|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
797-1541 |
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: 938.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 797 ELDDPSLVTKAQPFKGQFlqPENAP---VPEKLNRVHNTYKSILENTLAGYClpepfNAQRLRDIIEKFMQSLRDPSLPL 873
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQL--PELGPptvVGNKPHQRFAALLNILENILAGYD-----NQVIMNETLKDLIEVLRDPELPY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 874 LELQEVIASISGRIPISVEKKIRKLMTLYERNitsvLAQFPSQQIASVIDSHAATLQKRADRDVFFLTTQSIVQLVQRYR 953
Cdd:pfam08326 74 LEWQEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 954 NGIRGRMKAAVHELLRQYYDVESQFQYG--HYDKCVGLVREHNKDDMQTVVNTIFSHSQVAKKNLLVTLLIDHLW---AN 1028
Cdd:pfam08326 150 NGLKGHEYSVFASLLEEYYDVEKLFSGGnvREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRpncPN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1029 EPGLTDELANTLSELTSLNRAEHSRVALRSRQVLIAAHQPAYELRHNQMESIFLSAVDMYGH--------DFHPENLQRL 1100
Cdd:pfam08326 230 VSNVAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1101 ILSETSIFDILHDFFYHSNRAVCNAALEVYVRRAYTSYELTCLQHLELSGGLPLVHFQFLLPTAHPN------------- 1167
Cdd:pfam08326 310 IDSKYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSefgsplspssdss 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1168 RLFSRMSSPDGLDQAAAESLgNSFVRTGAIAAFDSFEHFEMYSDEILDLLedfvspamvnakvleaveaadsisdsrhst 1247
Cdd:pfam08326 390 PPFKRIASVSDLSYLVNKSE-DEPLRTGAMVAFKSLDDLEEALPRALEEF------------------------------ 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1248 sinvslsdPVTRANAAEEAKSTEPIHIVSVAVRETGELD-DLQMAQIFGNYCQEHNEELFQRRIRRITFAALKK-RQFPK 1325
Cdd:pfam08326 439 --------PSEPEESGESNSSDEPINVLNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKdGQYPK 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1326 FFTFRARDKFTEDRIYRHLEPASAFHLELNRMKTYDLEALPTANQKMHLYLGKAKVSKgqevTDYRFFIRSIIRHSDLIT 1405
Cdd:pfam08326 511 YFTFRGPDNYEEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRD 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1406 KEASFEYLQNEGERVLLEAMDELEVAfsHPHAKRTDCNHIFLNFVPTVIMDPAKIEESVTKMIMRYGPRLWKLRVLQAEL 1485
Cdd:pfam08326 587 DIPTAEYLISEAERLLNDILDALEVA--SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEI 664
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 665399403 1486 KMVIRQSPQSPTQAVRLCIANDSGYFLDISMYTEQTEPEtGIIKFKAYGeKQGSLH 1541
Cdd:pfam08326 665 RIIIRDPETGPPIPLRLVITNVSGYVVKVELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1641-2183 |
1.58e-161 |
|
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: 507.57 E-value: 1.58e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1641 PEYPNGREIIVIANDLTYLIGSFGIKEDVLFAKASQLARQlKVPRIYISVNSGARIGLAEEVKAMFKIAWEDPEEPDKGF 1720
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRK-RIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1721 KYLYLSTEdyaqvanlnsvrAIlieDEGEQRYKITDIIGKDDGLGVENLRYAGLIAGETSQAYEEIVTIAMVTCRTIGIG 1800
Cdd:pfam01039 80 KILRAMEI------------AI---KTGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1801 SYVVRLGQRVIQIDN-SHIILTGYAALNKLLGRkVYASNNQLGGTQIMFNNGVTHKTEAIDLDGVYTILDWLSYIPAYIG 1879
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTGE-EVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1880 ---CDLPIVLPNDRIERP---VDFMPT--KSPYDPRWMLGGRVnpvnandwengffDRDSWSEIMASWAKTVVTGRARLG 1951
Cdd:pfam01039 224 nnrEPVPIVPTKDPPDRDaplVSIVPDdpKKPYDVREVIAGIV-------------DEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1952 GVPVGVIAVETRtvevempadpanldseaktlQQAGqVWYPDSSYKTAQAIKDFGREELPLIVFANWRGFSGGMKDMYEQ 2031
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 2032 IVKFGAYIVDGLREYKKPVLIYLPPnaELRGGAWAVLDSLINPRYMeTYADPEARGGVLEPEGIVEIKYKEKDLVKTIHR 2111
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665399403 2112 LDPttialkkeldeanasgdkvrAAQVDEKIKARIAVLMHVYHTVAVHFADLHDTPERMLEKECISEIVPWR 2183
Cdd:pfam01039 427 KDL--------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWT 478
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
101-605 |
8.86e-126 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 405.17 E-value: 8.86e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 101 INKVLIANNGIAAVKCMRSIRrwayEMfknerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGSNNNNYANVELIVDIA 180
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 181 LRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPWSgsdlkaqysgkkikis 260
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 261 selfaRGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEVP---GSP-IFVMKLARGARHL 336
Cdd:COG4770 135 -----DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIERPRHI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 337 EVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPEGRYFFLEL 416
Cdd:COG4770 210 EVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 417 NPRLQVEHPCTEMVADVNLPAAQLQIGMGIPL-YRLKDIrllygespwgssvidfenppnkpRPSGHVIAARITSENPDE 495
Cdd:COG4770 290 NTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLpFTQEDI-----------------------KLRGHAIECRINAEDPAR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 496 GFKPSSGTVQELNFRSSknvwgyFSVAASGGLHE------FADSQFGHCFSWGENRQQARENLVIALKELSIRGdFRTTV 569
Cdd:COG4770 347 GFLPSPGTITRLRPPGG------PGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG-VKTNI 419
|
490 500 510
....*....|....*....|....*....|....*.
gi 665399403 570 EYLITLLETNRFLDNSIDTAWLDALIAERVQSEKPD 605
Cdd:COG4770 420 PFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
101-601 |
1.08e-104 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 343.71 E-value: 1.08e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 101 INKVLIANNGIAAVKCMRSIRrwayemfknERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGSNNNNYANVELIVDIA 180
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 181 LRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPwsGSDlkaqysgkkikis 260
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GSD------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 261 selfarGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEVP---GSPIFVM-KLARGARHL 336
Cdd:PRK08591 136 ------GPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPGVYMeKYLENPRHI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 337 EVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPEGRYFFLEL 416
Cdd:PRK08591 210 EIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 417 NPRLQVEHPCTEMVADVNLPAAQLQIGMGIPL-YRLKDIRLlygespwgssvidfenppnkprpSGHVIAARITSENPDE 495
Cdd:PRK08591 290 NTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLsIKQEDIVF-----------------------RGHAIECRINAEDPAK 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 496 GFKPSSGTVQelnfrssknvwGYFsvaASGGLH--------------EFADSQFGHCFSWGENRQQARENLVIALKELSI 561
Cdd:PRK08591 347 NFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRALSEFVI 412
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 665399403 562 RGdFRTTVEYLITLLETNRFLDNSIDTAWLDALIAERVQS 601
Cdd:PRK08591 413 DG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
103-592 |
1.13e-87 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 313.69 E-value: 1.13e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 103 KVLIANNGIAAVKCMRSIrrwayemfkNERAIRFVVMVTPED------LKANAEY-IKMADHYVPVpggsnnNNYANVEL 175
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 176 IVDIALRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPwsGSDlkaqysgk 255
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVP--GTD-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 256 kikisselfarGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRV----DTTEEFPGLFRQVQAEVPGSPIFVMKLAR 331
Cdd:TIGR01235 136 -----------GPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVrseaDVADAFQRAKSEAKAAFGNDEVYVEKLIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 332 GARHLEVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPEGRY 411
Cdd:TIGR01235 205 RPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 412 FFLELNPRLQVEHPCTEMVADVNLPAAQLQI--GMGIPLYRL-----KDIRLlygespwgssvidfenppnkprpSGHVI 484
Cdd:TIGR01235 285 YFIEVNPRIQVEHTVTEEITGIDIVQAQIHIadGASLPTPQLgvpnqEDIRT-----------------------NGYAI 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 485 AARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSVAASGG-------LHEFADSQFGHCFSWGENRQQARENLVIALK 557
Cdd:TIGR01235 342 QCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAKMDRALR 415
|
490 500 510
....*....|....*....|....*....|....*
gi 665399403 558 ELSIRGdFRTTVEYLITLLETNRFLDNSIDTAWLD 592
Cdd:TIGR01235 416 EFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
225-448 |
1.30e-60 |
|
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: 207.16 E-value: 1.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 225 DKVASSIVAQTAEIPTLPwsGSDlkaqysgkkikisselfarGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDT 304
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVP--GTA-------------------GPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARN 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 305 TEEFPGLFRQVQAEVPGSP----IFVMKLARGARHLEVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFE 380
Cdd:pfam02786 60 EEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665399403 381 DMEKAAVRLAKMVGYVSAGTVEYLYDPE-GRYFFLELNPRLQVEHPCTEMVADVNLPAAQLQIGMGIPL 448
Cdd:pfam02786 140 MLREAAVKIARHLGYVGAGTVEFALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
486-592 |
8.00e-29 |
|
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: 112.12 E-value: 8.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 486 ARITSENPDEGFKPSSGTVQELNFRSSKNVwgYFSVAASGGLHE--FADSQFGHCFSWGENRQQARENLVIALKELSIRG 563
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 665399403 564 dFRTTVEYLITLLETNRFLDNSIDTAWLD 592
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
732-793 |
5.40e-16 |
|
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: 74.37 E-value: 5.40e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665399403 732 LRSPSAGKLINMIVEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVTFVR-RPGAVLDAGSLL 793
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLL 64
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
732-793 |
4.71e-14 |
|
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: 68.78 E-value: 4.71e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665399403 732 LRSPSAGKLI-----NMIVEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVTFVRRP-GAVLDAGSLL 793
Cdd:pfam00364 3 IKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPL 70
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1645-2147 |
6.95e-12 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 70.44 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1645 NGREIIVIANDLTYLIGSFG----IKedvlFAKASQLARQLKVPRIYIsVNS-GARIGLAEEVKAMF-KIawedpeepdk 1718
Cdd:COG4799 80 DGRPVVVVANDFTVKGGSLGpmtaKK----ILRAQDIALENGLPVIYL-VDSgGARLQEGVESFAGYgRI---------- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1719 gFkylylstedYAQVanlnsvrailiedegeqrykitdiigkddglgvenlRYAGLIAgetsQayeeiVTIAMVTCrtIG 1798
Cdd:COG4799 145 -F---------YRNA------------------------------------RSSGGIP----Q-----ISVIMGPC--AA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1799 IGSYVVRLGQRVIQID-NSHIILTGyAALNKL-LGRKVyaSNNQLGGTQI-MFNNGVTHKTEAIDLDGVYTILDWLSYIP 1875
Cdd:COG4799 168 GGAYSPALSDFVIMVKgTSQMFLGG-PPVVKAaTGEEV--TAEELGGADVhARVSGVADYLAEDEEEALALARRLLSYLP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1876 AYIGCDLPIV---LPNDRIERPVDFMPT--KSPYDPRWMLGgRVnpvnandwengfFDRDSWSEIMASWAKTVVTGRARL 1950
Cdd:COG4799 245 SNNLEDPPRAepaPPARDPEELYGIVPEdpRKPYDMREVIA-RL------------VDGGSFFEFKPLYGPNIVTGFARI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1951 GGVPVGVIAvetrtvevempADPANLdseaktlqqAGqVWYPDSSYKTAQAIKDFGREELPLIVFANWRGFsggmkdM-- 2028
Cdd:COG4799 312 DGRPVGIVA-----------NQPMVL---------AG-VLDIDAADKAARFIRLCDAFNIPLVFLVDVPGF------Mvg 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 2029 --YEQ--IVKFGAyivdglreyKkpvLIYLPPNAE-------LR---GGAWAVLDSL-INPRYMetYADPEARGGVLEPE 2093
Cdd:COG4799 365 teQERggIIRHGA---------K---LLYAVAEATvpkitviLRkayGAGYYAMCGKaLGPDFL--FAWPTAEIAVMGGE 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 665399403 2094 GIVEIkykekdlvktIHRldpttialkKELDEAnASGDKVRA---AQVDEKIKARIA 2147
Cdd:COG4799 431 GAANV----------LYR---------RELAAA-EDPEALRAeliAEYEEQANPYYA 467
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
727-793 |
5.29e-07 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 55.14 E-value: 5.29e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665399403 727 NDPSLLRSPSAGKLINMIVEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVTFV-RRPGAVLDAGSLL 793
Cdd:PRK12999 1074 GNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVlVKAGDQVEAGDLL 1141
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
727-793 |
2.06e-05 |
|
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: 50.08 E-value: 2.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665399403 727 NDPSLLRSPSAGKLINMIVEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVTFVR-RPGAVLDAGSLL 793
Cdd:COG1038 1074 GNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLvKEGDQVEAGDLL 1141
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
797-1541 |
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: 938.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 797 ELDDPSLVTKAQPFKGQFlqPENAP---VPEKLNRVHNTYKSILENTLAGYClpepfNAQRLRDIIEKFMQSLRDPSLPL 873
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQL--PELGPptvVGNKPHQRFAALLNILENILAGYD-----NQVIMNETLKDLIEVLRDPELPY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 874 LELQEVIASISGRIPISVEKKIRKLMTLYERNitsvLAQFPSQQIASVIDSHAATLQKRADRDVFFLTTQSIVQLVQRYR 953
Cdd:pfam08326 74 LEWQEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 954 NGIRGRMKAAVHELLRQYYDVESQFQYG--HYDKCVGLVREHNKDDMQTVVNTIFSHSQVAKKNLLVTLLIDHLW---AN 1028
Cdd:pfam08326 150 NGLKGHEYSVFASLLEEYYDVEKLFSGGnvREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRpncPN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1029 EPGLTDELANTLSELTSLNRAEHSRVALRSRQVLIAAHQPAYELRHNQMESIFLSAVDMYGH--------DFHPENLQRL 1100
Cdd:pfam08326 230 VSNVAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1101 ILSETSIFDILHDFFYHSNRAVCNAALEVYVRRAYTSYELTCLQHLELSGGLPLVHFQFLLPTAHPN------------- 1167
Cdd:pfam08326 310 IDSKYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSefgsplspssdss 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1168 RLFSRMSSPDGLDQAAAESLgNSFVRTGAIAAFDSFEHFEMYSDEILDLLedfvspamvnakvleaveaadsisdsrhst 1247
Cdd:pfam08326 390 PPFKRIASVSDLSYLVNKSE-DEPLRTGAMVAFKSLDDLEEALPRALEEF------------------------------ 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1248 sinvslsdPVTRANAAEEAKSTEPIHIVSVAVRETGELD-DLQMAQIFGNYCQEHNEELFQRRIRRITFAALKK-RQFPK 1325
Cdd:pfam08326 439 --------PSEPEESGESNSSDEPINVLNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKdGQYPK 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1326 FFTFRARDKFTEDRIYRHLEPASAFHLELNRMKTYDLEALPTANQKMHLYLGKAKVSKgqevTDYRFFIRSIIRHSDLIT 1405
Cdd:pfam08326 511 YFTFRGPDNYEEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRD 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1406 KEASFEYLQNEGERVLLEAMDELEVAfsHPHAKRTDCNHIFLNFVPTVIMDPAKIEESVTKMIMRYGPRLWKLRVLQAEL 1485
Cdd:pfam08326 587 DIPTAEYLISEAERLLNDILDALEVA--SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEI 664
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 665399403 1486 KMVIRQSPQSPTQAVRLCIANDSGYFLDISMYTEQTEPEtGIIKFKAYGeKQGSLH 1541
Cdd:pfam08326 665 RIIIRDPETGPPIPLRLVITNVSGYVVKVELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1641-2183 |
1.58e-161 |
|
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: 507.57 E-value: 1.58e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1641 PEYPNGREIIVIANDLTYLIGSFGIKEDVLFAKASQLARQlKVPRIYISVNSGARIGLAEEVKAMFKIAWEDPEEPDKGF 1720
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRK-RIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1721 KYLYLSTEdyaqvanlnsvrAIlieDEGEQRYKITDIIGKDDGLGVENLRYAGLIAGETSQAYEEIVTIAMVTCRTIGIG 1800
Cdd:pfam01039 80 KILRAMEI------------AI---KTGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1801 SYVVRLGQRVIQIDN-SHIILTGYAALNKLLGRkVYASNNQLGGTQIMFNNGVTHKTEAIDLDGVYTILDWLSYIPAYIG 1879
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTGE-EVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1880 ---CDLPIVLPNDRIERP---VDFMPT--KSPYDPRWMLGGRVnpvnandwengffDRDSWSEIMASWAKTVVTGRARLG 1951
Cdd:pfam01039 224 nnrEPVPIVPTKDPPDRDaplVSIVPDdpKKPYDVREVIAGIV-------------DEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1952 GVPVGVIAVETRtvevempadpanldseaktlQQAGqVWYPDSSYKTAQAIKDFGREELPLIVFANWRGFSGGMKDMYEQ 2031
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 2032 IVKFGAYIVDGLREYKKPVLIYLPPnaELRGGAWAVLDSLINPRYMeTYADPEARGGVLEPEGIVEIKYKEKDLVKTIHR 2111
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665399403 2112 LDPttialkkeldeanasgdkvrAAQVDEKIKARIAVLMHVYHTVAVHFADLHDTPERMLEKECISEIVPWR 2183
Cdd:pfam01039 427 KDL--------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWT 478
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
101-605 |
8.86e-126 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 405.17 E-value: 8.86e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 101 INKVLIANNGIAAVKCMRSIRrwayEMfknerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGSNNNNYANVELIVDIA 180
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 181 LRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPWSgsdlkaqysgkkikis 260
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 261 selfaRGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEVP---GSP-IFVMKLARGARHL 336
Cdd:COG4770 135 -----DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIERPRHI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 337 EVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPEGRYFFLEL 416
Cdd:COG4770 210 EVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 417 NPRLQVEHPCTEMVADVNLPAAQLQIGMGIPL-YRLKDIrllygespwgssvidfenppnkpRPSGHVIAARITSENPDE 495
Cdd:COG4770 290 NTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLpFTQEDI-----------------------KLRGHAIECRINAEDPAR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 496 GFKPSSGTVQELNFRSSknvwgyFSVAASGGLHE------FADSQFGHCFSWGENRQQARENLVIALKELSIRGdFRTTV 569
Cdd:COG4770 347 GFLPSPGTITRLRPPGG------PGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG-VKTNI 419
|
490 500 510
....*....|....*....|....*....|....*.
gi 665399403 570 EYLITLLETNRFLDNSIDTAWLDALIAERVQSEKPD 605
Cdd:COG4770 420 PFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
101-601 |
1.08e-104 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 343.71 E-value: 1.08e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 101 INKVLIANNGIAAVKCMRSIRrwayemfknERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGSNNNNYANVELIVDIA 180
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 181 LRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPwsGSDlkaqysgkkikis 260
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GSD------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 261 selfarGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEVP---GSPIFVM-KLARGARHL 336
Cdd:PRK08591 136 ------GPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPGVYMeKYLENPRHI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 337 EVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPEGRYFFLEL 416
Cdd:PRK08591 210 EIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 417 NPRLQVEHPCTEMVADVNLPAAQLQIGMGIPL-YRLKDIRLlygespwgssvidfenppnkprpSGHVIAARITSENPDE 495
Cdd:PRK08591 290 NTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLsIKQEDIVF-----------------------RGHAIECRINAEDPAK 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 496 GFKPSSGTVQelnfrssknvwGYFsvaASGGLH--------------EFADSQFGHCFSWGENRQQARENLVIALKELSI 561
Cdd:PRK08591 347 NFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRALSEFVI 412
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 665399403 562 RGdFRTTVEYLITLLETNRFLDNSIDTAWLDALIAERVQS 601
Cdd:PRK08591 413 DG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
99-592 |
1.70e-99 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 349.44 E-value: 1.70e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 99 RVINKVLIANNGIAAVKCMRSIrrwayemfkNERAIRFVVMVTPED------LKANAEY-IKMADHyvPVPGgsnnnnYA 171
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAA---------TELGIRTVAIYSEEDklslhrFKADEAYlIGEGKH--PVRA------YL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 172 NVELIVDIALRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPwsGSDlkaq 251
Cdd:PRK12999 66 DIDEIIRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIP--GSE---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 252 ysgkkikisselfarGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEVP---GSP-IFVM 327
Cdd:PRK12999 140 ---------------GPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafGNDeVYLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 328 KLARGARHLEVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDP 407
Cdd:PRK12999 205 KYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 408 EGRYFFLELNPRLQVEHPCTEMVADVNLPAAQLQIGMGiplYRLKDIrllygespwGSSVIDFENppnkPRPSGHVIAAR 487
Cdd:PRK12999 285 DGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG---ATLHDL---------EIGIPSQED----IRLRGYAIQCR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 488 ITSENPDEGFKPSSGTVQElnFRSSknvwGYFSVAASGGLHeFADSQFGHCF--------SWGENRQQARENLVIALKEL 559
Cdd:PRK12999 349 ITTEDPANNFMPDTGRITA--YRSP----GGFGVRLDGGNA-FAGAEITPYYdsllvkltAWGRTFEQAVARMRRALREF 421
|
490 500 510
....*....|....*....|....*....|...
gi 665399403 560 SIRGdFRTTVEYLITLLETNRFLDNSIDTAWLD 592
Cdd:PRK12999 422 RIRG-VKTNIPFLENVLKHPDFRAGDYTTSFID 453
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
101-591 |
3.77e-96 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 319.28 E-value: 3.77e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 101 INKVLIANNGIAAVKCMRSIRRWAyemfkneraIRFVVMVTPEDlkANAEYIKMADHYVPVPGGSNNNNYANVELIVDIA 180
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLG---------IRTVAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 181 LRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPWSGSDLkaqysgkkikis 260
Cdd:PRK06111 71 KKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNL------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 261 selfargcvTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEVP---GSP-IFVMKLARGARHL 336
Cdd:PRK06111 139 ---------EDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAAnffGNGeMYIEKYIEDPRHI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 337 EVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPEGRYFFLEL 416
Cdd:PRK06111 210 EIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 417 NPRLQVEHPCTEMVADVNLPAAQLQIGMGIPL-YRLKDIRLlygespwgssvidfenppnkprpSGHVIAARITSENPDE 495
Cdd:PRK06111 290 NTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR-----------------------SGHAIEVRIYAEDPKT 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 496 gFKPSSGTVQELNFRSSKNVWGYFSVAASGGLHEFADSQFGHCFSWGENRQQARENLVIALKELSIRGdFRTTVEYLITL 575
Cdd:PRK06111 347 -FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEG-IKTNIPLLLQV 424
|
490
....*....|....*.
gi 665399403 576 LETNRFLDNSIDTAWL 591
Cdd:PRK06111 425 LEDPVFKAGGYTTGFL 440
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
98-592 |
9.05e-95 |
|
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: 335.13 E-value: 9.05e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 98 TRVINKVLIANNG-IAavkcmrsIR--RWAYEMfknerAIRFVVMVTPED------LKANAEY-IKMADHyvPVpggsnn 167
Cdd:COG1038 1 MKKIKKVLVANRGeIA-------IRvfRAATEL-----GIRTVAIYSEEDryslhrFKADEAYlIGEGKG--PV------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 168 NNYANVELIVDIALRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPwsGSD 247
Cdd:COG1038 61 DAYLDIEEIIRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP--GTE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 248 lkaqysgkkikisselfarGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEVP---GSP- 323
Cdd:COG1038 139 -------------------GPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafGDDe 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 324 IFVMKLARGARHLEVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEY 403
Cdd:COG1038 200 VFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEF 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 404 LYDPEGRYFFLELNPRLQVEHPCTEMVADVNLPAAQLQIGMGiplYRL--KDIRLlygesPWGSSVidfenppnkpRPSG 481
Cdd:COG1038 280 LVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG---YSLddPEIGI-----PSQEDI----------RLNG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 482 HVIAARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSV---AASGglheFA--------DSQFGHCFSWGENRQQARE 550
Cdd:COG1038 342 YAIQCRITTEDPANNFMPDTGRITA--YRSA----GGFGIrldGGNA----YTgavitpyyDSLLVKVTAWGRTFEEAIR 411
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 665399403 551 NLVIALKELSIRGdFRTTVEYLITLLETNRFLDNSIDTAWLD 592
Cdd:COG1038 412 KMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFID 452
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
102-592 |
4.59e-93 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 311.92 E-value: 4.59e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 102 NKVLIANNGIAAVKCMRSIRrwayemfknERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGSNNNNYANVELIVDIAL 181
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACR---------ELGIKTVAVYSEAD--KNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 182 RTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPWSGsdlkaqysgkkikiss 261
Cdd:PRK08654 72 KAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTE---------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 262 elfarGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLF---RQVQAEVPGSP-IFVMKLARGARHLE 337
Cdd:PRK08654 136 -----EGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIestQSIAQSAFGDStVFIEKYLEKPRHIE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 338 VQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDpEGRYFFLELN 417
Cdd:PRK08654 211 IQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFYFLEMN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 418 PRLQVEHPCTEMVADVNLPAAQLQIGMGIPL-YRLKDIRLlygespwgssvidfenppnkprpSGHVIAARITSENPDEG 496
Cdd:PRK08654 290 TRLQVEHPITEMVTGIDIVKEQIKIAAGEELsFKQEDITI-----------------------RGHAIECRINAEDPLND 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 497 FKPSSGTVQelNFRSSknvwGYFSVAASGGLH------EFADSQFGHCFSWGENRQQARENLVIALKELSIRGdFRTTVE 570
Cdd:PRK08654 347 FAPSPGKIK--RYRSP----GGPGVRVDSGVHmgyeipPYYDSMISKLIVWGRTREEAIARMRRALYEYVIVG-VKTNIP 419
|
490 500
....*....|....*....|..
gi 665399403 571 YLITLLETNRFLDNSIDTAWLD 592
Cdd:PRK08654 420 FHKAVMENENFVRGNLHTHFIE 441
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
101-598 |
3.71e-88 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 296.67 E-value: 3.71e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 101 INKVLIANNGIAAVKCMRSIRrwayemfknERAIRFVVMVTPEDLKANAeyIKMADHYVPVPGGSNNNNYANVELIVDIA 180
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAAR---------ELGMRTVAACSDADRDSLA--ARMADEAVHIGPSHAAKSYLNPAAILAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 181 LRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPwsGSDlkaqysgkkikis 260
Cdd:PRK12833 74 RQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVP--GSD------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 261 selfarGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRV----DTTEEFPGLFRQVQAEVPGSPIFVMKLARGARHL 336
Cdd:PRK12833 139 ------GVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAhdaaQLAAELPLAQREAQAAFGDGGVYLERFIARARHI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 337 EVQLLADQYgNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPE-GRYFFLE 415
Cdd:PRK12833 213 EVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDArGEFYFIE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 416 LNPRLQVEHPCTEMVADVNLPAAQLQIGMGIPL-YRLKDIRLlygespwgssvidfenppnkprpSGHVIAARITSENPD 494
Cdd:PRK12833 292 MNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLrFAQGDIAL-----------------------RGAALECRINAEDPL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 495 EGFKPSSGTVQELNF------RSSKNVWGYFSVAAsgglheFADSQFGHCFSWGENRQQARENLVIALKELSIRGdFRTT 568
Cdd:PRK12833 349 RDFFPNPGRIDALVWpqgpgvRVDSLLYPGYRVPP------FYDSLLAKLIVHGEDRAAALARAARALRELRIDG-MKTT 421
|
490 500 510
....*....|....*....|....*....|
gi 665399403 569 VEYLITLLETNRFLDNSIDTAWLDALIAER 598
Cdd:PRK12833 422 APLHRALLADADVRAGRFHTNFLEAWLAEW 451
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
103-592 |
1.13e-87 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 313.69 E-value: 1.13e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 103 KVLIANNGIAAVKCMRSIrrwayemfkNERAIRFVVMVTPED------LKANAEY-IKMADHYVPVpggsnnNNYANVEL 175
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 176 IVDIALRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPwsGSDlkaqysgk 255
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVP--GTD-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 256 kikisselfarGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRV----DTTEEFPGLFRQVQAEVPGSPIFVMKLAR 331
Cdd:TIGR01235 136 -----------GPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVrseaDVADAFQRAKSEAKAAFGNDEVYVEKLIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 332 GARHLEVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPEGRY 411
Cdd:TIGR01235 205 RPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 412 FFLELNPRLQVEHPCTEMVADVNLPAAQLQI--GMGIPLYRL-----KDIRLlygespwgssvidfenppnkprpSGHVI 484
Cdd:TIGR01235 285 YFIEVNPRIQVEHTVTEEITGIDIVQAQIHIadGASLPTPQLgvpnqEDIRT-----------------------NGYAI 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 485 AARITSENPDEGFKPSSGTVQElnFRSSknvwGYFSVAASGG-------LHEFADSQFGHCFSWGENRQQARENLVIALK 557
Cdd:TIGR01235 342 QCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAKMDRALR 415
|
490 500 510
....*....|....*....|....*....|....*
gi 665399403 558 ELSIRGdFRTTVEYLITLLETNRFLDNSIDTAWLD 592
Cdd:TIGR01235 416 EFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
101-591 |
1.22e-87 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 294.31 E-value: 1.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 101 INKVLIANNGIAAVKCMRSIRrwayemfknERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGSNNNNYANVELIVDIA 180
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACR---------EMGIETVAVYSEAD--KDALHVQLADEAVCIGPASSKDSYLNIQNIISAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 181 LRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPwsGSDlkaqysgkkikis 260
Cdd:PRK05586 71 VLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVP--GSE------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 261 selfarGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEVPGS----PIFVMKLARGARHL 336
Cdd:PRK05586 136 ------GEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFIENPKHI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 337 EVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPEGRYFFLEL 416
Cdd:PRK05586 210 EFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 417 NPRLQVEHPCTEMVADVNLPAAQLQIGMGIPL-YRLKDIRLlygespwgssvidfenppnkprpSGHVIAARITSENPDE 495
Cdd:PRK05586 290 NTRIQVEHPITEMITGVDLVKEQIKIAYGEKLsIKQEDIKI-----------------------NGHSIECRINAEDPKN 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 496 GFKPSSGTVQELNFRSSKNVWGYFSVAASGGLHEFADSQFGHCFSWGENRQQARENLVIALKELSIRGdFRTTVEYLITL 575
Cdd:PRK05586 347 GFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEG-VNTNIDFQFII 425
|
490
....*....|....*.
gi 665399403 576 LETNRFLDNSIDTAWL 591
Cdd:PRK05586 426 LEDEEFIKGTYDTSFI 441
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
101-592 |
1.31e-85 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 288.57 E-value: 1.31e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 101 INKVLIANNGIAAVKCMRSIRrwayEMFKNErairfVVMVTPEDLKANaeYIKMADHYVPVPGGSNNNNYANVELIVDIA 180
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQ----EMGKEA-----IAIYSTADKDAL--YLKYADAKICIGGAKSSESYLNIPAIISAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 181 LRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPwsGSDlkaqysgkkikis 260
Cdd:PRK08462 73 EIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIP--GSD------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 261 selfarGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEVPGS----PIFVMKLARGARHL 336
Cdd:PRK08462 138 ------GALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAfgdgTMYMEKFINNPRHI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 337 EVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPEGRYFFLEL 416
Cdd:PRK08462 212 EVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEM 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 417 NPRLQVEHPCTEMVADVNLPAAQLQIGMGIPLYRLKDIRLlygespwgssvidfenppnkprpSGHVIAARITSENPdEG 496
Cdd:PRK08462 292 NTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKL-----------------------KGHAIECRITAEDP-KK 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 497 FKPSSGTVQEL------NFRSSKNVWGYFSVAAsgglheFADSQFGHCFSWGENRQQARENLVIALKELSIRGdFRTTVE 570
Cdd:PRK08462 348 FYPSPGKITKWiapggrNVRMDSHAYAGYVVPP------YYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEG-IKTTIP 420
|
490 500
....*....|....*....|..
gi 665399403 571 YLITLLETNRFLDNSIDTAWLD 592
Cdd:PRK08462 421 FHLEMMENADFINNKYDTKYLE 442
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
100-502 |
1.53e-79 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 271.98 E-value: 1.53e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 100 VINKVLIANNGIAAVKCMRSIRrwayemfknERAIRFVVMVTPEDlkANAEYIKMADHYV-----PVPGgsnnnnYANVE 174
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACA---------EMGIRSVAIYSEAD--RHALHVKRADEAYsigadPLAG------YLNPR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 175 LIVDIALRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPwsGSDlkaqysg 254
Cdd:PRK07178 64 RLVNLAVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTP--GSE------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 255 kkikisselfarGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEVP---GSP-IFVMKLA 330
Cdd:PRK07178 135 ------------GNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafGSAeVFLEKCI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 331 RGARHLEVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPEGR 410
Cdd:PRK07178 203 VNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 411 YFFLELNPRLQVEHPCTEMVADVNLPAAQLQIGMGIPL-YRLKDIRLlygespwgssvidfenppnkprpSGHVIAARIT 489
Cdd:PRK07178 283 VYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH-----------------------RGFALQFRIN 339
|
410
....*....|...
gi 665399403 490 SENPDEGFKPSSG 502
Cdd:PRK07178 340 AEDPKNDFLPSFG 352
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
101-597 |
9.04e-69 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 240.87 E-value: 9.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 101 INKVLIANNGIAAVKCMRSIRrwayemfknERAIRFVVMVTPEDlkANAEYIKMADHYVPVpGGSNNNNYANVELIVDIA 180
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACR---------DLHIKSVAIYTEPD--RECLHVKIADEAYRI-GTDPIKGYLDVKRIVEIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 181 LRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERAMWALGDKVASSIVAQTAEIPTLPwsGSDLKAQYSGKKIKIs 260
Cdd:PRK08463 70 KACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVP--GTEKLNSESMEEIKI- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 261 selFARgcvtnveqglaavnKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLF----RQVQAEVPGSPIFVMKLARGARHL 336
Cdd:PRK08463 147 ---FAR--------------KIGYPVILKASGGGGGRGIRVVHKEEDLENAFesckREALAYFNNDEVFMEKYVVNPRHI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 337 EVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAivaqPEVFEDMEK----AAVRLAKMVGYVSAGTVEYLYDPEGRYF 412
Cdd:PRK08463 210 EFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPC----PSISDNLRKtmgvTAVAAAKAVGYTNAGTIEFLLDDYNRFY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 413 FLELNPRLQVEHPCTEMVADVNLPAAQLQIGMGiplyrlkdirllygespwgsSVIDFENppNKPRPSGHVIAARITSEN 492
Cdd:PRK08463 286 FMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG--------------------EILDLEQ--SDIKPRGFAIEARITAEN 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 493 PDEGFKPSSGTVQEL------NFRSSKNVWGYFSVAAsgglheFADSQFGHCFSWGENRQQARENLVIALKELSIRGdFR 566
Cdd:PRK08463 344 VWKNFIPSPGKITEYypalgpSVRVDSHIYKDYTIPP------YYDSMLAKLIVKATSYDLAVNKLERALKEFVIDG-IR 416
|
490 500 510
....*....|....*....|....*....|.
gi 665399403 567 TTVEYLITLLETNRFLDNSIDTAWLDALIAE 597
Cdd:PRK08463 417 TTIPFLIAITKTREFRRGYFDTSYIETHMQE 447
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
225-448 |
1.30e-60 |
|
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: 207.16 E-value: 1.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 225 DKVASSIVAQTAEIPTLPwsGSDlkaqysgkkikisselfarGCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDT 304
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVP--GTA-------------------GPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARN 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 305 TEEFPGLFRQVQAEVPGSP----IFVMKLARGARHLEVQLLADQYGNAISLFGRDCSIQRRHQKIIEEAPAIVAQPEVFE 380
Cdd:pfam02786 60 EEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665399403 381 DMEKAAVRLAKMVGYVSAGTVEYLYDPE-GRYFFLELNPRLQVEHPCTEMVADVNLPAAQLQIGMGIPL 448
Cdd:pfam02786 140 MLREAAVKIARHLGYVGAGTVEFALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
101-219 |
2.11e-43 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 153.80 E-value: 2.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 101 INKVLIANNGIAAVKCMRSIRRWAyemfkneraIRFVVMVTPEDlkANAEYIKMADHYVPVPGGSNNNNYANVELIVDIA 180
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELG---------IRTVAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAA 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 665399403 181 LRTQVQAVWAGWGHASENPKLPELLHKEGLVFLGPPERA 219
Cdd:pfam00289 70 KETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
173-447 |
1.64e-38 |
|
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: 145.79 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 173 VELIVDIALRTQVQAVWAGWGHASEnpKLPELLHKEGLVflGPPERAMWALGDKVASSIVAQTAEIPTlPWSGsdlkaqy 252
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVE--TAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 253 sgkkikisselfargCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEV----PGSPIFVMK 328
Cdd:COG0439 74 ---------------LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNGEVLVEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 329 LARGaRHLEVQLLADQyGNAISlfgrdCSIQRRHQK---IIE---EAPAIVAqPEVFEDMEKAAVRLAKMVGYV-SAGTV 401
Cdd:COG0439 139 FLEG-REYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPLP-EELRAEIGELVARALRALGYRrGAFHT 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 665399403 402 EYLYDPEGRYFFLELNPRLQVEH--PCTEMVADVNLPAAQLQIGMGIP 447
Cdd:COG0439 211 EFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
486-592 |
8.00e-29 |
|
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: 112.12 E-value: 8.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 486 ARITSENPDEGFKPSSGTVQELNFRSSKNVwgYFSVAASGGLHE--FADSQFGHCFSWGENRQQARENLVIALKELSIRG 563
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 665399403 564 dFRTTVEYLITLLETNRFLDNSIDTAWLD 592
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
486-592 |
6.41e-26 |
|
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: 104.11 E-value: 6.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 486 ARITSENPDEGFKPSSGTVQELNFRSSKNVWGYFSVAASGGLHEFADSQFGHCFSWGENRQQARENLVIALKELSIRGdF 565
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*..
gi 665399403 566 RTTVEYLITLLETNRFLDNSIDTAWLD 592
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLE 107
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
732-793 |
5.40e-16 |
|
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: 74.37 E-value: 5.40e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665399403 732 LRSPSAGKLINMIVEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVTFVR-RPGAVLDAGSLL 793
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLL 64
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
732-793 |
4.71e-14 |
|
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: 68.78 E-value: 4.71e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665399403 732 LRSPSAGKLI-----NMIVEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVTFVRRP-GAVLDAGSLL 793
Cdd:pfam00364 3 IKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPL 70
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1645-2147 |
6.95e-12 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 70.44 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1645 NGREIIVIANDLTYLIGSFG----IKedvlFAKASQLARQLKVPRIYIsVNS-GARIGLAEEVKAMF-KIawedpeepdk 1718
Cdd:COG4799 80 DGRPVVVVANDFTVKGGSLGpmtaKK----ILRAQDIALENGLPVIYL-VDSgGARLQEGVESFAGYgRI---------- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1719 gFkylylstedYAQVanlnsvrailiedegeqrykitdiigkddglgvenlRYAGLIAgetsQayeeiVTIAMVTCrtIG 1798
Cdd:COG4799 145 -F---------YRNA------------------------------------RSSGGIP----Q-----ISVIMGPC--AA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1799 IGSYVVRLGQRVIQID-NSHIILTGyAALNKL-LGRKVyaSNNQLGGTQI-MFNNGVTHKTEAIDLDGVYTILDWLSYIP 1875
Cdd:COG4799 168 GGAYSPALSDFVIMVKgTSQMFLGG-PPVVKAaTGEEV--TAEELGGADVhARVSGVADYLAEDEEEALALARRLLSYLP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1876 AYIGCDLPIV---LPNDRIERPVDFMPT--KSPYDPRWMLGgRVnpvnandwengfFDRDSWSEIMASWAKTVVTGRARL 1950
Cdd:COG4799 245 SNNLEDPPRAepaPPARDPEELYGIVPEdpRKPYDMREVIA-RL------------VDGGSFFEFKPLYGPNIVTGFARI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 1951 GGVPVGVIAvetrtvevempADPANLdseaktlqqAGqVWYPDSSYKTAQAIKDFGREELPLIVFANWRGFsggmkdM-- 2028
Cdd:COG4799 312 DGRPVGIVA-----------NQPMVL---------AG-VLDIDAADKAARFIRLCDAFNIPLVFLVDVPGF------Mvg 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 2029 --YEQ--IVKFGAyivdglreyKkpvLIYLPPNAE-------LR---GGAWAVLDSL-INPRYMetYADPEARGGVLEPE 2093
Cdd:COG4799 365 teQERggIIRHGA---------K---LLYAVAEATvpkitviLRkayGAGYYAMCGKaLGPDFL--FAWPTAEIAVMGGE 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 665399403 2094 GIVEIkykekdlvktIHRldpttialkKELDEAnASGDKVRA---AQVDEKIKARIA 2147
Cdd:COG4799 431 GAANV----------LYR---------RELAAA-EDPEALRAeliAEYEEQANPYYA 467
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
269-448 |
1.82e-11 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 68.42 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 269 VTNVEQGLAAVNKIGFPVMIKASEG--------GGGKGIRRVDTTEEFPGLFRQ---------VQAEVPG--SPIFVmkl 329
Cdd:COG3919 138 LDSADDLDALAEDLGFPVVVKPADSvgydelsfPGKKKVFYVDDREELLALLRRiaaagyeliVQEYIPGddGEMRG--- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 330 argarhleVQLLADQYGNAISLFGRdcsiQRRHQKIIEEAPAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPE- 408
Cdd:COG3919 215 --------LTAYVDRDGEVVATFTG----RKLRHYPPAGGNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRd 282
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 665399403 409 GRYFFLELNPRLQVEHPCTEmVADVNLPAAQLQIGMGIPL 448
Cdd:COG3919 283 GEYKLIEINPRFWRSLYLAT-AAGVNFPYLLYDDAVGRPL 321
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
257-420 |
3.27e-10 |
|
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: 65.79 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 257 IKISSELFARGCVTNVEQGLAAVNKIGFPVMIKASE--GGGGKGIrrVDTTEEFPGLFRQVQAEVPGSPIFVMKLARGAR 334
Cdd:TIGR01369 136 KEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSASPINQVLVEKSLAGWK 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 335 HLEVQLLADQYGNAISLfgrdCSIQRRHQKIIEEAPAIVAQP------EVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPE 408
Cdd:TIGR01369 214 EIEYEVMRDSNDNCITV----CNMENFDPMGVHTGDSIVVAPsqtltdKEYQMLRDASIKIIRELGIEGGCNVQFALNPD 289
|
170
....*....|...
gi 665399403 409 -GRYFFLELNPRL 420
Cdd:TIGR01369 290 sGRYYVIEVNPRV 302
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
269-419 |
5.43e-10 |
|
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: 64.51 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 269 VTNVEQGLAAVNKIGFPVMIKASE--GGGGKGIrrVDTTEEFPGLFRQVQAEVPGSPIFVMKLARGARHLEVQLLADQYG 346
Cdd:COG0458 135 ATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGED 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 347 NAISLfgrdCSIQrrHqkiIEEA-----------PAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDpEGRYFFLE 415
Cdd:COG0458 213 NVIIV----GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD-DGRVYVIE 282
|
....
gi 665399403 416 LNPR 419
Cdd:COG0458 283 VNPR 286
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
727-793 |
5.29e-07 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 55.14 E-value: 5.29e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665399403 727 NDPSLLRSPSAGKLINMIVEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVTFV-RRPGAVLDAGSLL 793
Cdd:PRK12999 1074 GNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVlVKAGDQVEAGDLL 1141
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
284-446 |
5.64e-07 |
|
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: 54.15 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 284 FPVMIKASEGGGGKGIRRVDTTEE-FPGLFrqVQAEVPGSPIFVMKLARGaRHLEV-----QLLAD------QYGNAISl 351
Cdd:COG2232 139 GPWLVKPIGGAGGWHIRPADSEAPpAPGRY--FQRYVEGTPASVLFLADG-SDARVlgfnrQLIGPagerpfRYGGNIG- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 352 fgrdcsiqrrhqkiieeaPAIVAQPEVfEDMEKAAVRLAKMVGYVSAGTVEYLYDPEGrYFFLELNPRLQVEHPCTEMVA 431
Cdd:COG2232 215 ------------------PLALPPALA-EEMRAIAEALVAALGLVGLNGVDFILDGDG-PYVLEVNPRPQASLDLYEDAT 274
|
170
....*....|....*
gi 665399403 432 DVNLPAAQLQIGMGI 446
Cdd:COG2232 275 GGNLFDAHLRACRGE 289
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
269-419 |
5.67e-07 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 55.01 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 269 VTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEVPGSPIFVMKLARGARHLEVQLLADqyGNA 348
Cdd:TIGR01369 690 ATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 349 ISLFGrdcsIQrRHqkiIEEA-----------PAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDpEGRYFFLELN 417
Cdd:TIGR01369 768 VLIPG----IM-EH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVN 838
|
..
gi 665399403 418 PR 419
Cdd:TIGR01369 839 PR 840
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
273-419 |
3.28e-06 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 52.86 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 273 EQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEfpgLFRQVQAEV---PGSPIFVMKLARGARHLEVQLLADQYGNAI 349
Cdd:PLN02735 727 ADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDK---LKTYLETAVevdPERPVLVDKYLSDATEIDVDALADSEGNVV 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 350 SlfgrdCSIQRRhqkiIEEA-----------PAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPEGRYFFLELNP 418
Cdd:PLN02735 804 I-----GGIMEH----IEQAgvhsgdsacslPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANP 874
|
.
gi 665399403 419 R 419
Cdd:PLN02735 875 R 875
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
729-794 |
5.08e-06 |
|
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: 46.24 E-value: 5.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665399403 729 PSLLRSPSAGKLINMIVEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVT-FVRRPGAVLDAGSLLG 794
Cdd:cd06849 6 PDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAkILVEEGDTVPVGQVIA 72
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
269-420 |
1.23e-05 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 50.74 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 269 VTNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEVPGSPIFVMKLARGARHLEVQLLADQYGNA 348
Cdd:PRK12815 149 VTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNC 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665399403 349 ISLfgrdCSIQRRHQKIIEEAPAIVAQP------EVFEDMEKAAVRLAKMVGYVSAGTVEYLYDPEG-RYFFLELNPRL 420
Cdd:PRK12815 229 ITV----CNMENIDPVGIHTGDSIVVAPsqtltdDEYQMLRSASLKIISALGVVGGCNIQFALDPKSkQYYLIEVNPRV 303
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
737-797 |
1.96e-05 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 44.39 E-value: 1.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665399403 737 AGKLINMIVEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVTFVRRP-GAVLDAGSLLGHLE 797
Cdd:PRK08225 9 AGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQeGDFVNEGDVLLEIE 70
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
727-793 |
2.06e-05 |
|
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: 50.08 E-value: 2.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665399403 727 NDPSLLRSPSAGKLINMIVEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVTFVR-RPGAVLDAGSLL 793
Cdd:COG1038 1074 GNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLvKEGDQVEAGDLL 1141
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
270-419 |
1.21e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 47.66 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 270 TNVEQGLAAVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRqvQAEVPGSPIFVMKLARGARhLEVQLLADqygnai 349
Cdd:PRK12815 692 TDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLA--ENASQLYPILIDQFIDGKE-YEVDAISD------ 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 350 slfGRDCSIQR--RHqkiIEEA-----------PAIVAQPEVFEDMEKAAVRLAKMVGYVSAGTVEYLYDpEGRYFFLEL 416
Cdd:PRK12815 763 ---GEDVTIPGiiEH---IEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLA-NDEIYVLEV 835
|
...
gi 665399403 417 NPR 419
Cdd:PRK12815 836 NPR 838
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
729-794 |
3.72e-04 |
|
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: 40.82 E-value: 3.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665399403 729 PSLLRSPSAGKLINMIVEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVTFVRR-PGAVLDAGSLLG 794
Cdd:COG0508 8 PDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVkEGDTVPVGAVIA 74
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
278-419 |
6.92e-04 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 44.10 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 278 AVNKIGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQ-----VQAEVPGSPIfvmklargarhlEVQLLADQYGNAISLF 352
Cdd:PRK12767 143 AKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYvpnliIQEFIEGQEY------------TVDVLCDLNGEVISIV 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665399403 353 GRdcsiqRRHQKIIEEA--PAIVAQPEVFedmeKAAVRLAKMVGYVSAGTVEYLYDpEGRYFFLELNPR 419
Cdd:PRK12767 211 PR-----KRIEVRAGETskGVTVKDPELF----KLAERLAEALGARGPLNIQCFVT-DGEPYLFEINPR 269
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
269-308 |
1.75e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 43.55 E-value: 1.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 665399403 269 VTNVEQGLAAVNKIGFPVMIKAS--EGGGGKGIrrVDTTEEF 308
Cdd:PRK05294 149 AHSMEEALEVAEEIGYPVIIRPSftLGGTGGGI--AYNEEEL 188
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
269-419 |
1.93e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 42.83 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 269 VTNVEQGLAAVNKIGFPVMIKASEGG-GGKGIRRVDTTEEFPGLFrqvqAEVPGSPI----FVmKLARgarhlEVQLLAd 343
Cdd:PRK06019 121 VDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEAAW----ALLGSVPCileeFV-PFER-----EVSVIV- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 344 qygnAISLFGR----DCS--IQRRHQKIIEEAPAIVaQPEVFEDMEKAAVRLAKMVGYVsaGT--VEYLYDPEGRYFFLE 415
Cdd:PRK06019 190 ----ARGRDGEvvfyPLVenVHRNGILRTSIAPARI-SAELQAQAEEIASRIAEELDYV--GVlaVEFFVTGDGELLVNE 262
|
....
gi 665399403 416 LNPR 419
Cdd:PRK06019 263 IAPR 266
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
203-418 |
2.19e-03 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 42.40 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 203 ELLhkeGLVFLGPPERAMwALG-DKVASSIVAQTAEIPTLPWsgsdlkaqysgkkikissELFARGCVTNVEqglAAVNK 281
Cdd:COG1181 76 ELL---GIPYTGSGVLAS-ALAmDKALTKRVLAAAGLPTPPY------------------VVLRRGELADLE---AIEEE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 282 IGFPVMIKASEGGGGKGIRRVDTTEEFPGLFRQVQAEvpGSPIFVMKLARGaRHLEVQLLADQyGNAISLFGRdcsIQRR 361
Cdd:COG1181 131 LGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY--DDKVLVEEFIDG-REVTVGVLGNG-GPRALPPIE---IVPE 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665399403 362 H-----------QKIIEEAPAIVAqPEVFEDMEKAAVRLAKMV---GYvsaGTVEYLYDPEGRYFFLELNP 418
Cdd:COG1181 204 NgfydyeakytdGGTEYICPARLP-EELEERIQELALKAFRALgcrGY---ARVDFRLDEDGEPYLLEVNT 270
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
724-793 |
6.01e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 41.75 E-value: 6.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665399403 724 EKENDPSLLRSPSAGKLINMIVEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVT--FVrRPGAVLDAGSLL 793
Cdd:PRK09282 517 PRASAPGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKeiLV-KEGDRVNPGDVL 587
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
222-313 |
6.74e-03 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 40.86 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 222 ALG-DKVASSIVAQTAEIPTLPWSgsdlkaqysgkkikisselfargCVTNVEQGLAAVNKIGFPVMIKASEGGGGKGIR 300
Cdd:PRK01372 94 ALAmDKLRTKLVWQAAGLPTPPWI-----------------------VLTREEDLLAAIDKLGLPLVVKPAREGSSVGVS 150
|
90
....*....|...
gi 665399403 301 RVDTTEEFPGLFR 313
Cdd:PRK01372 151 KVKEEDELQAALE 163
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
234-418 |
7.25e-03 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 39.99 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 234 QTAEIPTLPWsgsdlKAQYSGKKIKISSELFArgcvtNVEQGLaavnkiGFPVMIKASEGGGGKGIRRVDTTEEFPGLFR 313
Cdd:pfam07478 3 KAAGLPVVPF-----VTFTRADWKLNPKEWCA-----QVEEAL------GYPVFVKPARLGSSVGVSKVESREELQAAIE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399403 314 ---QVQAEVpgspifVMKLARGARHLEVQLLADQYGNAISLfGR---DCSIQRRHQKIIEEA-----PAIVAqPEVFEDM 382
Cdd:pfam07478 67 eafQYDEKV------LVEEGIEGREIECAVLGNEDPEVSPV-GEivpSGGFYDYEAKYIDDSaqivvPADLE-EEQEEQI 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 665399403 383 EKAAVRLAKMVGYVSAGTVEYLYDPEGRYFFLELNP 418
Cdd:pfam07478 139 QELALKAYKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
745-797 |
7.58e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 37.30 E-value: 7.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 665399403 745 VEDGAHVSKGQAYAEIEVMKMVMTLTSQEAGTVT-FVRRPGAVLDAGSLLGHLE 797
Cdd:PRK07051 26 VEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVeFLVEDGEPVEAGQVLARIE 79
|
|
| |
