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Conserved domains on  [gi|1387222609|ref|XP_024835375|]
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acetyl-CoA carboxylase 1 isoform X9 [Bos taurus]

Protein Classification

acetyl-CoA carboxylase( domain architecture ID 18109860)

acetyl-CoA carboxylase (ACC) carries out three functions: biotin carboxyl carrier protein, biotin carboxylase, and carboxyltransferase; it is involved in the synthesis of very-long-chain fatty acid synthesis which is required to maintain a functional nuclear envelope

Graphical summary

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List of domain hits

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 super family cl44129
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];


The actual alignment was detected with superfamily member COG4770:

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
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
 
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
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
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
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
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
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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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