 507
Cdd:COG4770 456 ELALA----AAMK 464
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
31-490 |
2.98e-105 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 345.25 E-value: 2.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 31 ANSEYIRMADQYVQVPGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHASENPCLPELLASSQrkILFIGPPGRAMRSLG 110
Cdd:PRK08591 37 RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPGYGFLSENADFAEICEDSG--FTFIGPSAETIRLMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 111 DKISSTIVAQSAKIPCIPwsGShidtihidnktnfvsvpddvyvRGCCSSPEDALEKAKLIGFPVMIKASEGGGGKGIRR 190
Cdd:PRK08591 115 DKVTAKATMKKAGVPVVP--GS----------------------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 191 VDNEDDFIALYRQAVNETP---GSPMFVM-KVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEAPVTITKPE 266
Cdd:PRK08591 171 VRTEAELEKAFSMARAEAKaafGNPGVYMeKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 267 TFQRMERAAIRLGELVGYVSAGTVEYLYSpKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPMHMI-SDIR 345
Cdd:PRK08591 251 LRRKIGEAAVKAAKAIGYRGAGTIEFLYE-KNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSIKqEDIV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 346 klygldptgtsyidfknlkrpsPKGHCISCRITSEDPNEGFKPSTGKI---HE---LNFRSSSNVW-GYfsvgnngAIHS 418
Cdd:PRK08591 330 ----------------------FRGHAIECRINAEDPAKNFMPSPGKItryHPpggPGVRVDSAVYtGY-------TIPP 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323863 419 FSDSQFGHIFAVGNDRQDAKQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDDLILKNLSS 490
Cdd:PRK08591 381 YYDSMIGKLIVHGETREEAIARMKRALSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
54-482 |
7.30e-100 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 350.21 E-value: 7.30e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 54 YANIDLILDVAEQTDVDAVWAGWGHASENPCLPEllASSQRKILFIGPPGRAMRSLGDKISSTIVAQSAKIPCIPWSGSH 133
Cdd:PRK12999 64 YLDIDEIIRVAKQAGVDAIHPGYGFLSENPEFAR--ACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 134 IDtihidnktnfvsvpddvyvrgccsSPEDALEKAKLIGFPVMIKASEGGGGKGIRRVDNEDDFIALYRQAVNETP---G 210
Cdd:PRK12999 142 ID------------------------DIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 211 SP-MFVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEAP-VTITkPETFQRMERAAIRLGELVGYVSAG 288
Cdd:PRK12999 198 NDeVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPaPGLS-EELRERICEAAVKLARAVGYVNAG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 289 TVEYLYSPkDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPMHmisdirklyglDPTgtsyIDFKNLKRPSP 368
Cdd:PRK12999 277 TVEFLVDA-DGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATLH-----------DLE----IGIPSQEDIRL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 369 KGHCISCRITSEDPNEGFKPSTGKIHElnFRSSsnvwGYFSV---GNN---GA-IHSFSDSQFGHIFAVGNDRQDAKQNM 441
Cdd:PRK12999 341 RGYAIQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVrldGGNafaGAeITPYYDSLLVKLTAWGRTFEQAVARM 414
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 6323863 442 VLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDD 482
Cdd:PRK12999 415 RRALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFIDE 454
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
54-482 |
3.30e-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: 348.22 E-value: 3.30e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 54 YANIDLILDVAEQTDVDAVWAGWGHASENPCLPEllASSQRKILFIGPPGRAMRSLGDKISSTIVAQSAKIPCIPwsgsh 133
Cdd:COG1038 63 YLDIEEIIRVAKEKGVDAIHPGYGFLSENPEFAR--ACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP----- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 134 idtihidnktnfvSVPDDVyvrgccSSPEDALEKAKLIGFPVMIKASEGGGGKGIRRVDNEDDFIALYRQAVNETP---G 210
Cdd:COG1038 136 -------------GTEGPV------DDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 211 SP-MFVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEAP-VTITkPETFQRMERAAIRLGELVGYVSAG 288
Cdd:COG1038 197 DDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPaPNLD-EELREAICEAAVKLAKAVGYVNAG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 289 TVEYLYSpKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPMHmisdirklyglDPTgtsyIDFKNLKRPSP 368
Cdd:COG1038 276 TVEFLVD-DDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSLD-----------DPE----IGIPSQEDIRL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 369 KGHCISCRITSEDPNEGFKPSTGKIheLNFRSSSnvwGyFSV----GN--NGAIHS-FSDSQFGHIFAVGNDRQDAKQNM 441
Cdd:COG1038 340 NGYAIQCRITTEDPANNFMPDTGRI--TAYRSAG---G-FGIrldgGNayTGAVITpYYDSLLVKVTAWGRTFEEAIRKM 413
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 6323863 442 VLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDD 482
Cdd:COG1038 414 RRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFIDE 453
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
31-482 |
4.03e-99 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 327.76 E-value: 4.03e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 31 ANSEYIRMADQYVQVPGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHASENPCLPEllASSQRKILFIGPPGRAMRSLG 110
Cdd:PRK06111 37 RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPGYGLLSENASFAE--RCKEEGIVFIGPSADIIAKMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 111 DKISSTIVAQSAKIPCIPWSGSHIDtihidnktnfvsvpddvyvrgccsSPEDALEKAKLIGFPVMIKASEGGGGKGIRR 190
Cdd:PRK06111 115 SKIEARRAMQAAGVPVVPGITTNLE------------------------DAEEAIAIARQIGYPVMLKASAGGGGIGMQL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 191 VDNEDDF---IALYRQAVNETPGSP-MFVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEAPVTITKPE 266
Cdd:PRK06111 171 VETEQELtkaFESNKKRAANFFGNGeMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 267 TFQRMERAAIRLGELVGYVSAGTVEYLYSpKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPM-HMISDIR 345
Cdd:PRK06111 251 TRKAMGERAVQAAKAIGYTNAGTIEFLVD-EQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 346 KlygldptgtsyidfknlkrpspKGHCISCRITSEDPNEgFKPSTGKIHELNFRSSSNVWGYFSVGNNGAIHSFSDSQFG 425
Cdd:PRK06111 330 R----------------------SGHAIEVRIYAEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323863 426 HIFAVGNDRQDAKQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDD 482
Cdd:PRK06111 387 KLIAHGETREEAISRLHDALEELKVEG-IKTNIPLLLQVLEDPVFKAGGYTTGFLTK 442
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
32-482 |
1.82e-93 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 313.07 E-value: 1.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 32 NSEYIRMADQYVQVPGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHASENPCLPELLAssQRKILFIGPPGRAMRSLGD 111
Cdd:PRK08654 38 NALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGYGFLAENPEFAKACE--KAGIVFIGPSSDVIEAMGS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 112 KISSTIVAQSAKIPCIPWSGSHIDtihidnktnfvsvpddvyvrgccsSPEDALEKAKLIGFPVMIKASEGGGGKGIRRV 191
Cdd:PRK08654 116 KINAKKLMKKAGVPVLPGTEEGIE------------------------DIEEAKEIAEEIGYPVIIKASAGGGGIGMRVV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 192 DNEDDFI-ALYR-QAVNETP-GSP-MFVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEAPVTITKPET 267
Cdd:PRK08654 172 YSEEELEdAIEStQSIAQSAfGDStVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 268 FQRMERAAIRLGELVGYVSAGTVEYLYSpkDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPMhmisdirkl 347
Cdd:PRK08654 252 RERMGEAAVKAAKAINYENAGTVEFLYS--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL--------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 348 ygldPTGTSYIDFknlkrpspKGHCISCRITSEDPNEGFKPSTGKIheLNFRS--------SSNVW-GYfsvgnngAIHS 418
Cdd:PRK08654 321 ----SFKQEDITI--------RGHAIECRINAEDPLNDFAPSPGKI--KRYRSpggpgvrvDSGVHmGY-------EIPP 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323863 419 FSDSQFGHIFAVGNDRQDAKQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDD 482
Cdd:PRK08654 380 YYDSMISKLIVWGRTREEAIARMRRALYEYVIVG-VKTNIPFHKAVMENENFVRGNLHTHFIEE 442
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
27-482 |
3.18e-91 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 304.71 E-value: 3.18e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 27 DDLHanseyIRMADQYVQVPGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHASENPCLPELlaSSQRKILFIGPPGRAM 106
Cdd:PRK05586 38 DALH-----VQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPGFGFLSENSKFAKM--CKECNIVFIGPDSETI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 107 RSLGDKISSTIVAQSAKIPCIPWSGSHIDtihidnktnfvsvpddvyvrgccsSPEDALEKAKLIGFPVMIKASEGGGGK 186
Cdd:PRK05586 111 ELMGNKSNAREIMIKAGVPVVPGSEGEIE------------------------NEEEALEIAKEIGYPVMVKASAGGGGR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 187 GIRRVDNEDDFIALYRQAVNETPGS----PMFVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEAPVTI 262
Cdd:PRK05586 167 GIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 263 TKPETFQRMERAAIRLGELVGYVSAGTVEYLYSpKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPMHMIS 342
Cdd:PRK05586 247 MTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 343 DIRKLygldptgtsyidfknlkrpspKGHCISCRITSEDPNEGFKPSTGKIHELNFRSSSNVWGYFSVGNNGAIHSFSDS 422
Cdd:PRK05586 326 EDIKI---------------------NGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDS 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 423 QFGHIFAVGNDRQDAKQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDD 482
Cdd:PRK05586 385 MIGKLIVYGKDREEAIQKMKRALGEFIIEG-VNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
23-483 |
1.84e-90 |
|
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: 302.45 E-value: 1.84e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 23 MATPDDLHanseyIRMADQYVQVPGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHASENPCLPELLASSQrkILFIGPP 102
Cdd:TIGR00514 34 TADRDALH-----VLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPGYGFLSENANFAEQCERSG--FTFIGPS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 103 GRAMRSLGDKISSTIVAQSAKIPCIPWSGSHIDTIhidnktnfvsvpddvyvrgccsspEDALEKAKLIGFPVMIKASEG 182
Cdd:TIGR00514 107 AESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDE------------------------EENVRIAKRIGYPVIIKATAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 183 GGGKGIRRVDNEDDFIALYRQAVNETP---GSPMFVM-KVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEA 258
Cdd:TIGR00514 163 GGGRGMRVVREPDELVKSISMTRAEAKaafGNDGVYIeKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 259 PVTITKPETFQRMERAAIRLGELVGYVSAGTVEYLYSpKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPM 338
Cdd:TIGR00514 243 PSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLD-KNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 339 HMISDIRKLygldptgtsyidfknlkrpspKGHCISCRITSEDPNEGFKPSTGKIHE------LNFRSSSNVW-GYfsvg 411
Cdd:TIGR00514 322 SLKQEDVVV---------------------RGHAIECRINAEDPIKTFLPSPGRITRylppggPGVRWDSHVYsGY---- 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323863 412 nngAIHSFSDSQFGHIFAVGNDRQDAKQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDDL 483
Cdd:TIGR00514 377 ---TVPPYYDSMIGKLITYGKTREVAIARMKRALSEFIIDG-IKTTIPFHQRILEDENFQHGGTNIHYLEKK 444
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
31-483 |
6.81e-87 |
|
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: 311.97 E-value: 6.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 31 ANSEYIRMADQYVQVPGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHASENPCLPELLASSqrKILFIGPPGRAMRSLG 110
Cdd:TIGR02712 36 AASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGYGFLSENAAFAEACEAA--GIVFVGPTPEQIRKFG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 111 DKISSTIVAQSAKIPCIPwsGShidtihidnktnfvsvpddvyvrGCCSSPEDALEKAKLIGFPVMIKASEGGGGKGIRR 190
Cdd:TIGR02712 114 LKHTARELAEAAGVPLLP--GT-----------------------GLLSSLDEALEAAKEIGYPVMLKSTAGGGGIGMQK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 191 VDNEDDFIALY----RQAVNETPGSPMFVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEAPVTITKPE 266
Cdd:TIGR02712 169 CDSAAELAEAFetvkRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEETPAPNLPPE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 267 TFQRMERAAIRLGELVGYVSAGTVEYLYSPKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAmgipmhmisdirk 346
Cdd:TIGR02712 249 TRQALLAAAERLGEAVNYRSAGTVEFIYDEARDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIA------------- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 347 lYGLDPtgtsyiDFKNLKRP-SPKGHCISCRITSEDPNEGFKPSTGKIHELNFRSSSNVWGYFSVGNNgaIHSFSDSQFG 425
Cdd:TIGR02712 316 -AGELP------DFASLNISlTPRGAAIEARVYAENPAKNFQPSPGLLTDVQFPDDVRVDTWVETGTE--VSPEYDPMLA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323863 426 HIFAVGNDRQDAKQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDDL 483
Cdd:TIGR02712 387 KIIVHGSDREDAILKLHQALAETRVYG-IETNLDYLRSILSSETFRSAQVSTRTLNSF 443
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
35-481 |
1.16e-85 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 288.57 E-value: 1.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 35 YIRMADQYVQVPGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHASENPCLPELlaSSQRKILFIGPPGRAMRSLGDKIS 114
Cdd:PRK08462 43 YLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGYGFLSENQNFVEI--CSHHNIKFIGPSVEVMALMSDKSK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 115 STIVAQSAKIPCIPWSgshidtihidnktnfvsvpddvyvRGCCSSPEDALEKAKLIGFPVMIKASEGGGGKGIRRVDNE 194
Cdd:PRK08462 121 AKEVMKRAGVPVIPGS------------------------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 195 DDFIALYRQAVNETPGS----PMFVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEAPVTITKPETFQR 270
Cdd:PRK08462 177 SDLENLYLAAESEALSAfgdgTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRER 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 271 MERAAIRLGELVGYVSAGTVEYLYSpKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPMHMISDIrklygl 350
Cdd:PRK08462 257 LHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESI------ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 351 dptgtsyidfknlkrpSPKGHCISCRITSEDPNEgFKPSTGKIHEL------NFRSSSNVWGYFSVGnngaihSFSDSQF 424
Cdd:PRK08462 330 ----------------KLKGHAIECRITAEDPKK-FYPSPGKITKWiapggrNVRMDSHAYAGYVVP------PYYDSMI 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 6323863 425 GHIFAVGNDRQDAKQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLD 481
Cdd:PRK08462 387 GKLIVWGEDRNRAIAKMKRALKEFKVEG-IKTTIPFHLEMMENADFINNKYDTKYLE 442
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
54-509 |
3.64e-82 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 279.29 E-value: 3.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 54 YANIDLILDVAEQTDVDAVWAGWGHASENPCLPELLAssQRKILFIGPPGRAMRSLGDKISSTIVAQSAKIPCIPWSGSH 133
Cdd:PRK07178 59 YLNPRRLVNLAVETGCDALHPGYGFLSENAELAEICA--ERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 134 IDTIhidnktnfvsvpddvyvrgccsspEDALEKAKLIGFPVMIKASEGGGGKGIRRVDNEDDFIALYRQAVNETP---G 210
Cdd:PRK07178 137 LADL------------------------DEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 211 SP-MFVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEAPVTITKPETFQRMERAAIRLGELVGYVSAGT 289
Cdd:PRK07178 193 SAeVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 290 VEYLYSpKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPMHMI-SDIRKlygldptgtsyidfknlkrpsp 368
Cdd:PRK07178 273 VEFLLD-ADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLSYKqEDIQH---------------------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 369 KGHCISCRITSEDPNEGFKPSTGKIHElnfrsssnvwgYFSVGNNG-----AIHS------FSDSQFGHIFAVGNDRQDA 437
Cdd:PRK07178 330 RGFALQFRINAEDPKNDFLPSFGKITR-----------YYAPGGPGvrtdtAIYTgytippYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323863 438 KQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDD-LILKNLSSDSKlDPTLAIICGAAMKAY 509
Cdd:PRK07178 399 LDRGRRALDDMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVEShPELTNYSIKRK-PEELAAAIAAAIAAH 469
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
54-482 |
9.44e-82 |
|
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: 295.20 E-value: 9.44e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 54 YANIDLILDVAEQTDVDAVWAGWGHASENPCLPEllASSQRKILFIGPPGRAMRSLGDKISSTIVAQSAKIPCIPWSGSH 133
Cdd:TIGR01235 60 YLSIDEIIRVAKLNGVDAIHPGYGFLSENSEFAD--ACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 134 IDTIhidnktnfvsvpddvyvrgccsspEDALEKAKLIGFPVMIKASEGGGGKGIRRVDNEDDFIALYRQAVNETPGS-- 211
Cdd:TIGR01235 138 PETM------------------------EEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfg 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 212 --PMFVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEAPVTITKPETFQRMERAAIRLGELVGYVSAGT 289
Cdd:TIGR01235 194 ndEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 290 VEYLYSpKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPMHmisdirklygldptgTSYIDFKNLKRPSPK 369
Cdd:TIGR01235 274 VEFLVD-NDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLP---------------TPQLGVPNQEDIRTN 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 370 GHCISCRITSEDPNEGFKPSTGKIHElnFRSSSNVWGYFSVGNN--GAIHS-FSDSQFGHIFAVGNDRQDAKQNMVLALK 446
Cdd:TIGR01235 338 GYAIQCRVTTEDPANNFQPDTGRIEA--YRSAGGFGIRLDGGNSyaGAIITpYYDSLLVKVSAWASTPEEAAAKMDRALR 415
|
410 420 430
....*....|....*....|....*....|....*.
gi 6323863 447 DFSIRGeFKTPIEYLIELLETRDFESNNISTGWLDD 482
Cdd:TIGR01235 416 EFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFIDT 450
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
37-481 |
3.08e-81 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 276.64 E-value: 3.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 37 RMADQYVQVPGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHASENPCLPEllASSQRKILFIGPPGRAMRSLGDKISST 116
Cdd:PRK12833 46 RMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPGYGFLSENAAFAE--AVEAAGLIFVGPDAQTIRTMGDKARAR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 117 IVAQSAKIPCIPWSGshidtihidnktnfvsvpddvyvrGCCSSPEDALEKAKLIGFPVMIKASEGGGGKGIRRVDNEDD 196
Cdd:PRK12833 124 RTARRAGVPTVPGSD------------------------GVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 197 FIALYRQAVNETP---GSP-MFVMKVVTDARHLEVQLLADqyGTN-ITLFGRDCSIQRRHQKIIEEAPVTITKPETFQRM 271
Cdd:PRK12833 180 LAAELPLAQREAQaafGDGgVYLERFIARARHIEVQILGD--GERvVHLFERECSLQRRRQKILEEAPSPSLTPAQRDAL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 272 ERAAIRLGELVGYVSAGTVEYLYSPKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPMHMI-SDIRKlygl 350
Cdd:PRK12833 258 CASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRFAqGDIAL---- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 351 dptgtsyidfknlkrpspKGHCISCRITSEDPNEGFKPSTGKIHELNF------RSSSNVW-GYfsvgnngAIHSFSDSQ 423
Cdd:PRK12833 334 ------------------RGAALECRINAEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYpGY-------RVPPFYDSL 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 6323863 424 FGHIFAVGNDRQDAKQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGWLD 481
Cdd:PRK12833 389 LAKLIVHGEDRAAALARAARALRELRIDG-MKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
13-509 |
1.41e-64 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 228.54 E-value: 1.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 13 NDEKIIQFVVMATPDdlhANSEYIRMADQYVQVpGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHASENPCLPELLASS 92
Cdd:PRK08463 22 RDLHIKSVAIYTEPD---RECLHVKIADEAYRI-GTDPIKGYLDVKRIVEIAKACGADAIHPGYGFLSENYEFAKAVEDA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 93 qrKILFIGPPGRAMRSLGDKISSTIVAQSAKIPCIPWSgshidtihidNKTNFVSVpddvyvrgccsspEDALEKAKLIG 172
Cdd:PRK08463 98 --GIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGT----------EKLNSESM-------------EEIKIFARKIG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 173 FPVMIKASEGGGGKGIRRVDNEDD----FIALYRQAVNETPGSPMFVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQ 248
Cdd:PRK08463 153 YPVILKASGGGGGRGIRVVHKEEDlenaFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 249 RRHQKIIEEAPVTITKPETFQRMERAAIRLGELVGYVSAGTVEYLYspkDD--KFYFLELNPRLQVEHPTTEMISGVNLP 326
Cdd:PRK08463 233 RRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLL---DDynRFYFMEMNTRIQVEHGVTEEITGIDLI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 327 ATQLQIAMGIPMHMI-SDIRklygldptgtsyidfknlkrpsPKGHCISCRITSEDPNEGFKPSTGKIHEL------NFR 399
Cdd:PRK08463 310 VRQIRIAAGEILDLEqSDIK----------------------PRGFAIEARITAENVWKNFIPSPGKITEYypalgpSVR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 400 SSSNVWGYFSvgnngaIHSFSDSQFGHIFAVGNDRQDAKQNMVLALKDFSIRGeFKTPIEYLIELLETRDFESNNISTGW 479
Cdd:PRK08463 368 VDSHIYKDYT------IPPYYDSMLAKLIVKATSYDLAVNKLERALKEFVIDG-IRTTIPFLIAITKTREFRRGYFDTSY 440
|
490 500 510
....*....|....*....|....*....|....
gi 6323863 480 LD----DLILKNLSSDSKLDPTLAIICGAAMKAY 509
Cdd:PRK08463 441 IEthmqELLEKTEDRHQENKEEVIAAIAAALKKI 474
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
111-338 |
7.88e-63 |
|
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: 213.71 E-value: 7.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 111 DKISSTIVAQSAKIPCIPWSGSHIDTIhidnktnfvsvpddvyvrgccsspEDALEKAKLIGFPVMIKASEGGGGKGIRR 190
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETE------------------------EEALAAAKEIGYPVIIKAAFGGGGLGMGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 191 VDNEDDFIALYRQAVNETP---GSPM-FVMKVVTDARHLEVQLLADQYGTNITLFGRDCSIQRRHQKIIEEAPVTITKPE 266
Cdd:pfam02786 57 ARNEEELAELFALALAEAPaafGNPQvLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323863 267 TFQRMERAAIRLGELVGYVSAGTVEYLYSPKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQLQIAMGIPM 338
Cdd:pfam02786 137 ERQMLREAAVKIARHLGYVGAGTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
57-337 |
5.57e-45 |
|
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: 164.28 E-value: 5.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 57 IDLILDVAEQTDVDAVWAGWGHASEnpclpelLASSQRKIL-FIGPPGRAMRSLGDKISSTIVAQSAKIPCIPWSgshid 135
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVE-------TAAELAEELgLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 136 tihidnktnfvsvpddvyvrgCCSSPEDALEKAKLIGFPVMIKASEGGGGKGIRRVDNEDDFIALYRQAVNET----PGS 211
Cdd:COG0439 74 ---------------------LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 212 PMFVMKVVtDARHLEVQLLADQyGTNITlfgrdCSIQRRHQK---IIE---EAPVTITkPETFQRMERAAIRLGELVGYV 285
Cdd:COG0439 133 EVLVEEFL-EGREYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPLP-EELRAEIGELVARALRALGYR 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6323863 286 -SAGTVEYLYSPkDDKFYFLELNPRLQVEH--PTTEMISGVNLPATQLQIAMGIP 337
Cdd:COG0439 205 rGAFHTEFLLTP-DGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
1-105 |
2.85e-31 |
|
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: 119.13 E-value: 2.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1 MRSIRKWAyetfndekiIQFVVMATPDDlhANSEYIRMADQYVQVPGGTNNNNYANIDLILDVAEQTDVDAVWAGWGHAS 80
Cdd:pfam00289 17 IRACRELG---------IRTVAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPGYGFLS 85
|
90 100
....*....|....*....|....*
gi 6323863 81 ENPCLPELLAssQRKILFIGPPGRA 105
Cdd:pfam00289 86 ENAEFARACE--EAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
375-481 |
1.38e-30 |
|
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: 117.13 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 375 CRITSEDPNEGFKPSTGKIHELNFRSSSNVwgYFSVGNNG--AIHSFSDSQFGHIFAVGNDRQDAKQNMVLALKDFSIRG 452
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEgyEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 6323863 453 eFKTPIEYLIELLETRDFESNNISTGWLD 481
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
375-482 |
2.33e-29 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 113.74 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 375 CRITSEDPNEGFKPSTGKIHELNFRSSSNVWGYFSVGNNGAIHSFSDSQFGHIFAVGNDRQDAKQNMVLALKDFSIRGeF 454
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*...
gi 6323863 455 KTPIEYLIELLETRDFESNNISTGWLDD 482
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
621-686 |
1.34e-21 |
|
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: 90.17 E-value: 1.34e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323863 621 QVISPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKL 686
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVkEILVKEGDQVEAGQLLVVI 67
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
620-686 |
1.54e-18 |
|
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: 81.49 E-value: 1.54e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323863 620 TQVISPTPGKLV-----KYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVIELLRQP-GSIIEAGDVIAKL 686
Cdd:pfam00364 1 TEIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
21-337 |
1.21e-17 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 87.29 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 21 VVMATPDDLHAN-SEYIrmaDQYVQVPGGTNNNNyANIDLILDVAEQTDVDAVWA---GWGHA-SENpcLPELlassQRK 95
Cdd:COG3919 32 IVVDRDPLGPAArSRYV---DEVVVVPDPGDDPE-AFVDALLELAERHGPDVLIPtgdEYVELlSRH--RDEL----EEH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 96 ILFIGPPGRAMRSLGDKISSTIVAQSAKIPcIPwsgshiDTIHIDnktnfvsvpddvyvrgccsSPEDALEKAKLIGFPV 175
Cdd:COG3919 102 YRLPYPDADLLDRLLDKERFYELAEELGVP-VP------KTVVLD-------------------SADDLDALAEDLGFPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 176 MIKASEG--------GGGKGIRRVDNEDDFIALYRQAvnETPGSPMFVMKVVT--DARHLEVQLLADQYGTnITLFgrdC 245
Cdd:COG3919 156 VVKPADSvgydelsfPGKKKVFYVDDREELLALLRRI--AAAGYELIVQEYIPgdDGEMRGLTAYVDRDGE-VVAT---F 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 246 SIQRRHQKIIEEAPVTITKPETFQRMERAAIRLGELVGYVSAGTVEYLYSPKDDKFYFLELNPRL--QVEHPTtemISGV 323
Cdd:COG3919 230 TGRKLRHYPPAGGNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRFwrSLYLAT---AAGV 306
|
330
....*....|....
gi 6323863 324 NLPATQLQIAMGIP 337
Cdd:COG3919 307 NFPYLLYDDAVGRP 320
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1596-1852 |
1.13e-14 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 79.30 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1596 GVECLQGSGLIAGATSKAYRDIFTITAVTCRSVGIGSYLVRLGQRTIQVEDKPII-LTGASAINKVLGTDIytSNLQIGG 1674
Cdd:COG4799 134 GVESFAGYGRIFYRNARSSGGIPQISVIMGPCAAGGAYSPALSDFVIMVKGTSQMfLGGPPVVKAATGEEV--TAEELGG 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1675 TQI-MYKNGIAHLTASNDMKAIEKIMTWLSYVPAKRDMSPPLLETMD--RWDRDV-DFKPAKQ-VPYEARWLIEGkwdsn 1749
Cdd:COG4799 212 ADVhARVSGVADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPpaRDPEELyGIVPEDPrKPYDMREVIAR----- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 1750 nnfqsgLFDKDSFFETLSGWAKGVIVGRARLGGIPVGVIAvetktieeiipADPANLdssefsvkeAGqVWYPNSAFKTA 1829
Cdd:COG4799 287 ------LVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA-----------NQPMVL---------AG-VLDIDAADKAA 339
|
250 260
....*....|....*....|....*.
gi 6323863 1830 QTI---NDFNygeqLPLIILANWRGF 1852
Cdd:COG4799 340 RFIrlcDAFN----IPLVFLVDVPGF 361
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
158-309 |
1.45e-14 |
|
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: 79.15 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 158 CSSPEDALEKAKLIGFPVMIKASE--GGGGKGIrrVDNEDDFIALYRQAVNETPGSPMFVMKVVTDARHLEVQLLADQYG 235
Cdd:COG0458 135 ATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGED 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 236 TNITLfgrdCSIQrrHqkiIEEA------------PVTITkPETFQRMERAAIRLGELVGYVSAGTVEYLYspKDDKFYF 303
Cdd:COG0458 213 NVIIV----GIME--H---IEPAgvhsgdsicvapPQTLS-DKEYQRLRDATLKIARALGVVGLCNIQFAV--DDGRVYV 280
|
....*.
gi 6323863 304 LELNPR 309
Cdd:COG0458 281 IEVNPR 286
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
159-335 |
1.02e-13 |
|
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: 77.35 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 159 SSPEDALEKAKLIGFPVMIKASEGGGGKGIRRVDNEDDFIALYRQAVNETPGSPMFVMKVVTDARHLEVQLLADqyGTNI 238
Cdd:TIGR01369 691 TSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEEV 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 239 TLFGrdcsIQrRHqkiIEEA------------PVTITKpETFQRMERAAIRLGELVGYVSAGTVEYLYspKDDKFYFLEL 306
Cdd:TIGR01369 769 LIPG----IM-EH---IEEAgvhsgdstcvlpPQTLSA-EIVDRIKDIVRKIAKELNVKGLMNIQFAV--KDGEVYVIEV 837
|
170 180
....*....|....*....|....*....
gi 6323863 307 NPRLQVEHPTTEMISGVNLPATQLQIAMG 335
Cdd:TIGR01369 838 NPRASRTVPFVSKATGVPLAKLAVRVMLG 866
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
618-686 |
4.94e-12 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 71.71 E-value: 4.94e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 618 NPTQVISPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKL 686
Cdd:PRK12999 1075 NPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVkRVLVKAGDQVEAGDLLVEL 1144
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
618-686 |
5.19e-12 |
|
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: 71.65 E-value: 5.19e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 618 NPTQVISPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKL 686
Cdd:COG1038 1075 NPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVkEVLVKEGDQVEAGDLLIEL 1144
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
158-310 |
6.67e-11 |
|
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: 68.10 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 158 CSSPEDALEKAKLIGFPVMIKASE--GGGGKGIrrVDNEDDFIALYRQAVNETPGSPMFVMKVVTDARHLEVQLLADQYG 235
Cdd:TIGR01369 148 AHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSND 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 236 TNITLfgrdCSIQR-----RHQ-KIIEEAPV-TITKPEtFQRMERAAIRLGELVGYVSAGTVEYLYSPKDDKFYFLELNP 308
Cdd:TIGR01369 226 NCITV----CNMENfdpmgVHTgDSIVVAPSqTLTDKE-YQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNP 300
|
..
gi 6323863 309 RL 310
Cdd:TIGR01369 301 RV 302
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
117-309 |
5.22e-10 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 65.18 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 117 IVAQSAKIPCIPWsGSHIDTIHI-DNKTNFVSVPDDVYVR----GCCSSPEDALEKAKLIGFPVMIKASEGGGGKGIRRV 191
Cdd:PLN02735 678 PPSASGNGNVKIW-GTSPDSIDAaEDRERFNAILNELKIEqpkgGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 192 DNEDDFIALYRQAVNETPGSPMFVMKVVTDARHLEVQLLADQYGtNITLFGrdcsIQRRhqkiIEEA-----------PV 260
Cdd:PLN02735 757 YSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEG-NVVIGG----IMEH----IEQAgvhsgdsacslPT 827
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6323863 261 TITKPETFQRMERAAIRLGELVGYVSAGTVEYLYSPkDDKFYFLELNPR 309
Cdd:PLN02735 828 QTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITP-SGEVYIIEANPR 875
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
131-338 |
7.18e-10 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 64.61 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 131 GSHIDTIH-IDNKTNFVSVPDDVYVR----GCCSSPEDALEKAKLIGFPVMIKASEGGGGKGIRRVDNEDDFIALYRQav 205
Cdd:PRK12815 659 GTSPDTIDrLEDRDRFYQLLDELGLPhvpgLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAE-- 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 206 NETPGSPMFVMKVVtDARHLEVQLLADqyGTNITLFGrdcSIQrrHqkiIEEA------------PVTITkPETFQRMER 273
Cdd:PRK12815 737 NASQLYPILIDQFI-DGKEYEVDAISD--GEDVTIPG---IIE--H---IEQAgvhsgdsiavlpPQSLS-EEQQEKIRD 804
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323863 274 AAIRLGELVGYVSAGTVEYLYspKDDKFYFLELNPRlqvehpttemiSGVNLPAtqLQIAMGIPM 338
Cdd:PRK12815 805 YAIKIAKKLGFRGIMNIQFVL--ANDEIYVLEVNPR-----------ASRTVPF--VSKATGVPL 854
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
156-309 |
1.63e-09 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 63.58 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 156 GCCSSPEDALEKAKLIGFPVMIKASEGGGGKGIRRVDNEDDFIALYRQAVNETPGSPMFVMKVVTDARHLEVQLLADqyG 235
Cdd:PRK05294 688 GTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD--G 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 236 TNITLFGrdcsiqrrhqkI---IEEA------------PVTITkPETFQRMERAAIRLG---ELVGYVSagtVEYLYspK 297
Cdd:PRK05294 766 EDVLIGG-----------ImehIEEAgvhsgdsacslpPQTLS-EEIIEEIREYTKKLAlelNVVGLMN---VQFAV--K 828
|
170
....*....|..
gi 6323863 298 DDKFYFLELNPR 309
Cdd:PRK05294 829 DDEVYVIEVNPR 840
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
620-686 |
5.93e-09 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 54.41 E-value: 5.93e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323863 620 TQVISPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKL 686
Cdd:PRK08225 2 TKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVkKINVQEGDFVNEGDVLLEI 69
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
618-686 |
1.06e-08 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 60.24 E-value: 1.06e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 618 NPTQVISPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKL 686
Cdd:PRK09282 521 APGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVkEILVKEGDRVNPGDVLMEI 590
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
624-686 |
1.80e-08 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 53.18 E-value: 1.80e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323863 624 SPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKL 686
Cdd:cd06849 11 SMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLaKILVEEGDTVPVGQVIAVI 74
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
28-336 |
2.41e-08 |
|
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: 58.39 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 28 DLHANSEYIRMADQYVQVPGGTNNNNYANI-DLILDVAEQTDVDAVWAGwghaSENPCLPELLASSQRKILFIGPPGRAM 106
Cdd:COG2232 32 DLFADLDTRALAERWVRLDAESCGFDLEDLpAALLELAAADDPDGLVYG----SGFENFPELLERLARRLPLLGNPPEVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 107 RSLGDKISSTIVAQSAKIPCIPWSgshidtihidnktnFVSVPDDvyvrgccsspedalekakligFPVMIKASEGGGGK 186
Cdd:COG2232 108 RRVKDPLRFFALLDELGIPHPETR--------------FEPPPDP---------------------GPWLVKPIGGAGGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 187 GIRRVDNEDdFIA--LYRQAvnETPGSPMFVMkVVTDARHLEV-----QLLAD------QYGTNITlfgrdcsiqrrhqk 253
Cdd:COG2232 153 HIRPADSEA-PPApgRYFQR--YVEGTPASVL-FLADGSDARVlgfnrQLIGPagerpfRYGGNIG-------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 254 iieeaPVTITKPETfQRMERAA---IRLGELVGYVSAGTVEylyspKDDKFYFLELNPRLQVEHPTTEMISGVNLPATQL 330
Cdd:COG2232 215 -----PLALPPALA-EEMRAIAealVAALGLVGLNGVDFIL-----DGDGPYVLEVNPRPQASLDLYEDATGGNLFDAHL 283
|
....*.
gi 6323863 331 QIAMGI 336
Cdd:COG2232 284 RACRGE 289
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
148-310 |
7.87e-08 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 58.06 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 148 VPDDVYVRgccsSPEDALEKAKLIGFPVMIKASEGGGGKGIRRVDNEDDFIALYRQAVNETPGSPMFVMKVVTDARHLEV 227
Cdd:PRK12815 143 VPESEIVT----SVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 228 QLLADQYGTNITLfgrdCSIQRrhqkiIEeaPVTI-------TKP------ETFQRMERAAIRLGELVGYVSAGTVEYLY 294
Cdd:PRK12815 219 EVMRDRNGNCITV----CNMEN-----ID--PVGIhtgdsivVAPsqtltdDEYQMLRSASLKIISALGVVGGCNIQFAL 287
|
170
....*....|....*.
gi 6323863 295 SPKDDKFYFLELNPRL 310
Cdd:PRK12815 288 DPKSKQYYLIEVNPRV 303
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
615-686 |
2.95e-07 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 52.17 E-value: 2.95e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323863 615 AELNPTQVISPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVIE-LLRQPGSIIEAGDVIAKL 686
Cdd:PRK05641 80 ASAGENVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKkILVKEGDTVDTGQPLIEL 152
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
93-308 |
3.23e-07 |
|
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: 54.18 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 93 QRKILFIGPPgRAMRSLGDKISSTIVAQSAKIPcIPwsgshidtihidnKTNFVSvpddvyvrgccsSPEDALEKAKLIG 172
Cdd:COG0189 79 AAGVPVVNDP-EAIRRARDKLFTLQLLARAGIP-VP-------------PTLVTR------------DPDDLRAFLEELG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 173 FPVMIKASEGGGGKGIRRVDNEDDFIALYRqAVNETPGSPMFVMKVV-----TDARhlevqlladqygtnITLFGRDC-- 245
Cdd:COG0189 132 GPVVLKPLDGSGGRGVFLVEDEDALESILE-ALTELGSEPVLVQEFIpeedgRDIR--------------VLVVGGEPva 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323863 246 SIQRRHQK-----------IIEEAPVTitkpetfQRMERAAIRLGELVGYVSAGtVEYLYSpkDDKFYFLELNP 308
Cdd:COG0189 197 AIRRIPAEgefrtnlarggRAEPVELT-------DEERELALRAAPALGLDFAG-VDLIED--DDGPLVLEVNV 260
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
614-686 |
5.84e-07 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 50.66 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 614 EAELNPTQVISPTPGKL-------VKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAK 685
Cdd:COG0511 55 AAASGGGAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVvEILVENGQPVEYGQPLFV 134
|
.
gi 6323863 686 L 686
Cdd:COG0511 135 I 135
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
624-686 |
1.33e-06 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 47.75 E-value: 1.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323863 624 SPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKL 686
Cdd:COG0508 13 SMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLlEILVKEGDTVPVGAVIAVI 76
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
16-327 |
2.22e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 51.81 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 16 KIIQFVVMATPD------DLHANSEYIRMADQYVQVPGGTNNNnYanIDLILDVAEQTDVDAVWAGwghaSEnpclPELL 89
Cdd:PRK12767 14 QLVKALKKSLLKgrvigaDISELAPALYFADKFYVVPKVTDPN-Y--IDRLLDICKKEKIDLLIPL----ID----PELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 90 ASSQRKILFigppgramrslgdkisstivaqsAKIPCIPwSGSHIDTIHIDN---------KTNFVSVPDDVyvrgCCSS 160
Cdd:PRK12767 83 LLAQNRDRF-----------------------EEIGVKV-LVSSKEVIEICNdkwltyeflKENGIPTPKSY----LPES 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 161 PEDALE--KAKLIGFPVMIKASEGGGGKGIRRVDNEDDFIALYRQAVNetpgsPMfVMKVVTDarhlevqllaDQYGTNI 238
Cdd:PRK12767 135 LEDFKAalAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPN-----LI-IQEFIEG----------QEYTVDV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 239 TLF--GRDCSI--QRRHQKIIEEAPVTITKPetFQRMERAAIRLGELVGYVSAGTVEYLYspKDDKFYFLELNPRLQVEH 314
Cdd:PRK12767 199 LCDlnGEVISIvpRKRIEVRAGETSKGVTVK--DPELFKLAERLAEALGARGPLNIQCFV--TDGEPYLFEINPRFGGGY 274
|
330
....*....|...
gi 6323863 315 PTTEMiSGVNLPA 327
Cdd:PRK12767 275 PLSYM-AGANEPD 286
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
624-681 |
4.99e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 44.80 E-value: 4.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 6323863 624 SPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDG-VIELLRQPGSIIEAGD 681
Cdd:PRK06549 66 SPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGtVTAIHVTPGQVVNPGD 124
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
158-309 |
9.63e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 47.78 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 158 CSSPEDALEKAKLIGFPVMIKAS--EGGGGKGIrrVDNEDDFIALYRQAVNETPGSPMFVMKVVTDARHLEVQLLADQYG 235
Cdd:PRK05294 149 AHSMEEALEVAEEIGYPVIIRPSftLGGTGGGI--AYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKND 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 236 TNITLfgrdCSIqrrhqkiieE---------------APV-TITkPETFQRMERAAIRLGELVGYVSAGT-VEYLYSPKD 298
Cdd:PRK05294 227 NCIIV----CSI---------EnidpmgvhtgdsitvAPAqTLT-DKEYQMLRDASIAIIREIGVETGGCnVQFALNPKD 292
|
170
....*....|.
gi 6323863 299 DKFYFLELNPR 309
Cdd:PRK05294 293 GRYIVIEMNPR 303
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
622-686 |
1.56e-04 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 41.92 E-value: 1.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323863 622 VISPTPGKLVK-------YLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDG-VIELLRQPGSIIEAGDVIAKL 686
Cdd:PRK07051 6 IVSPLPGTFYRrpspdapPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGrVVEFLVEDGEPVEAGQVLARI 78
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
624-710 |
3.47e-04 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 45.49 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 624 SPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKLT--LDSPSKANESSLY 700
Cdd:TIGR01347 11 SITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLqEILFKEGDTVESGQVLAILEegNDATAAPPAKSGE 90
|
90
....*....|
gi 6323863 701 RGELPVLGPP 710
Cdd:TIGR01347 91 EKEETPAASA 100
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
166-311 |
3.59e-04 |
|
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: 43.14 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 166 EKAKLIGFPVMIKASEGGGGKGIRRVDNEDDFialyrqavnETPGSPMFVMKVVtDARHLEVQLLADQYGTNITLFGRDC 245
Cdd:pfam02655 25 EELLREEKKYVVKPRDGCGGEGVRKVENGRED---------EAFIENVLVQEFI-EGEPLSVSLLSDGEKALPLSVNRQY 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323863 246 SIQRRHQKII--EEAPV-TITKPETFQRMERAAIRLGELVGYVSagtVEYLYspKDDKFYFLELNPRLQ 311
Cdd:pfam02655 95 IDNGGSGFVYagNVTPSrTELKEEIIELAEEVVECLPGLRGYVG---VDLVL--KDNEPYVIEVNPRIT 158
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
162-310 |
5.14e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 45.22 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 162 EDALEKAkliGFPVMIKASEGGGGKGIRRVDNEDDFIALYrqAVNETPGSPMFVMKVVTDARHLEVQLLADQYGTNITlf 241
Cdd:PRK02186 135 LDALDGL---TYPVVVKPRMGSGSVGVRLCASVAEAAAHC--AALRRAGTRAALVQAYVEGDEYSVETLTVARGHQVL-- 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323863 242 grdcSIQRRHQ-------KIIEEAPVTITKPeTFQRMERAAIRLGELVGYvSAGTVEYLYSPKDDKFYFLELNPRL 310
Cdd:PRK02186 208 ----GITRKHLgppphfvEIGHDFPAPLSAP-QRERIVRTVLRALDAVGY-AFGPAHTELRVRGDTVVIIEINPRL 277
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
616-686 |
8.35e-04 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 44.33 E-value: 8.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323863 616 ELNPTQVISPTPGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKL 686
Cdd:PRK14042 522 KIGPGDITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVaEILCQKGDKVTPGQVLIRV 593
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
146-207 |
1.44e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 43.61 E-value: 1.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323863 146 VSVPDDVYVRgccsSPEDALEKAKLIGFPVMIKASEGGGGKGIR-RVDNEDDFIALYRQAVNE 207
Cdd:PRK14016 227 VPVPEGRVVT----SAEDAWEAAEEIGYPVVVKPLDGNHGRGVTvNITTREEIEAAYAVASKE 285
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
628-686 |
3.21e-03 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 42.09 E-value: 3.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 628 GKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI-ELLRQPGSIIEAGDVIAKL 686
Cdd:PRK11856 17 GEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVaKLLVEEGDVVPVGSVIAVI 76
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
634-684 |
3.39e-03 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 38.25 E-value: 3.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 6323863 634 LVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVIELLR-QPGSIIEAGDVIA 684
Cdd:PRK05889 17 VVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSvSVGDVIQAGDLIA 68
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
105-204 |
4.02e-03 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 41.64 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323863 105 AMrslgDKISSTIVAQSAKIPcipwsgshidtihidnktnfvsVPDDVYVrgccSSPEDALEKAKLIGFPVMIKASEGGG 184
Cdd:PRK01372 96 AM----DKLRTKLVWQAAGLP----------------------TPPWIVL----TREEDLLAAIDKLGLPLVVKPAREGS 145
|
90 100
....*....|....*....|
gi 6323863 185 GKGIRRVDNEDDFIALYRQA 204
Cdd:PRK01372 146 SVGVSKVKEEDELQAALELA 165
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
619-667 |
4.53e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 41.83 E-value: 4.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6323863 619 PTQV----ISPT--PGKLVKYLVRSGDHVFAGQQYAEIEIMKMQMPLVAKSDGVI 667
Cdd:PRK11892 2 AIEIlmpaLSPTmeEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTL 56
|
|
| |
