|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
673-1422 |
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: 1014.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 673 LDNPSKVQQAELHTGSLPRIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLpdpffSSRVKDWVERLMKTLRDPSLPLLEL 752
Cdd:pfam08326 2 LDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLEW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 753 QDIMTSVSGRIPPNVEKSIKKEMAQYASNitsvLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGI 832
Cdd:pfam08326 77 QEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 833 RGHMKAVVMDLLRQYLRVETQFQ--NGHYDKCVFALREENKSDMNTVLNYIFSHAQVTRKNLLVTMLIDQLCGR---DPT 907
Cdd:pfam08326 153 KGHEYSVFASLLEEYYDVEKLFSggNVREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVSN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 908 LTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCIENLQKLILS 979
Cdd:pfam08326 233 VAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELIDS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 980 ETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRMSFSSnl 1059
Cdd:pfam08326 313 KYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSP-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1060 nhyGMTHVASVSD-VLLDNAFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFCDSPPQSPTFPEaghtslydedkvpRDEP 1138
Cdd:pfam08326 391 ---PFKRIASVSDlSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESGESNS-------------SDEP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1139 IHILNVAIKTDCDIEDDS-LAAMFREFTQQNKATLVEHGIRRLTFLVAQKDfrkqvnyevdqrfhREFPKFFTFRARDKF 1217
Cdd:pfam08326 455 INVLNVAIRDAEGSDSDEeLLERLEEILKENKEELLAAGVRRITFIIGRKD--------------GQYPKYFTFRGPDNY 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1218 EEDRIYRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVgtevTDYRFFVRAIIRHSDLVTKEASFEYLQN 1297
Cdd:pfam08326 521 EEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRDDIPTAEYLIS 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1298 EGERLLLEAMDELEVAfNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTPTGK 1377
Cdd:pfam08326 597 EAERLLNDILDALEVA-SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGP 675
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1387222609 1378 AIPIRLFLTNESGYYLDISLYKEVTDSRtAQIMFQAYGdKQGPLH 1422
Cdd:pfam08326 676 PIPLRLVITNVSGYVVKVELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1522-2070 |
0e+00 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 605.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1522 PEYPDGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEgIPRIYVAANSGARIGLAEEIRHMFHVAWVDPEDPYKGY 1601
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1602 KylyLTPQDYKRVSAlnsvhcehvedeGESRYKITDIIGKEEGLGAENLRGSGMIAGESSLAYDEIITISLVTCRAIGIG 1681
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1682 AYLVRLGQRTIQVEN-SHLILTGAGALNKVLGrEVYTSNNQLGGIQIMHNNGVTHSTVCDDFEGVFTVLHWLSYMPKSV- 1759
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAp 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1760 --YSSVPLLNSKDPIDR---VIEFVPT--KAPYDPRWMLAGRphptqkgqwlsgfFDYGSFSEIMQPWAQTVVVGRARLG 1832
Cdd:pfam01039 224 nnREPVPIVPTKDPPDRdapLVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1833 GIPVGVVAVETRtvelsipadpanldseakiiQQAGqVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQ 1912
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1913 VLKFGAYIVDGLRECSQPVMVYIPPqaELRGGSWVVIDPTINPRHMeMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRR 1992
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387222609 1993 VDPvyihlaerlgtpelsvaeRKELESKLKEREEFLLPIYHQVAVQFADLHDTPGRMQEKGVINDILDWKTSRtFFYW 2070
Cdd:pfam01039 427 KDL------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
21-480 |
6.11e-133 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 425.20 E-value: 6.11e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 21 YIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASS 100
Cdd:COG4770 41 HVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 101 IVAQTAGIPTLPWSgsglcvdwhendfskrilnvpqelyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNA 180
Cdd:COG4770 121 KLMKAAGVPVVPGS--------------------------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 181 DDFPNLFRQVQAEVP---GSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEH 256
Cdd:COG4770 175 EELEEAFESARREAKaafGDDrVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRER 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 257 MEQCAVKLARMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRmmygv 335
Cdd:COG4770 255 MGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLpFTQEDIK----- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 336 spwgdapidfensahvpcPRGHVIAARITSENPDEGFKPSSGTVQELNF------------RSNKNVWGYFsvaaagglh 403
Cdd:COG4770 330 ------------------LRGHAIECRINAEDPARGFLPSPGTITRLRPpggpgvrvdsgvYEGYEIPPYY--------- 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387222609 404 efaDSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQAERPD 480
Cdd:COG4770 383 ---DSMIAKLIVWGPDREEAIARMRRALAEFVIEG-VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
21-476 |
1.67e-111 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 363.35 E-value: 1.67e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 21 YIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASS 100
Cdd:PRK08591 41 HVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 101 IVAQTAGIPTLPwsGSglcvdwhendfskrilnvpqelyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNA 180
Cdd:PRK08591 121 ATMKKAGVPVVP--GS------------------------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 181 DDFPNLFRQVQAEVP---GSPIFVM-RLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEH 256
Cdd:PRK08591 175 AELEKAFSMARAEAKaafGNPGVYMeKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 257 MEQCAVKLARMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygv 335
Cdd:PRK08591 255 IGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLsIKQEDIVF---- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 336 spwgdapidfensahvpcpRGHVIAARITSENPDEGFKPSSGTVQelnfrsnknvwGYFsvaAAGGLH------------ 403
Cdd:PRK08591 331 -------------------RGHAIECRINAEDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgyt 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387222609 404 --EFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQA 476
Cdd:PRK08591 378 ipPYYDSMIGKLIVHGETREEAIARMKRALSEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
21-472 |
6.33e-101 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 332.88 E-value: 6.33e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 21 YIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASS 100
Cdd:TIGR00514 41 HVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 101 IVAQTAGIPTLPWSgsglcvdwhendfskrilnvpqelyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNA 180
Cdd:TIGR00514 121 ETMKKAGVPCVPGS--------------------------DGLVEDEEENVRIAKRIGYPVIIKATAGGGGRGMRVVREP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 181 DDFPNLFRQVQAEVP---GSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEH 256
Cdd:TIGR00514 175 DELVKSISMTRAEAKaafGNDgVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 257 MEQCAVKLARMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygv 335
Cdd:TIGR00514 255 MGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPLsLKQEDVVV---- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 336 spwgdapidfensahvpcpRGHVIAARITSENPDEGFKPSSGTVQE------LNFRSNKNVWGYFSVAAagglheFADSQ 409
Cdd:TIGR00514 331 -------------------RGHAIECRINAEDPIKTFLPSPGRITRylppggPGVRWDSHVYSGYTVPP------YYDSM 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387222609 410 FGHCFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAE 472
Cdd:TIGR00514 386 IGKLITYGKTREVAIARMKRALSEFIIDG-IKTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
40-467 |
1.35e-100 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 352.52 E-value: 1.35e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 40 YANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGlc 119
Cdd:PRK12999 64 YLDIDEIIRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGP-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 120 vdwhendfskrilnvpqelyekgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---G 196
Cdd:PRK12999 142 ------------------------IDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 197 SP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLARMVGYVSAGT 275
Cdd:PRK12999 198 NDeVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 276 VEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLyrikdirmmygvspwGDAPIDFENSAHVpCPR 355
Cdd:PRK12999 278 VEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATL---------------HDLEIGIPSQEDI-RLR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 356 GHVIAARITSENPDEGFKPSSGTVQElnFRSNknvwGYFSV------AAAGGlhEFA---DSQFGHCFSWGENREEAISN 426
Cdd:PRK12999 342 GYAIQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVrldggnAFAGA--EITpyyDSLLVKLTAWGRTFEQAVAR 413
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1387222609 427 MVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD 467
Cdd:PRK12999 414 MRRALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFID 453
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
21-475 |
1.95e-100 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 333.49 E-value: 1.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 21 YIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASS 100
Cdd:PRK08654 41 FVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 101 IVAQTAGIPTLPWSGSGlcvdwhendfskrilnvpqelyekgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNA 180
Cdd:PRK08654 121 KLMKKAGVPVLPGTEEG--------------------------IEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 181 DDFPNLF---RQVQAEVPGSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEH 256
Cdd:PRK08654 175 EELEDAIestQSIAQSAFGDStVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRER 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 257 MEQCAVKLARMVGYVSAGTVEYLYSqDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygv 335
Cdd:PRK08654 255 MGEAAVKAAKAINYENAGTVEFLYS-NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELsFKQEDITI---- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 336 spwgdapidfensahvpcpRGHVIAARITSENPDEGFKPSSGTVQelnfrsnknvwGYFSVAAAG-----GLH------E 404
Cdd:PRK08654 330 -------------------RGHAIECRINAEDPLNDFAPSPGKIK-----------RYRSPGGPGvrvdsGVHmgyeipP 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387222609 405 FADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD--RLIAEKVQ 475
Cdd:PRK08654 380 YYDSMISKLIVWGRTREEAIARMRRALYEYVIVG-VKTNIPFHKAVMENENFVRGNLHTHFIEeeTTILEEMK 451
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
20-468 |
6.93e-99 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 326.98 E-value: 6.93e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 20 EYIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIAS 99
Cdd:PRK06111 40 LHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 100 SIVAQTAGIPTLPWSGSGLcvdwhendfskrilnvpqelyekgyvKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNN 179
Cdd:PRK06111 120 RRAMQAAGVPVVPGITTNL--------------------------EDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVET 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 180 ADDFPNLFRQVQAEVP---GSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFE 255
Cdd:PRK06111 174 EQELTKAFESNKKRAAnffGNGeMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 256 HMEQCAVKLARMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmyg 334
Cdd:PRK06111 254 AMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR--- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 335 vspwgdapidfensahvpcpRGHVIAARITSENPDEgFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCF 414
Cdd:PRK06111 331 --------------------SGHAIEVRIYAEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLI 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1387222609 415 SWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDR 468
Cdd:PRK06111 390 AHGETREEAISRLHDALEELKVEG-IKTNIPLLLQVLEDPVFKAGGYTTGFLTK 442
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
40-467 |
1.70e-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: 1.70e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 40 YANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSglc 119
Cdd:COG1038 63 YLDIEEIIRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP--GT--- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 120 vdwhendfskrilnvpqelyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---G 196
Cdd:COG1038 138 ---------------------EGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 197 SP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLARMVGYVSAGT 275
Cdd:COG1038 197 DDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 276 VEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLyrikdirmmygvspwGDAPIDFENSAHVPCpR 355
Cdd:COG1038 277 VEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSL---------------DDPEIGIPSQEDIRL-N 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 356 GHVIAARITSENPDEGFKPSSGTVQElnFRSnknvwgyfsvaaAGGlhefadsqFG------HCFS-------------- 415
Cdd:COG1038 341 GYAIQCRITTEDPANNFMPDTGRITA--YRS------------AGG--------FGirldggNAYTgavitpyydsllvk 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1387222609 416 ---WGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD 467
Cdd:COG1038 399 vtaWGRTFEEAIRKMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFID 452
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
23-476 |
5.87e-92 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 307.45 E-value: 5.87e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 23 KMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIV 102
Cdd:PRK12833 46 RMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 103 AQTAGIPTLPWSgsglcvdwhendfskrilnvpqelyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADD 182
Cdd:PRK12833 126 ARRAGVPTVPGS--------------------------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 183 FPNLFRQVQAEVP---GSP-IFVMRLAKQSRHLEVQILADQYgNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHME 258
Cdd:PRK12833 180 LAAELPLAQREAQaafGDGgVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALC 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 259 QCAVKLARMVGYVSAGTVEYLY-SQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvs 336
Cdd:PRK12833 259 ASAVRLARQVGYRGAGTLEYLFdDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLrFAQGDIAL----- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 337 pwgdapidfensahvpcpRGHVIAARITSENPDEGFKPSSGTVQELNF------RSNKNVWGYFSVAAagglheFADSQF 410
Cdd:PRK12833 334 ------------------RGAALECRINAEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYPGYRVPP------FYDSLL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387222609 411 GHCFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQA 476
Cdd:PRK12833 390 AKLIVHGEDRAAALARAARALRELRIDG-MKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAA 454
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
21-468 |
2.00e-91 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 305.13 E-value: 2.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 21 YIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASS 100
Cdd:PRK08462 43 YLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 101 IVAQTAGIPTLPWSgsglcvdwhendfskrilnvpqelyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNA 180
Cdd:PRK08462 123 EVMKRAGVPVIPGS--------------------------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 181 DDFPNLFRQVQAEVPGS----PIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEH 256
Cdd:PRK08462 177 SDLENLYLAAESEALSAfgdgTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRER 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 257 MEQCAVKLARMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMmygvs 336
Cdd:PRK08462 257 LHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKL----- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 337 pwgdapidfensahvpcpRGHVIAARITSENPdEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQF 410
Cdd:PRK08462 332 ------------------KGHAIECRITAEDP-KKFYPSPGKITKWiapggrNVRMDSHAYAGYVVPP------YYDSMI 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387222609 411 GHCFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDR 468
Cdd:PRK08462 387 GKLIVWGEDRNRAIAKMKRALKEFKVEG-IKTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
21-468 |
1.13e-89 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 300.09 E-value: 1.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 21 YIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASS 100
Cdd:PRK05586 41 HVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 101 IVAQTAGIPTLPWSgsglcvdwhendfskrilnvpqelyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNA 180
Cdd:PRK05586 121 EIMIKAGVPVVPGS--------------------------EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 181 DDFPNLFRQVQAEVPGS----PIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEH 256
Cdd:PRK05586 175 EELIKAFNTAKSEAKAAfgddSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 257 MEQCAVKLARMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygv 335
Cdd:PRK05586 255 MGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLsIKQEDIKI---- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 336 spwgdapidfensahvpcpRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFS 415
Cdd:PRK05586 331 -------------------NGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1387222609 416 WGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDR 468
Cdd:PRK05586 392 YGKDREEAIQKMKRALGEFIIEG-VNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
18-469 |
1.77e-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: 307.73 E-value: 1.77e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 18 YDEYIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKI 97
Cdd:TIGR02712 37 ASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKKTGAQAIHPGYGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 98 ASSIVAQTAGIPTLPwsGSGLcvdwhendfskrilnvpqelyekgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKV 177
Cdd:TIGR02712 117 TARELAEAAGVPLLP--GTGL-------------------------LSSLDEALEAAKEIGYPVMLKSTAGGGGIGMQKC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 178 NNADDFPNLF----RQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAV 253
Cdd:TIGR02712 170 DSAAELAEAFetvkRLGESFFGDAGVFLERFVENARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEETPAPNLPPET 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 254 FEHMEQCAVKLARMVGYVSAGTVEYLY-SQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAmgiplyrikdirmm 332
Cdd:TIGR02712 250 RQALLAAAERLGEAVNYRSAGTVEFIYdEARDEFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIA-------------- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 333 ygvspwGDAPIDFENSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYfsVAAAGGLHEFADSQFGH 412
Cdd:TIGR02712 316 ------AGELPDFASLNISLTPRGAAIEARVYAENPAKNFQPSPGLLTDVQFPDDVRVDTW--VETGTEVSPEYDPMLAK 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387222609 413 CFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRL 469
Cdd:TIGR02712 388 IIVHGSDREDAILKLHQALAETRVYG-IETNLDYLRSILSSETFRSAQVSTRTLNSF 443
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
40-467 |
1.68e-83 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 283.15 E-value: 1.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 40 YANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglc 119
Cdd:PRK07178 59 YLNPRRLVNLAVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGS----- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 120 vdwhendfskrilnvpqelyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---G 196
Cdd:PRK07178 134 ---------------------EGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 197 SP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLARMVGYVSAGT 275
Cdd:PRK07178 193 SAeVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 276 VEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdapidfensahvpcp 354
Cdd:PRK07178 273 VEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH----------------------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 355 RGHVIAARITSENPDEGFKPSSGTVQElnfrsnknvwgYFSVAAAG---------GLH--EFADSQFGHCFSWGENREEA 423
Cdd:PRK07178 330 RGFALQFRINAEDPKNDFLPSFGKITR-----------YYAPGGPGvrtdtaiytGYTipPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1387222609 424 ISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD 467
Cdd:PRK07178 399 LDRGRRALDDMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVE 441
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
40-467 |
7.69e-83 |
|
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: 298.66 E-value: 7.69e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 40 YANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglc 119
Cdd:TIGR01235 60 YLSIDEIIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 120 vdwhendfskrilnvpqelyeKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGS-- 197
Cdd:TIGR01235 135 ---------------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfg 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 198 --PIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLARMVGYVSAGT 275
Cdd:TIGR01235 194 ndEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 276 VEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIK-------DIRMmygvspwgdapidfens 348
Cdd:TIGR01235 274 VEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLPTPQlgvpnqeDIRT----------------- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 349 ahvpcpRGHVIAARITSENPDEGFKPSSGTVQElnFRSNknvwGYFSVAAAGG-------LHEFADSQFGHCFSWGENRE 421
Cdd:TIGR01235 337 ------NGYAIQCRVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPE 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1387222609 422 EAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLD 467
Cdd:TIGR01235 405 EAAAKMDRALREFRIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
21-490 |
1.17e-66 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 234.71 E-value: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 21 YIKMADHYVPVPGGPNNNnYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASS 100
Cdd:PRK08463 41 HVKIADEAYRIGTDPIKG-YLDVKRIVEIAKACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 101 IVAQTAGIPTLPWSgsglcvdwhendfskrilnvpqelyEKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNA 180
Cdd:PRK08463 120 YLMKKNGIPIVPGT-------------------------EKLNSESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 181 DDFPNLF----RQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEH 256
Cdd:PRK08463 175 EDLENAFesckREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 257 MEQCAVKLARMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMG-IPLYRIKDIRmmygv 335
Cdd:PRK08463 255 MGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGeILDLEQSDIK----- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 336 spwgdapidfensahvpcPRGHVIAARITSENPDEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQ 409
Cdd:PRK08463 330 ------------------PRGFAIEARITAENVWKNFIPSPGKITEYypalgpSVRVDSHIYKDYTIPP------YYDSM 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 410 FGHCFSWGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQLNRIDTGWLDRLIAEKVQA------ERPDTML 483
Cdd:PRK08463 386 LAKLIVKATSYDLAVNKLERALKEFVIDG-IRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKtedrhqENKEEVI 464
|
....*..
gi 1387222609 484 GVVCGAL 490
Cdd:PRK08463 465 AAIAAAL 471
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
132-323 |
2.09e-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: 212.55 E-value: 2.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 132 LNVPQELYEKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSP----IFVMRLAKQ 207
Cdd:pfam02786 12 AGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 208 SRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPAAIATPAVFEHMEQCAVKLARMVGYVSAGTVEYLYSQD-GSF 286
Cdd:pfam02786 92 PKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsGEY 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1387222609 287 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL 323
Cdd:pfam02786 172 YFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
43-322 |
1.88e-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: 160.04 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 43 VELILDIAKRIPVQAVWAGWGHASEnpKLPELLLKNGIAfmGPPSQAMWALGDKIASSIVAQTAGIPTlPWSGSglcvdw 122
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVE--TAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFAL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 123 hendfskrilnvpqelyekgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEV----PGSP 198
Cdd:COG0439 75 ---------------------VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNGE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 199 IFVMRLAkQSRHLEVQILADQyGNAISlfgrdCSVQRRHQK---IIE---EAPAAIaTPAVFEHMEQCAVKLARMVGYV- 271
Cdd:COG0439 134 VLVEEFL-EGREYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPL-PEELRAEIGELVARALRALGYRr 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1387222609 272 SAGTVEYLYSQDGSFYFLELNPRLQVEH--PCTEMVADVNLPAAQLQIAMGIP 322
Cdd:COG0439 206 GAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
361-467 |
2.99e-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: 2.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 361 ARITSENPDEGFKPSSGTVQELNFRSNKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 438
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 1387222609 439 dFRTTVEYLIKLLETESFQLNRIDTGWLD 467
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
361-468 |
1.25e-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: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 361 ARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 440
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*...
gi 1387222609 441 RTTVEYLIKLLETESFQLNRIDTGWLDR 468
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
20-89 |
3.00e-26 |
|
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: 104.88 E-value: 3.00e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 20 EYIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQA 89
Cdd:pfam00289 39 LHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1509-1840 |
4.70e-19 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 93.17 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1509 EIGM-VAWKMTLKSPEYP-----------DGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVAANSGAR 1576
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPgdgvvtgigtvDGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1577 IGLAEEIRHMFhvawvdpedpykgykylyltpqdykrvsalnsvhcehvedeGESRYKitdiigkeeglgaeNLRGSGMI 1656
Cdd:COG4799 131 LQEGVESFAGY-----------------------------------------GRIFYR--------------NARSSGGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1657 AgesslaydeiiTISLVTCRAIGIGAYLVRLGQRTIQVE-NSHLILTGAGALNKVLGREVytSNNQLGGIQiMHN--NGV 1733
Cdd:COG4799 156 P-----------QISVIMGPCAAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvSGV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1734 THSTVCDDFEGVFTVLHWLSYMPKSVYSSVPLLNSKDP---IDRVIEFVPT--KAPYDPRWMLAGrphptqkgqwlsgFF 1808
Cdd:COG4799 222 ADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPPardPEELYGIVPEdpRKPYDMREVIAR-------------LV 288
|
330 340 350
....*....|....*....|....*....|..
gi 1387222609 1809 DYGSFSEIMQPWAQTVVVGRARLGGIPVGVVA 1840
Cdd:COG4799 289 DGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA 320
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
606-671 |
3.54e-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: 77.64 E-value: 3.54e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387222609 606 VLRSPSAGKLI-----QYIVEDGGHVFAGQCYAEIEVMKMVMTLTAAESGCIHYVKRP-GAALDPGCVIAKM 671
Cdd:pfam00364 2 EIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
606-671 |
8.55e-15 |
|
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: 70.91 E-value: 8.55e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387222609 606 VLRSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAAESGCIHYVK-RPGAALDPGCVIAKM 671
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
25-330 |
4.62e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 76.51 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 25 ADHYVPVPGgPNNNNYANVELILDIAKRIPVQAVWA---GWGHA-SEN-PKLPElllknGIAFMGPPSQAMWALGDKIAS 99
Cdd:COG3919 48 VDEVVVVPD-PGDDPEAFVDALLELAERHGPDVLIPtgdEYVELlSRHrDELEE-----HYRLPYPDADLLDRLLDKERF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 100 SIVAQTAGIPtlpwsgsglcvdwhendfskrilnVPQELYekgyVKDVDDGLKAAEEVGYPVMIKASEG--------GGG 171
Cdd:COG3919 122 YELAEELGVP------------------------VPKTVV----LDSADDLDALAEDLGFPVVVKPADSvgydelsfPGK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 172 KGIRKVNNADDFPNLFRQ---------VQAEVPGSpifvmrlakQSRHLEVQILADQYGNAISLFGrdcsvqrrHQKIIE 242
Cdd:COG3919 174 KKVFYVDDREELLALLRRiaaagyeliVQEYIPGD---------DGEMRGLTAYVDRDGEVVATFT--------GRKLRH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 243 eAPAAIATPAVFEH-----MEQCAVKLARMVGYVSAGTVEYLY-SQDGSFYFLELNPRLQVEHPCTEmVADVNLPAAQLQ 316
Cdd:COG3919 237 -YPPAGGNSAARESvddpeLEEAARRLLEALGYHGFANVEFKRdPRDGEYKLIEINPRFWRSLYLAT-AAGVNFPYLLYD 314
|
330
....*....|....
gi 1387222609 317 IAMGIPLYRIKDIR 330
Cdd:COG3919 315 DAVGRPLEPVPAYR 328
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
127-323 |
5.21e-09 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 61.94 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 127 FSKRI--LNVPQElyEKGYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRL 204
Cdd:TIGR01369 673 FSELLdeLGIPQP--KWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKY 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 205 AKQSRHLEVQILADqyGNAISLFGrdcsvQRRHqkiIEEA-----------PAAIATPAVFEHMEQCAVKLARMVGYVSA 273
Cdd:TIGR01369 751 LEDAVEVDVDAVSD--GEEVLIPG-----IMEH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGL 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1387222609 274 GTVEYLYSqDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL 323
Cdd:TIGR01369 821 MNIQFAVK-DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
142-294 |
1.33e-08 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 60.56 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 142 GYVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDfpnLFRQVQAEV---PGSPIFVMRLAKQSRHLEVQILAD 218
Cdd:PLN02735 721 GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDK---LKTYLETAVevdPERPVLVDKYLSDATEIDVDALAD 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 219 QYGNAISlfgrdCSVQRRhqkiIEEA-----------PAAIATPAVFEHMEQCAVKLARMVGYVSAGTVEYLYSQDGSFY 287
Cdd:PLN02735 798 SEGNVVI-----GGIMEH----IEQAgvhsgdsacslPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVY 868
|
....*..
gi 1387222609 288 FLELNPR 294
Cdd:PLN02735 869 IIEANPR 875
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
73-293 |
3.23e-08 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 57.42 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 73 ELLlknGIAFMGPPSQAMwALG-DKIASSIVAQTAGIPTLPWsgsglcvdwhendfskrilnvpqELYEKGYVKDVDDgl 151
Cdd:COG1181 76 ELL---GIPYTGSGVLAS-ALAmDKALTKRVLAAAGLPTPPY-----------------------VVLRRGELADLEA-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 152 kAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNlfrqvqaevpgspifVMRLAKQSRHlevQILADQYgnaISlfGRD- 230
Cdd:COG1181 127 -IEEELGLPLFVKPAREGSSVGVSKVKNAEELAA---------------ALEEAFKYDD---KVLVEEF---ID--GREv 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 231 -CSV-QRRHQK---IIE----------EA-----------PAAIaTPAVFEHMEQCAVKLARMV---GYvsaGTVEYLYS 281
Cdd:COG1181 183 tVGVlGNGGPRalpPIEivpengfydyEAkytdggteyicPARL-PEELEERIQELALKAFRALgcrGY---ARVDFRLD 258
|
250
....*....|..
gi 1387222609 282 QDGSFYFLELNP 293
Cdd:COG1181 259 EDGEPYLLEVNT 270
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
132-295 |
6.46e-08 |
|
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: 58.09 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 132 LNVPQElyEKGYVKDVDDGLKAAEEVGYPVMIKASE--GGGGKGIrkVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSR 209
Cdd:TIGR01369 138 IGEPVP--ESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSASPINQVLVEKSLAGWK 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 210 HLEVQILADQYGNAISLfgrdCSVQR-----RHQ-KIIEEAPAAIATPAVFEHMEQCAVKLARMVGYVSAGTVEY-LYSQ 282
Cdd:TIGR01369 214 EIEYEVMRDSNDNCITV----CNMENfdpmgVHTgDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFaLNPD 289
|
170
....*....|...
gi 1387222609 283 DGSFYFLELNPRL 295
Cdd:TIGR01369 290 SGRYYVIEVNPRV 302
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
127-294 |
9.18e-08 |
|
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: 57.20 E-value: 9.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 127 FSKRI--LNVPQElyEKGYVKDVDDGLKAAEEVGYPVMIKASE--GGGGKGIrkVNNADDFPNLFRQVQAEVPGSPIFVM 202
Cdd:COG0458 118 FKELLdkLGIPQP--KSGTATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLID 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 203 RLAKQSRHLEVQILADQYGNAISLfgrdCSVQrrHqkiIEEA-----------PAAIATPAVFEHMEQCAVKLARMVGYV 271
Cdd:COG0458 194 ESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVV 264
|
170 180
....*....|....*....|...
gi 1387222609 272 SAGTVEYLYsQDGSFYFLELNPR 294
Cdd:COG0458 265 GLCNIQFAV-DDGRVYVIEVNPR 286
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
143-294 |
1.74e-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: 53.03 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 143 YVKDVDDGLKAAEEVGYPVMIKASEGG-GGKGIRKVNNADDFPnlfrQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYG 221
Cdd:pfam02222 12 AAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLP----QAWEELGDGPVIVEEFVPFDRELSVLVVRSVDG 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387222609 222 NAISlfgrdCS-VQRRHQK---IIEEAPAAIaTPAVFEHMEQCAVKLARMVGYVSAGTVEYLYSQDGSFYFLELNPR 294
Cdd:pfam02222 88 ETAF-----YPvVETIQEDgicRLSVAPARV-PQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLINELAPR 158
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
153-321 |
1.04e-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: 53.38 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 153 AAEEVGYPVMIKASEGGGGKGIRKVNNAD-DFPNLFrqVQAEVPGSPIfvmrlakqSrhleVQILADqygnaislfGRDC 231
Cdd:COG2232 133 EPPPDPGPWLVKPIGGAGGWHIRPADSEApPAPGRY--FQRYVEGTPA--------S----VLFLAD---------GSDA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 232 SVQRRHQKIIEEAPAA------IATPAVFEH-----MEQCAVKLARMVGYVSAGTVEYLYSQDGsFYFLELNPRLQVEHP 300
Cdd:COG2232 190 RVLGFNRQLIGPAGERpfryggNIGPLALPPalaeeMRAIAEALVAALGLVGLNGVDFILDGDG-PYVLEVNPRPQASLD 268
|
170 180
....*....|....*....|.
gi 1387222609 301 CTEMVADVNLPAAQLQIAMGI 321
Cdd:COG2232 269 LYEDATGGNLFDAHLRACRGE 289
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
127-294 |
7.19e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 50.27 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 127 FSKRILNVPQElYEKGYVKDVDDGLkAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQ-----VQAEVPGSPIfv 201
Cdd:PRK12767 119 LKENGIPTPKS-YLPESLEDFKAAL-AKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYvpnliIQEFIEGQEY-- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 202 mrlakqsrhlEVQILADQYGNAISLFGRdcsvqRRHQKIIEEAPAAIAT--PAVFEHMEQCAVKLarmvGYVSAGTVEYL 279
Cdd:PRK12767 195 ----------TVDVLCDLNGEVISIVPR-----KRIEVRAGETSKGVTVkdPELFKLAERLAEAL----GARGPLNIQCF 255
|
170
....*....|....*
gi 1387222609 280 YSqDGSFYFLELNPR 294
Cdd:PRK12767 256 VT-DGEPYLFEINPR 269
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
92-188 |
1.50e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 49.34 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 92 ALG-DKIASSIVAQTAGIPTLPWsgsglcvdwhendfskRILNvpqelyekgyvkDVDDGLKAAEEVGYPVMIKASEGGG 170
Cdd:PRK01372 94 ALAmDKLRTKLVWQAAGLPTPPW----------------IVLT------------REEDLLAAIDKLGLPLVVKPAREGS 145
|
90
....*....|....*...
gi 1387222609 171 GKGIRKVNNADDFPNLFR 188
Cdd:PRK01372 146 SVGVSKVKEEDELQAALE 163
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
154-296 |
2.18e-05 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 46.61 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 154 AEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQ--VQAEVPGSPIFVMRLAKQSRHLEVQIlADQY-GNAISLFGRD 230
Cdd:pfam02655 27 LLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIENvlVQEFIEGEPLSVSLLSDGEKALPLSV-NRQYiDNGGSGFVYA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 231 -CSVQRRH---QKIIEEAPAAIAtpavfehmeqcavKLARMVGYVSagtVEYLYSqDGSFYFLELNPRLQ 296
Cdd:pfam02655 106 gNVTPSRTelkEEIIELAEEVVE-------------CLPGLRGYVG---VDLVLK-DNEPYVIEVNPRIT 158
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
132-294 |
1.40e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 47.27 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 132 LNVPQELYEKgyVKDVDDGLKAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRqvQAEVPGSPIFVMRL--AKQsr 209
Cdd:PRK12815 681 LGLPHVPGLT--ATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLA--ENASQLYPILIDQFidGKE-- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 210 hLEVQILADqyGNAISLFGrdcsvqrrhqkI---IEEA-----------PAAIATPAVFEHMEQCAVKLARMVGYVSAGT 275
Cdd:PRK12815 755 -YEVDAISD--GEDVTIPG-----------IiehIEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMN 820
|
170
....*....|....*....
gi 1387222609 276 VEYLYsQDGSFYFLELNPR 294
Cdd:PRK12815 821 IQFVL-ANDEIYVLEVNPR 838
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
104-293 |
1.89e-04 |
|
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: 45.00 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 104 QTAGIPTLPWSGSgLCVDWHENdfskrilnvPQELYEKgyvkdvddglkAAEEVGYPVMIKASEGGGGKGIRKVNNAD-- 181
Cdd:pfam07478 3 KAAGLPVVPFVTF-TRADWKLN---------PKEWCAQ-----------VEEALGYPVFVKPARLGSSVGVSKVESREel 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 182 -DFPNLFRQVQAEVpgspifVMRLAKQSRHLEVQILADQYGNAISLfGR---DCSVQRRHQKIIEEA-----PAAIaTPA 252
Cdd:pfam07478 62 qAAIEEAFQYDEKV------LVEEGIEGREIECAVLGNEDPEVSPV-GEivpSGGFYDYEAKYIDDSaqivvPADL-EEE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1387222609 253 VFEHMEQCAVKLARMVGYVSAGTVEYLYSQDGSFYFLELNP 293
Cdd:pfam07478 134 QEEQIQELALKAYKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1659-1921 |
2.42e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 46.34 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1659 ESSLAYDEIITISLVTCRAIGIGAYLVRLGQRTIQV-ENSHLILTGAGALNKVLGREVytSNNQLGGIQImH--NNGVTH 1735
Cdd:PLN02820 198 QARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVkGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-HckVSGVSD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1736 STVCDDFEG------VFTVLHWLSYMPKSVYSSVPLLNSKDPIDRVIEF---VPT--KAPYDPRWMLAGrphptqkgqwl 1804
Cdd:PLN02820 275 HFAQDELHAlaigrnIVKNLHLAAKQGMENTLGSKNPEYKEPLYDVKELrgiVPAdhKQSFDVRSVIAR----------- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 1805 sgFFDYGSFSEIMQPWAQTVVVGRARLGGIPVGVVAvetrtvelsipadpanldseakiiqqAGQVWFPDSAFKTYQAIK 1884
Cdd:PLN02820 344 --IVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALKGAHFIE 395
|
250 260 270
....*....|....*....|....*....|....*..
gi 1387222609 1885 DFNREGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIV 1921
Cdd:PLN02820 396 LCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMV 432
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
86-313 |
2.80e-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: 45.32 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 86 PSQAMWALGDKIASSIVAQTAGIPTlpwsgsglcvdwhendfskrilnvPQELYekgyVKDVDDGLKAAEEVGYPVMIKA 165
Cdd:COG0189 87 DPEAIRRARDKLFTLQLLARAGIPV------------------------PPTLV----TRDPDDLRAFLEELGGPVVLKP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 166 SEGGGGKGIRKVNNADDFPNLFRQVQaEVPGSPIFVMRLAKQSRHLEVQILadqygnaisLFGRDC--SVQRRHQK---I 240
Cdd:COG0189 139 LDGSGGRGVFLVEDEDALESILEALT-ELGSEPVLVQEFIPEEDGRDIRVL---------VVGGEPvaAIRRIPAEgefR 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387222609 241 IEEAPAAIATPAVF-EHMEQCAVKLARMVGYVSAGtVEYLYSQDGsFYFLELNPRLQVEHpcTEMVADVNLPAA 313
Cdd:COG0189 209 TNLARGGRAEPVELtDEERELALRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVTPGFRG--LERATGVDIAEA 278
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
144-294 |
4.50e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 44.76 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 144 VKDVDDGLKAAEEVGYPVMIKASEGG-GGKGIRKVNNADDFPNLFRQVQAE-------VPgspiFVMrlakqsrhlEVQI 215
Cdd:PRK06019 121 VDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEAAWALLGSVpcileefVP----FER---------EVSV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387222609 216 LAdqygnAISLFGRDCS---VQRRHQKII---EEAPAAIaTPAVFEHMEQCAVKLARMVGYVsaGT--VEYLYSQDGSFY 287
Cdd:PRK06019 188 IV-----ARGRDGEVVFyplVENVHRNGIlrtSIAPARI-SAELQAQAEEIASRIAEELDYV--GVlaVEFFVTGDGELL 259
|
....*..
gi 1387222609 288 FLELNPR 294
Cdd:PRK06019 260 VNEIAPR 266
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
126-174 |
6.61e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 44.76 E-value: 6.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1387222609 126 DFSKRILN-----VPqelyeKGY-VKDVDDGLKAAEEVGYPVMIKASEGGGGKGI 174
Cdd:PRK14016 216 ELTKRLLAaagvpVP-----EGRvVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGV 265
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
142-183 |
1.92e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 43.55 E-value: 1.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1387222609 142 GYVKDVDDGLKAAEEVGYPVMIKAS--EGGGGKGIrkVNNADDF 183
Cdd:PRK05294 147 GIAHSMEEALEVAEEIGYPVIIRPSftLGGTGGGI--AYNEEEL 188
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
609-672 |
7.46e-03 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 37.30 E-value: 7.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387222609 609 SPSAgkliQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAAESG-CIHYVKRPGAALDPGCVIAKMQ 672
Cdd:PRK07051 19 SPDA----PPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGrVVEFLVEDGEPVEAGQVLARIE 79
|
|
|