|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
650-1399 |
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: 1010.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 650 LDNPSKVQQAELHTGSLPQIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLpdpffSSRVKDWVERLMKTLRDPSLPLLEL 729
Cdd:pfam08326 2 LDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLEW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 730 QDIMTSVSGRIPLNVEKSIKKEMAQYASNitsvLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGI 809
Cdd:pfam08326 77 QEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 810 RGHMKAVVMDLLRQYLRVETQFQ--NGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGR---DPT 884
Cdd:pfam08326 153 KGHEYSVFASLLEEYYDVEKLFSggNVREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVSN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 885 LTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCIENLQKLILS 956
Cdd:pfam08326 233 VAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELIDS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 957 ETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRMSFASnl 1036
Cdd:pfam08326 313 KYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSP-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1037 nhyGMTHVASVSD-VLLDNAFTPPCQRMGGMVSFRTFEDFVRIFDEIMGCFCDSPPQSPTFPESghtslydedkvprDEP 1115
Cdd:pfam08326 391 ---PFKRIASVSDlSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESGESNSS-------------DEP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1116 IHILNVAIKTDGDIE-DDRLAAMFREFTQQNKATLVEHGIRRLTFLVAQKDfrkqvncevdqrfhREFPKFFTFRARDKF 1194
Cdd:pfam08326 455 INVLNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKD--------------GQYPKYFTFRGPDNY 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1195 EEDRIYRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVgtevTDYRFFVRAIIRHSDLVTKEASFEYLQN 1274
Cdd:pfam08326 521 EEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRDDIPTAEYLIS 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1275 EGERLLLEAMDELEVAfNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTTTGK 1354
Cdd:pfam08326 597 EAERLLNDILDALEVA-SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGP 675
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907079553 1355 AIPIRLFLTNESGYYLDISLYKEVTDSRtAQIMFQAYGdKQGPLH 1399
Cdd:pfam08326 676 PIPLRLVITNVSGYVVKVELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1499-2047 |
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: 606.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1499 PEYPDGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEgIPRIYVAANSGARIGLAEEIRHMFHVAWVDPEDPYKGY 1578
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1579 KylyLTPQDYKRVSAlnsvhcehvedeGESRYKITDIIGKEEGLGAENLRGSGMIAGESSLAYDEVITISLVTCRAIGIG 1658
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1659 AYLVRLGQRTIQVEN-SHLILTGAGALNKVLGrEVYTSNNQLGGIQIMHNNGVTHSTVCDDFEGVFTVLHWLSYMPKSVH 1737
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1738 S---SVPLLNSKDPIDR---IIEFVPT--KAPYDPRWMLAGRphptqkgqwlsgfFDYGSFSEIMQPWAQTVVVGRARLG 1809
Cdd:pfam01039 224 NnrePVPIVPTKDPPDRdapLVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1810 GIPVGVVAVETRtvelsipadpanldseakiiQQAGqVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQ 1889
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1890 VLKFGAYIVDGLRECSQPVMVYIPPqaELRGGSWVVIDPTINPRHMeMYADRESRGSVLEPEGTVEIKFRKKDLVKTMRR 1969
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907079553 1970 VDPvyirlaerlgtpelspteRKELESKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVINDILDWKTSRtFFYW 2047
Cdd:pfam01039 427 KDL------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-457 |
1.04e-132 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 424.81 E-value: 1.04e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1 MADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVA 80
Cdd:COG4770 44 LADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 81 QTAGIPTLPWSgsglrvdwqendfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDF 160
Cdd:COG4770 124 KAAGVPVVPGS--------------------------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 161 PNLFRQVQAEVP---GSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQ 236
Cdd:COG4770 178 EEAFESARREAKaafGDDrVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 237 CAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRmmygvspw 315
Cdd:COG4770 258 AAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLpFTQEDIK-------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 316 gdapidfensahvpcPRGHVIAARITSENPDEGFKPSSGTVQELNFRsnknvwGYFSVAAAGGLHE------FADSQFGH 389
Cdd:COG4770 330 ---------------LRGHAIECRINAEDPARGFLPSPGTITRLRPP------GGPGVRVDSGVYEgyeippYYDSMIAK 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907079553 390 CFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQAERPD 457
Cdd:COG4770 389 LIVWGPDREEAIARMRRALAEFVIEG-VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-453 |
5.22e-111 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 361.81 E-value: 5.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1 MADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVA 80
Cdd:PRK08591 44 LADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 81 QTAGIPTLPwsGSglrvdwqendfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDF 160
Cdd:PRK08591 124 KKAGVPVVP--GS------------------------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 161 PNLFRQVQAEVP---GSPIFVM-RLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQ 236
Cdd:PRK08591 178 EKAFSMARAEAKaafGNPGVYMeKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 237 CAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspw 315
Cdd:PRK08591 258 AAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLsIKQEDIVF------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 316 gdapidfensahvpcpRGHVIAARITSENPDEGFKPSSGTVQelnfrsnknvwGYFsvaAAGGLH--------------E 381
Cdd:PRK08591 331 ----------------RGHAIECRINAEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipP 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907079553 382 FADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQA 453
Cdd:PRK08591 381 YYDSMIGKLIVHGETREEAIARMKRALSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-449 |
5.43e-100 |
|
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: 330.18 E-value: 5.43e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1 MADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVA 80
Cdd:TIGR00514 44 LADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 81 QTAGIPTLPWSgsglrvdwqendfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDF 160
Cdd:TIGR00514 124 KKAGVPCVPGS--------------------------DGLVEDEEENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 161 PNLFRQVQAEVP---GSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQ 236
Cdd:TIGR00514 178 VKSISMTRAEAKaafGNDgVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 237 CAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspw 315
Cdd:TIGR00514 258 AAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPLsLKQEDVVV------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 316 gdapidfensahvpcpRGHVIAARITSENPDEGFKPSSGTVQE------LNFRSNKNVWGYFSVAAagglheFADSQFGH 389
Cdd:TIGR00514 331 ----------------RGHAIECRINAEDPIKTFLPSPGRITRylppggPGVRWDSHVYSGYTVPP------YYDSMIGK 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 390 CFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAE 449
Cdd:TIGR00514 389 LITYGKTREVAIARMKRALSEFIIDG-IKTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
119-300 |
6.04e-62 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 211.01 E-value: 6.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 119 GYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSP----IFVMRLAKQSRHLEVQILA 194
Cdd:pfam02786 22 GPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 195 DQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQD-GSFYFLELNPRLQ 273
Cdd:pfam02786 102 DAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsGEYYFIEMNTRLQ 181
|
170 180
....*....|....*....|....*..
gi 1907079553 274 VEHPCTEMVADVNLPAAQLQIAMGIPL 300
Cdd:pfam02786 182 VEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
338-444 |
2.93e-32 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 122.14 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 338 ARITSENPDEGFKPSSGTVQELNFRSNKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 415
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 1907079553 416 dFRTTVEYLIKLLETESFQLNRIDTGWLD 444
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1486-1817 |
1.41e-19 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 94.71 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1486 EIGM-VAWKMSLKSPEYP-----------DGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVAANSGAR 1553
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPgdgvvtgigtvDGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1554 IGLAEEIRHMFhvawvdpedpykgykylyltpqdykrvsalnsvhcehvedeGESRYKitdiigkeeglgaeNLRGSGMI 1633
Cdd:COG4799 131 LQEGVESFAGY-----------------------------------------GRIFYR--------------NARSSGGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1634 AgesslaydeviTISLVTCRAIGIGAYLVRLGQRTIQVE-NSHLILTGAGALNKVLGREVytSNNQLGGIQiMHN--NGV 1710
Cdd:COG4799 156 P-----------QISVIMGPCAAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvSGV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1711 THSTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDP---IDRIIEFVPT--KAPYDPRWMLAGrphptqkgqwlsgFF 1785
Cdd:COG4799 222 ADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPPardPEELYGIVPEdpRKPYDMREVIAR-------------LV 288
|
330 340 350
....*....|....*....|....*....|..
gi 1907079553 1786 DYGSFSEIMQPWAQTVVVGRARLGGIPVGVVA 1817
Cdd:COG4799 289 DGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA 320
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
583-648 |
1.47e-17 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 78.80 E-value: 1.47e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907079553 583 VMRSPSAGKLI-----QYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRP-GAALDPGCVIAKM 648
Cdd:pfam00364 2 EIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
585-648 |
7.17e-14 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 68.21 E-value: 7.17e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907079553 585 RSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVK-RPGAALDPGCVIAKM 648
Cdd:cd06850 3 TAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1645-1898 |
6.64e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 44.80 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1645 ITISLVTCRAiGiGAYLVRLGQRTIQV-ENSHLILTGAGALNKVLGREVytSNNQLGGIQImH--NNGVTHSTVCDDFEG 1721
Cdd:PLN02820 209 IALVLGSCTA-G-GAYVPAMADESVIVkGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-HckVSGVSDHFAQDELHA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1722 ------VFTVLHWLSYMPKSVHSSVPLLNSKDPIDRIIEF---VPT--KAPYDPRWMLAGrphptqkgqwlsgFFDYGSF 1790
Cdd:PLN02820 284 laigrnIVKNLHLAAKQGMENTLGSKNPEYKEPLYDVKELrgiVPAdhKQSFDVRSVIAR-------------IVDGSEF 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1791 SEIMQPWAQTVVVGRARLGGIPVGVVAvetrtvelsipadpanldseakiiqqAGQVWFPDSAFKTYQAIKDFNREGLPL 1870
Cdd:PLN02820 351 DEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALKGAHFIELCAQRGIPL 404
|
250 260
....*....|....*....|....*...
gi 1907079553 1871 MVFANWRGFSGGMKDMYDQVLKFGAYIV 1898
Cdd:PLN02820 405 LFLQNITGFMVGSRSEASGIAKAGAKMV 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
650-1399 |
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: 1010.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 650 LDNPSKVQQAELHTGSLPQIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLpdpffSSRVKDWVERLMKTLRDPSLPLLEL 729
Cdd:pfam08326 2 LDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLEW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 730 QDIMTSVSGRIPLNVEKSIKKEMAQYASNitsvLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGI 809
Cdd:pfam08326 77 QEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 810 RGHMKAVVMDLLRQYLRVETQFQ--NGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGR---DPT 884
Cdd:pfam08326 153 KGHEYSVFASLLEEYYDVEKLFSggNVREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVSN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 885 LTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCIENLQKLILS 956
Cdd:pfam08326 233 VAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELIDS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 957 ETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRMSFASnl 1036
Cdd:pfam08326 313 KYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSP-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1037 nhyGMTHVASVSD-VLLDNAFTPPCQRMGGMVSFRTFEDFVRIFDEIMGCFCDSPPQSPTFPESghtslydedkvprDEP 1115
Cdd:pfam08326 391 ---PFKRIASVSDlSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESGESNSS-------------DEP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1116 IHILNVAIKTDGDIE-DDRLAAMFREFTQQNKATLVEHGIRRLTFLVAQKDfrkqvncevdqrfhREFPKFFTFRARDKF 1194
Cdd:pfam08326 455 INVLNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKD--------------GQYPKYFTFRGPDNY 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1195 EEDRIYRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVgtevTDYRFFVRAIIRHSDLVTKEASFEYLQN 1274
Cdd:pfam08326 521 EEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRDDIPTAEYLIS 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1275 EGERLLLEAMDELEVAfNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTTTGK 1354
Cdd:pfam08326 597 EAERLLNDILDALEVA-SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGP 675
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907079553 1355 AIPIRLFLTNESGYYLDISLYKEVTDSRtAQIMFQAYGdKQGPLH 1399
Cdd:pfam08326 676 PIPLRLVITNVSGYVVKVELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1499-2047 |
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: 606.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1499 PEYPDGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEgIPRIYVAANSGARIGLAEEIRHMFHVAWVDPEDPYKGY 1578
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1579 KylyLTPQDYKRVSAlnsvhcehvedeGESRYKITDIIGKEEGLGAENLRGSGMIAGESSLAYDEVITISLVTCRAIGIG 1658
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1659 AYLVRLGQRTIQVEN-SHLILTGAGALNKVLGrEVYTSNNQLGGIQIMHNNGVTHSTVCDDFEGVFTVLHWLSYMPKSVH 1737
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1738 S---SVPLLNSKDPIDR---IIEFVPT--KAPYDPRWMLAGRphptqkgqwlsgfFDYGSFSEIMQPWAQTVVVGRARLG 1809
Cdd:pfam01039 224 NnrePVPIVPTKDPPDRdapLVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1810 GIPVGVVAVETRtvelsipadpanldseakiiQQAGqVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQ 1889
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1890 VLKFGAYIVDGLRECSQPVMVYIPPqaELRGGSWVVIDPTINPRHMeMYADRESRGSVLEPEGTVEIKFRKKDLVKTMRR 1969
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907079553 1970 VDPvyirlaerlgtpelspteRKELESKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVINDILDWKTSRtFFYW 2047
Cdd:pfam01039 427 KDL------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-457 |
1.04e-132 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 424.81 E-value: 1.04e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1 MADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVA 80
Cdd:COG4770 44 LADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 81 QTAGIPTLPWSgsglrvdwqendfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDF 160
Cdd:COG4770 124 KAAGVPVVPGS--------------------------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 161 PNLFRQVQAEVP---GSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQ 236
Cdd:COG4770 178 EEAFESARREAKaafGDDrVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 237 CAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRmmygvspw 315
Cdd:COG4770 258 AAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLpFTQEDIK-------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 316 gdapidfensahvpcPRGHVIAARITSENPDEGFKPSSGTVQELNFRsnknvwGYFSVAAAGGLHE------FADSQFGH 389
Cdd:COG4770 330 ---------------LRGHAIECRINAEDPARGFLPSPGTITRLRPP------GGPGVRVDSGVYEgyeippYYDSMIAK 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907079553 390 CFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQAERPD 457
Cdd:COG4770 389 LIVWGPDREEAIARMRRALAEFVIEG-VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-453 |
5.22e-111 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 361.81 E-value: 5.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1 MADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVA 80
Cdd:PRK08591 44 LADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 81 QTAGIPTLPwsGSglrvdwqendfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDF 160
Cdd:PRK08591 124 KKAGVPVVP--GS------------------------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 161 PNLFRQVQAEVP---GSPIFVM-RLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQ 236
Cdd:PRK08591 178 EKAFSMARAEAKaafGNPGVYMeKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 237 CAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspw 315
Cdd:PRK08591 258 AAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLsIKQEDIVF------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 316 gdapidfensahvpcpRGHVIAARITSENPDEGFKPSSGTVQelnfrsnknvwGYFsvaAAGGLH--------------E 381
Cdd:PRK08591 331 ----------------RGHAIECRINAEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipP 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907079553 382 FADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQA 453
Cdd:PRK08591 381 YYDSMIGKLIVHGETREEAIARMKRALSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
17-444 |
2.62e-100 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 351.75 E-value: 2.62e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 17 YANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGlr 96
Cdd:PRK12999 64 YLDIDEIIRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGP-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 97 vdwqendfskrilnvpqdlyekgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---G 173
Cdd:PRK12999 142 ------------------------IDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 174 SP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGT 252
Cdd:PRK12999 198 NDeVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 253 VEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLfrikdirmmygvspwGDAPIDFENSAHVpCPR 332
Cdd:PRK12999 278 VEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATL---------------HDLEIGIPSQEDI-RLR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 333 GHVIAARITSENPDEGFKPSSGTVQElnFRSNknvwGYFSV------AAAGGlhEFA---DSQFGHCFSWGENREEAISN 403
Cdd:PRK12999 342 GYAIQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVrldggnAFAGA--EITpyyDSLLVKLTAWGRTFEQAVAR 413
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1907079553 404 MVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD 444
Cdd:PRK12999 414 MRRALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFID 453
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
2-452 |
4.83e-100 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 332.33 E-value: 4.83e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 2 ADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQ 81
Cdd:PRK08654 45 ADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 82 TAGIPTLPWSGSGlrvdwqendfskrilnvpqdlyekgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFP 161
Cdd:PRK08654 125 KAGVPVLPGTEEG--------------------------IEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 162 NLF---RQVQAEVPGSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQC 237
Cdd:PRK08654 179 DAIestQSIAQSAFGDStVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 238 AVKLAKMVGYVSAGTVEYLYSqDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspwg 316
Cdd:PRK08654 259 AVKAAKAINYENAGTVEFLYS-NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELsFKQEDITI-------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 317 dapidfensahvpcpRGHVIAARITSENPDEGFKPSSGTVQelnfrsnknvwGYFSVAAAG-----GLH------EFADS 385
Cdd:PRK08654 330 ---------------RGHAIECRINAEDPLNDFAPSPGKIK-----------RYRSPGGPGvrvdsGVHmgyeipPYYDS 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907079553 386 QFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD--RLIAEKVQ 452
Cdd:PRK08654 384 MISKLIVWGRTREEAIARMRRALYEYVIVG-VKTNIPFHKAVMENENFVRGNLHTHFIEeeTTILEEMK 451
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-449 |
5.43e-100 |
|
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: 330.18 E-value: 5.43e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1 MADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVA 80
Cdd:TIGR00514 44 LADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 81 QTAGIPTLPWSgsglrvdwqendfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDF 160
Cdd:TIGR00514 124 KKAGVPCVPGS--------------------------DGLVEDEEENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 161 PNLFRQVQAEVP---GSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQ 236
Cdd:TIGR00514 178 VKSISMTRAEAKaafGNDgVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 237 CAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspw 315
Cdd:TIGR00514 258 AAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPLsLKQEDVVV------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 316 gdapidfensahvpcpRGHVIAARITSENPDEGFKPSSGTVQE------LNFRSNKNVWGYFSVAAagglheFADSQFGH 389
Cdd:TIGR00514 331 ----------------RGHAIECRINAEDPIKTFLPSPGRITRylppggPGVRWDSHVYSGYTVPP------YYDSMIGK 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 390 CFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAE 449
Cdd:TIGR00514 389 LITYGKTREVAIARMKRALSEFIIDG-IKTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
17-444 |
1.95e-97 |
|
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: 343.21 E-value: 1.95e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 17 YANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSglr 96
Cdd:COG1038 63 YLDIEEIIRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP--GT--- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 97 vdwqendfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---G 173
Cdd:COG1038 138 ---------------------EGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 174 SP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGT 252
Cdd:COG1038 197 DDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 253 VEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLfrikdirmmygvspwGDAPIDFENSAHVPCpR 332
Cdd:COG1038 277 VEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSL---------------DDPEIGIPSQEDIRL-N 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 333 GHVIAARITSENPDEGFKPSSGTVQElnFRSnknvwgyfsvaaAGGlhefadsqFG------HCFS-------------- 392
Cdd:COG1038 341 GYAIQCRITTEDPANNFMPDTGRITA--YRS------------AGG--------FGirldggNAYTgavitpyydsllvk 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1907079553 393 ---WGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD 444
Cdd:COG1038 399 vtaWGRTFEEAIRKMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFID 452
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-445 |
2.71e-97 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 322.36 E-value: 2.71e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1 MADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVA 80
Cdd:PRK06111 44 MADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 81 QTAGIPTLPWSGSGLrvdwqendfskrilnvpqdlyekgyvKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDF 160
Cdd:PRK06111 124 QAAGVPVVPGITTNL--------------------------EDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 161 PNLFRQVQAEVP---GSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQ 236
Cdd:PRK06111 178 TKAFESNKKRAAnffGNGeMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 237 CAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspw 315
Cdd:PRK06111 258 RAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 316 gdapidfensahvpcpRGHVIAARITSENPDEgFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGE 395
Cdd:PRK06111 331 ----------------SGHAIEVRIYAEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1907079553 396 NREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDR 445
Cdd:PRK06111 394 TREEAISRLHDALEELKVEG-IKTNIPLLLQVLEDPVFKAGGYTTGFLTK 442
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-453 |
9.10e-92 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 307.07 E-value: 9.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1 MADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVA 80
Cdd:PRK12833 47 MADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 81 QTAGIPTLPWSgsglrvdwqendfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDF 160
Cdd:PRK12833 127 RRAGVPTVPGS--------------------------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 161 PNLFRQVQAEVP---GSP-IFVMRLAKQSRHLEVQILADQYgNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQ 236
Cdd:PRK12833 181 AAELPLAQREAQaafGDGgVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 237 CAVKLAKMVGYVSAGTVEYLY-SQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvsp 314
Cdd:PRK12833 260 SAVRLARQVGYRGAGTLEYLFdDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLrFAQGDIAL------ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 315 wgdapidfensahvpcpRGHVIAARITSENPDEGFKPSSGTVQELNF------RSNKNVWGYFSVAAagglheFADSQFG 388
Cdd:PRK12833 334 -----------------RGAALECRINAEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYPGYRVPP------FYDSLLA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907079553 389 HCFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQA 453
Cdd:PRK12833 391 KLIVHGEDRAAALARAARALRELRIDG-MKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAA 454
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
2-445 |
9.53e-91 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 303.20 E-value: 9.53e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 2 ADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQ 81
Cdd:PRK08462 47 ADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 82 TAGIPTLPWSgsglrvdwqendfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFP 161
Cdd:PRK08462 127 RAGVPVIPGS--------------------------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 162 NLFRQVQAEVPGS----PIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQC 237
Cdd:PRK08462 181 NLYLAAESEALSAfgdgTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHET 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 238 AVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLFRIKDIRMmygvspwgd 317
Cdd:PRK08462 261 AIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKL--------- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 318 apidfensahvpcpRGHVIAARITSENPdEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQFGHCF 391
Cdd:PRK08462 332 --------------KGHAIECRITAEDP-KKFYPSPGKITKWiapggrNVRMDSHAYAGYVVPP------YYDSMIGKLI 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1907079553 392 SWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDR 445
Cdd:PRK08462 391 VWGEDRNRAIAKMKRALKEFKVEG-IKTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-445 |
4.01e-90 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 301.63 E-value: 4.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1 MADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVA 80
Cdd:PRK05586 44 LADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 81 QTAGIPTLPWSgsglrvdwqendfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDF 160
Cdd:PRK05586 124 IKAGVPVVPGS--------------------------EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 161 PNLFRQVQAEVPGS----PIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQ 236
Cdd:PRK05586 178 IKAFNTAKSEAKAAfgddSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 237 CAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspw 315
Cdd:PRK05586 258 IAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLsIKQEDIKI------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 316 gdapidfensahvpcpRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGE 395
Cdd:PRK05586 331 ----------------NGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGK 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1907079553 396 NREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDR 445
Cdd:PRK05586 395 DREEAIQKMKRALGEFIIEG-VNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
2-446 |
1.27e-85 |
|
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: 308.11 E-value: 1.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 2 ADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQ 81
Cdd:TIGR02712 44 ADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGYGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 82 TAGIPTLPwsGSGLrvdwqendfskrilnvpqdlyekgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFP 161
Cdd:TIGR02712 124 AAGVPLLP--GTGL-------------------------LSSLDEALEAAKEIGYPVMLKSTAGGGGIGMQKCDSAAELA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 162 NLF----RQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQC 237
Cdd:TIGR02712 177 EAFetvkRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEETPAPNLPPETRQALLAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 238 AVKLAKMVGYVSAGTVEYLY-SQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAmgiplfrikdirmmygvspwG 316
Cdd:TIGR02712 257 AERLGEAVNYRSAGTVEFIYdEARDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIA--------------------A 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 317 DAPIDFENSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYfsVAAAGGLHEFADSQFGHCFSWGEN 396
Cdd:TIGR02712 317 GELPDFASLNISLTPRGAAIEARVYAENPAKNFQPSPGLLTDVQFPDDVRVDTW--VETGTEVSPEYDPMLAKIIVHGSD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1907079553 397 REEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRL 446
Cdd:TIGR02712 395 REDAILKLHQALAETRVYG-IETNLDYLRSILSSETFRSAQVSTRTLNSF 443
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
17-444 |
8.93e-84 |
|
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: 301.36 E-value: 8.93e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 17 YANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglr 96
Cdd:TIGR01235 60 YLSIDEIIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 97 vdwqendfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGS-- 174
Cdd:TIGR01235 135 ---------------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfg 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 175 --PIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGT 252
Cdd:TIGR01235 194 ndEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 253 VEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-------FRIKDIRMmygvspwgdapidfens 325
Cdd:TIGR01235 274 VEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLptpqlgvPNQEDIRT----------------- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 326 ahvpcpRGHVIAARITSENPDEGFKPSSGTVQElnFRSNknvwGYFSVAAAGG-------LHEFADSQFGHCFSWGENRE 398
Cdd:TIGR01235 337 ------NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPE 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907079553 399 EAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD 444
Cdd:TIGR01235 405 EAAAKMDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
17-444 |
3.63e-83 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 282.38 E-value: 3.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 17 YANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglr 96
Cdd:PRK07178 59 YLNPRRLVNLAVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGS----- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 97 vdwqendfskrilnvpqdlyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---G 173
Cdd:PRK07178 134 ---------------------EGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 174 SP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGT 252
Cdd:PRK07178 193 SAeVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 253 VEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-FRIKDIRMmygvspwgdapidfensahvpcp 331
Cdd:PRK07178 273 VEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH----------------------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 332 RGHVIAARITSENPDEGFKPSSGTVQElnfrsnknvwgYFSVAAAG---------GLH--EFADSQFGHCFSWGENREEA 400
Cdd:PRK07178 330 RGFALQFRINAEDPKNDFLPSFGKITR-----------YYAPGGPGvrtdtaiytGYTipPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1907079553 401 ISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD 444
Cdd:PRK07178 399 LDRGRRALDDMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVE 441
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
17-467 |
1.14e-66 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 234.71 E-value: 1.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 17 YANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglr 96
Cdd:PRK08463 59 YLDVKRIVEIAKACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGT----- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 97 vdwqendfskrilnvpqdlyEKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLF----RQVQAEVP 172
Cdd:PRK08463 134 --------------------EKLNSESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFesckREALAYFN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 173 GSPIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGT 252
Cdd:PRK08463 194 NDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 253 VEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMG-IPLFRIKDIRmmygvspwgdapidfensahvpcP 331
Cdd:PRK08463 274 IEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGeILDLEQSDIK-----------------------P 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 332 RGHVIAARITSENPDEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMV 405
Cdd:PRK08463 331 RGFAIEARITAENVWKNFIPSPGKITEYypalgpSVRVDSHIYKDYTIPP------YYDSMLAKLIVKATSYDLAVNKLE 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907079553 406 VALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQA------ERPDTMLGVVCGAL 467
Cdd:PRK08463 405 RALKEFVIDG-IRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKtedrhqENKEEVIAAIAAAL 471
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
119-300 |
6.04e-62 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 211.01 E-value: 6.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 119 GYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSP----IFVMRLAKQSRHLEVQILA 194
Cdd:pfam02786 22 GPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 195 DQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQD-GSFYFLELNPRLQ 273
Cdd:pfam02786 102 DAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsGEYYFIEMNTRLQ 181
|
170 180
....*....|....*....|....*..
gi 1907079553 274 VEHPCTEMVADVNLPAAQLQIAMGIPL 300
Cdd:pfam02786 182 VEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
20-301 |
2.39e-43 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 159.65 E-value: 2.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 20 VELILDIAKRIPVQAVWAGWGHASEnpKLPELLLKNGIAfmGPPSQAMWALGDKIASSIVAQTAGIPTlPWSGSglrvdw 99
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVE--TAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFAL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 100 qendfskrilnvpqdlyekgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEV----PGSP 175
Cdd:COG0439 75 ---------------------VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNGE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 176 IFVMRLAkQSRHLEVQILADQyGNAISlfgrdCSVQRRHQK---IIE---EAPAAIaTPAVFEHMEQCAVKLAKMVGYV- 248
Cdd:COG0439 134 VLVEEFL-EGREYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPL-PEELRAEIGELVARALRALGYRr 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907079553 249 SAGTVEYLYSQDGSFYFLELNPRLQVEH--PCTEMVADVNLPAAQLQIAMGIPLF 301
Cdd:COG0439 206 GAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEPRI 260
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
338-444 |
2.93e-32 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 122.14 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 338 ARITSENPDEGFKPSSGTVQELNFRSNKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 415
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 1907079553 416 dFRTTVEYLIKLLETESFQLNRIDTGWLD 444
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
338-445 |
1.24e-29 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 114.51 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 338 ARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 417
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*...
gi 1907079553 418 RTTVEYLIKLLETESFQLNRIDTGWLDR 445
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
1-66 |
1.35e-24 |
|
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: 100.25 E-value: 1.35e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907079553 1 MADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQA 66
Cdd:pfam00289 43 LADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1486-1817 |
1.41e-19 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 94.71 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1486 EIGM-VAWKMSLKSPEYP-----------DGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVAANSGAR 1553
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPgdgvvtgigtvDGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1554 IGLAEEIRHMFhvawvdpedpykgykylyltpqdykrvsalnsvhcehvedeGESRYKitdiigkeeglgaeNLRGSGMI 1633
Cdd:COG4799 131 LQEGVESFAGY-----------------------------------------GRIFYR--------------NARSSGGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1634 AgesslaydeviTISLVTCRAIGIGAYLVRLGQRTIQVE-NSHLILTGAGALNKVLGREVytSNNQLGGIQiMHN--NGV 1710
Cdd:COG4799 156 P-----------QISVIMGPCAAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvSGV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1711 THSTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDP---IDRIIEFVPT--KAPYDPRWMLAGrphptqkgqwlsgFF 1785
Cdd:COG4799 222 ADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPPardPEELYGIVPEdpRKPYDMREVIAR-------------LV 288
|
330 340 350
....*....|....*....|....*....|..
gi 1907079553 1786 DYGSFSEIMQPWAQTVVVGRARLGGIPVGVVA 1817
Cdd:COG4799 289 DGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA 320
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
583-648 |
1.47e-17 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 78.80 E-value: 1.47e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907079553 583 VMRSPSAGKLI-----QYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRP-GAALDPGCVIAKM 648
Cdd:pfam00364 2 EIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
585-648 |
7.17e-14 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 68.21 E-value: 7.17e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907079553 585 RSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVK-RPGAALDPGCVIAKM 648
Cdd:cd06850 3 TAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
2-307 |
1.74e-13 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 74.58 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 2 ADHYVPVPGgPNNNNYANVELILDIAKRIPVQAVWA---GWGHA-SEN-PKLPElllknGIAFMGPPSQAMWALGDKIAS 76
Cdd:COG3919 48 VDEVVVVPD-PGDDPEAFVDALLELAERHGPDVLIPtgdEYVELlSRHrDELEE-----HYRLPYPDADLLDRLLDKERF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 77 SIVAQTAGIPTlPWSGsglrvdwqendfskrilnvpqdlyekgYVKDVDDGLKAAEEVGYPVMIKASEG--------GGG 148
Cdd:COG3919 122 YELAEELGVPV-PKTV---------------------------VLDSADDLDALAEDLGFPVVVKPADSvgydelsfPGK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 149 KGIRKVNNADDFPNLFRQ---------VQAEVPGSpifvmrlakQSRHLEVQILADQYGNAISLFGrdcsvqrrHQKIIE 219
Cdd:COG3919 174 KKVFYVDDREELLALLRRiaaagyeliVQEYIPGD---------DGEMRGLTAYVDRDGEVVATFT--------GRKLRH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 220 eAPAAIATPAVFEH-----MEQCAVKLAKMVGYVSAGTVEYLY-SQDGSFYFLELNPRLQVEHPCTEmVADVNLPAAQLQ 293
Cdd:COG3919 237 -YPPAGGNSAARESvddpeLEEAARRLLEALGYHGFANVEFKRdPRDGEYKLIEINPRFWRSLYLAT-AAGVNFPYLLYD 314
|
330
....*....|....
gi 1907079553 294 IAMGIPLFRIKDIR 307
Cdd:COG3919 315 DAVGRPLEPVPAYR 328
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
104-301 |
3.77e-09 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 62.32 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 104 FSKRI--LNVPQDlyEKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRL 181
Cdd:TIGR01369 673 FSELLdeLGIPQP--KWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKY 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 182 AKQSRHLEVQILADqyGNAISLFGrdcsvQRRHqkiIEEA-----------PAAIATPAVFEHMEQCAVKLAKMVGYVSA 250
Cdd:TIGR01369 751 LEDAVEVDVDAVSD--GEEVLIPG-----IMEH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGL 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907079553 251 GTVEYLYSqDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLF 301
Cdd:TIGR01369 821 MNIQFAVK-DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLE 870
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
119-271 |
8.57e-09 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 60.95 E-value: 8.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 119 GYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDfpnLFRQVQAEV---PGSPIFVMRLAKQSRHLEVQILAD 195
Cdd:PLN02735 721 GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDK---LKTYLETAVevdPERPVLVDKYLSDATEIDVDALAD 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 196 QYGNAISlfgrdCSVQRRhqkiIEEA-----------PAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFY 264
Cdd:PLN02735 798 SEGNVVI-----GGIMEH----IEQAgvhsgdsacslPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVY 868
|
....*..
gi 1907079553 265 FLELNPR 271
Cdd:PLN02735 869 IIEANPR 875
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
120-271 |
1.15e-07 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 53.41 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 120 YVKDVDDGLKAAEEVGYPVMIKASEGG-GGKGIRKVNNADDFPnlfrQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYG 198
Cdd:pfam02222 12 AAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLP----QAWEELGDGPVIVEEFVPFDRELSVLVVRSVDG 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907079553 199 NAISlfgrdCS-VQRRHQK---IIEEAPAAIaTPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPR 271
Cdd:pfam02222 88 ETAF-----YPvVETIQEDgicRLSVAPARV-PQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLINELAPR 158
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
119-271 |
2.49e-07 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 55.65 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 119 GYVKDVDDGLKAAEEVGYPVMIKASE--GGGGKGIrkVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEVQILADQ 196
Cdd:COG0458 133 GTATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 197 YGNAISLfgrdCSVQrrHqkiIEEA-----------PAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYsQDGSFYF 265
Cdd:COG0458 211 EDNVIIV----GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAV-DDGRVYV 280
|
....*.
gi 1907079553 266 LELNPR 271
Cdd:COG0458 281 IEVNPR 286
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
104-272 |
4.13e-07 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 55.39 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 104 FSKRILNVPQDLYEKGYVKDVDDGLKAAEEVGYPVMIKASE--GGGGKGIrkVNNADDFPNLFRQVQAEVPGSPIFVMRL 181
Cdd:TIGR01369 131 FREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSASPINQVLVEKS 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 182 AKQSRHLEVQILADQYGNAISLfgrdCSVQR-----RHQ-KIIEEAPAAIATPAVFEHMEQCAVKLAKMVGYVSAGTVEY 255
Cdd:TIGR01369 209 LAGWKEIEYEVMRDSNDNCITV----CNMENfdpmgVHTgDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQF 284
|
170
....*....|....*...
gi 1907079553 256 -LYSQDGSFYFLELNPRL 272
Cdd:TIGR01369 285 aLNPDSGRYYVIEVNPRV 302
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
130-298 |
2.19e-06 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 52.23 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 130 AAEEVGYPVMIKASEGGGGKGIRKVNNAD-DFPNLFrqVQAEVPGSPIfvmrlakqSrhleVQILADqygnaislfGRDC 208
Cdd:COG2232 133 EPPPDPGPWLVKPIGGAGGWHIRPADSEApPAPGRY--FQRYVEGTPA--------S----VLFLAD---------GSDA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 209 SVQRRHQKIIEEAPAA------IATPAVFEH-----MEQCAVKLAKMVGYVSAGTVEYLYSQDGsFYFLELNPRLQVEHP 277
Cdd:COG2232 190 RVLGFNRQLIGPAGERpfryggNIGPLALPPalaeeMRAIAEALVAALGLVGLNGVDFILDGDG-PYVLEVNPRPQASLD 268
|
170 180
....*....|....*....|.
gi 1907079553 278 CTEMVADVNLPAAQLQIAMGI 298
Cdd:COG2232 269 LYEDATGGNLFDAHLRACRGE 289
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
104-271 |
7.98e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 50.27 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 104 FSKRILNVPQDlYEKGYVKDVDDGLkAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQ-----VQAEVPGSPIfv 178
Cdd:PRK12767 119 LKENGIPTPKS-YLPESLEDFKAAL-AKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYvpnliIQEFIEGQEY-- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 179 mrlakqsrhlEVQILADQYGNAISLFGRdcsvqRRHQKIIEEAPAAIAT--PAVFEHMEQCAVKLakmvGYVSAGTVEYL 256
Cdd:PRK12767 195 ----------TVDVLCDLNGEVISIVPR-----KRIEVRAGETSKGVTVkdPELFKLAERLAEAL----GARGPLNIQCF 255
|
170
....*....|....*
gi 1907079553 257 YSqDGSFYFLELNPR 271
Cdd:PRK12767 256 VT-DGEPYLFEINPR 269
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
69-165 |
1.22e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 49.34 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 69 ALG-DKIASSIVAQTAGIPTLPWsgsglrvdwqendfskRILNVPQDLYEkgyvkdvddglkAAEEVGYPVMIKASEGGG 147
Cdd:PRK01372 94 ALAmDKLRTKLVWQAAGLPTPPW----------------IVLTREEDLLA------------AIDKLGLPLVVKPAREGS 145
|
90
....*....|....*...
gi 1907079553 148 GKGIRKVNNADDFPNLFR 165
Cdd:PRK01372 146 SVGVSKVKEEDELQAALE 163
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
131-273 |
1.67e-05 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 46.99 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 131 AEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQ--VQAEVPGSPIFVMRLAKQSRHLEVQIlADQY-GNAISLFGRD 207
Cdd:pfam02655 27 LLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIENvlVQEFIEGEPLSVSLLSDGEKALPLSV-NRQYiDNGGSGFVYA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 208 -CSVQRRH---QKIIEEAPAAIAtpavfehmeqcavKLAKMVGYVSagtVEYLYSqDGSFYFLELNPRLQ 273
Cdd:pfam02655 106 gNVTPSRTelkEEIIELAEEVVE-------------CLPGLRGYVG---VDLVLK-DNEPYVIEVNPRIT 158
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
81-270 |
6.39e-05 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 46.16 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 81 QTAGIPTLPWSGSgLRVDWQENdfskrilnvPQDLYEKgyvkdvddglkAAEEVGYPVMIKASEGGGGKGIRKVNNAD-- 158
Cdd:pfam07478 3 KAAGLPVVPFVTF-TRADWKLN---------PKEWCAQ-----------VEEALGYPVFVKPARLGSSVGVSKVESREel 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 159 -DFPNLFRQVQAEVpgspifVMRLAKQSRHLEVQILADQYGNAISLfGR---DCSVQRRHQKIIEEA-----PAAIaTPA 229
Cdd:pfam07478 62 qAAIEEAFQYDEKV------LVEEGIEGREIECAVLGNEDPEVSPV-GEivpSGGFYDYEAKYIDDSaqivvPADL-EEE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907079553 230 VFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNP 270
Cdd:pfam07478 134 QEEQIQELALKAYKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
109-271 |
1.02e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 47.66 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 109 LNVPQDLYEKgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRqvQAEVPGSPIFVMRL--AKQsr 186
Cdd:PRK12815 681 LGLPHVPGLT--ATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLA--ENASQLYPILIDQFidGKE-- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 187 hLEVQILADqyGNAISLFGrdcsvqrrhqkI---IEEA-----------PAAIATPAVFEHMEQCAVKLAKMVGYVSAGT 252
Cdd:PRK12815 755 -YEVDAISD--GEDVTIPG-----------IiehIEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMN 820
|
170
....*....|....*....
gi 1907079553 253 VEYLYsQDGSFYFLELNPR 271
Cdd:PRK12815 821 IQFVL-ANDEIYVLEVNPR 838
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
63-290 |
3.08e-04 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 44.93 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 63 PSQAMWALGDKIASSIVAQTAGIPTlpwsgsglrvdwqendfskrilnvPQDLYekgyVKDVDDGLKAAEEVGYPVMIKA 142
Cdd:COG0189 87 DPEAIRRARDKLFTLQLLARAGIPV------------------------PPTLV----TRDPDDLRAFLEELGGPVVLKP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 143 SEGGGGKGIRKVNNADDFPNLFRQVQaEVPGSPIFVMRLAKQSRHLEVQILadqygnaisLFGRDC--SVQRRHQK---I 217
Cdd:COG0189 139 LDGSGGRGVFLVEDEDALESILEALT-ELGSEPVLVQEFIPEEDGRDIRVL---------VVGGEPvaAIRRIPAEgefR 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907079553 218 IEEAPAAIATPAVF-EHMEQCAVKLAKMVGYVSAGtVEYLYSQDGsFYFLELNPRLQVEHpcTEMVADVNLPAA 290
Cdd:COG0189 209 TNLARGGRAEPVELtDEERELALRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVTPGFRG--LERATGVDIAEA 278
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
121-271 |
3.12e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 45.53 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 121 VKDVDDGLKAAEEVGYPVMIKASEGG-GGKGIRKVNNADDFPNLFRQVQAE-------VPgspiFVMrlakqsrhlEVQI 192
Cdd:PRK06019 121 VDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEAAWALLGSVpcileefVP----FER---------EVSV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 193 LAdqygnAISLFGRDCS---VQRRHQKII---EEAPAAIaTPAVFEHMEQCAVKLAKMVGYVsaGT--VEYLYSQDGSFY 264
Cdd:PRK06019 188 IV-----ARGRDGEVVFyplVENVHRNGIlrtSIAPARI-SAELQAQAEEIASRIAEELDYV--GVlaVEFFVTGDGELL 259
|
....*..
gi 1907079553 265 FLELNPR 271
Cdd:PRK06019 260 VNEIAPR 266
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
100-151 |
5.86e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.15 E-value: 5.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907079553 100 QENDFSKRILN-----VPqdlyeKGY-VKDVDDGLKAAEEVGYPVMIKASEGGGGKGI 151
Cdd:PRK14016 213 CDKELTKRLLAaagvpVP-----EGRvVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGV 265
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1645-1898 |
6.64e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 44.80 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1645 ITISLVTCRAiGiGAYLVRLGQRTIQV-ENSHLILTGAGALNKVLGREVytSNNQLGGIQImH--NNGVTHSTVCDDFEG 1721
Cdd:PLN02820 209 IALVLGSCTA-G-GAYVPAMADESVIVkGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-HckVSGVSDHFAQDELHA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1722 ------VFTVLHWLSYMPKSVHSSVPLLNSKDPIDRIIEF---VPT--KAPYDPRWMLAGrphptqkgqwlsgFFDYGSF 1790
Cdd:PLN02820 284 laigrnIVKNLHLAAKQGMENTLGSKNPEYKEPLYDVKELrgiVPAdhKQSFDVRSVIAR-------------IVDGSEF 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079553 1791 SEIMQPWAQTVVVGRARLGGIPVGVVAvetrtvelsipadpanldseakiiqqAGQVWFPDSAFKTYQAIKDFNREGLPL 1870
Cdd:PLN02820 351 DEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALKGAHFIELCAQRGIPL 404
|
250 260
....*....|....*....|....*...
gi 1907079553 1871 MVFANWRGFSGGMKDMYDQVLKFGAYIV 1898
Cdd:PLN02820 405 LFLQNITGFMVGSRSEASGIAKAGAKMV 432
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
119-160 |
2.00e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 43.55 E-value: 2.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1907079553 119 GYVKDVDDGLKAAEEVGYPVMIKAS--EGGGGKGIrkVNNADDF 160
Cdd:PRK05294 147 GIAHSMEEALEVAEEIGYPVIIRPSftLGGTGGGI--AYNEEEL 188
|
|
| |
