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Conserved domains on  [gi|1167497201|ref|WP_080010575|]
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MULTISPECIES: acyl-CoA carboxylase subunit beta [Bacillus]

Protein Classification

acyl-CoA carboxylase subunit beta( domain architecture ID 11469175)

acyl-CoA carboxylase subunit beta, such as propionyl-CoA carboxylase subunit beta, which is the catalytic carboxyltransferase subunit of the enzyme that catalyzes the carboxylation of propionyl-CoA to form methylmalonyl-CoA

CATH:  3.90.226.10
Gene Ontology:  GO:0016874|GO:0006633|GO:0009317|GO:0003989
PubMed:  8102604
SCOP:  4000456

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
1-505 0e+00

Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];


:

Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 803.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201   1 MNEHMDHLYTKRKQAEEGGGREKLAQQRQKGKLTARERIIFLLDQDSFIELHPFMESQVLTREQRMLGDGVVTGYGTIDG 80
Cdd:COG4799     2 MRALLAELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGSFLELGALAGHRMYDDDDRVPGDGVVTGIGTVDG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  81 RSVYVFAQDFTVFGGALGETHARKICALMDLAAKNKAPIIGLNDSGGARIQEGVVSLDGYGHIFYRNVLYSGVIPQISVI 160
Cdd:COG4799    82 RPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGGIPQISVI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 161 LGPCAGGAVYSPALTDFIFMAEQTGRMFITGPKVIEKVTGEQVDAGSLGGAGIHNAVSGNAHFSGHTEKEVLTGVRKLLS 240
Cdd:COG4799   162 MGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 241 YLPLNGRttEPKPEKEASRPL-----LNHLVPADTTKPYDVRKVIRELADPQSFFEIQPFFAKNIVIGFARLGEKAIGIV 315
Cdd:COG4799   242 YLPSNNL--EDPPRAEPAPPArdpeeLYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 316 ASQPKHLAGSLTIDAADKAARFIRFCDAFDIPLLTVEDVPGFLPGIQQEHNGIIRHGAKLLFAYAEATVPKVTLIIRKAY 395
Cdd:COG4799   320 ANQPMVLAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAY 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 396 GGAYVAMNSKAIGADLVFAWPNAEIAVMGPEGAASILYEKEIKASADPQKTKREKTAEYKKQnAGPYKAAACGMVDDIIL 475
Cdd:COG4799   400 GAGYYAMCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAAAEDPEALRAELIAEYEEQ-ANPYYAAARGWIDDVID 478

                         490       500       510
                  ....*....|....*....|....*....|
gi 1167497201 476 PEESRGKLIQAFHMLAHKTEERPKKKHGNI 505
Cdd:COG4799   479 PRDTRRVLARALEAAANKPEERPPKKHGVI 508
 
Name Accession Description Interval E-value
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
1-505 0e+00

Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 803.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201   1 MNEHMDHLYTKRKQAEEGGGREKLAQQRQKGKLTARERIIFLLDQDSFIELHPFMESQVLTREQRMLGDGVVTGYGTIDG 80
Cdd:COG4799     2 MRALLAELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGSFLELGALAGHRMYDDDDRVPGDGVVTGIGTVDG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  81 RSVYVFAQDFTVFGGALGETHARKICALMDLAAKNKAPIIGLNDSGGARIQEGVVSLDGYGHIFYRNVLYSGVIPQISVI 160
Cdd:COG4799    82 RPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGGIPQISVI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 161 LGPCAGGAVYSPALTDFIFMAEQTGRMFITGPKVIEKVTGEQVDAGSLGGAGIHNAVSGNAHFSGHTEKEVLTGVRKLLS 240
Cdd:COG4799   162 MGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 241 YLPLNGRttEPKPEKEASRPL-----LNHLVPADTTKPYDVRKVIRELADPQSFFEIQPFFAKNIVIGFARLGEKAIGIV 315
Cdd:COG4799   242 YLPSNNL--EDPPRAEPAPPArdpeeLYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 316 ASQPKHLAGSLTIDAADKAARFIRFCDAFDIPLLTVEDVPGFLPGIQQEHNGIIRHGAKLLFAYAEATVPKVTLIIRKAY 395
Cdd:COG4799   320 ANQPMVLAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAY 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 396 GGAYVAMNSKAIGADLVFAWPNAEIAVMGPEGAASILYEKEIKASADPQKTKREKTAEYKKQnAGPYKAAACGMVDDIIL 475
Cdd:COG4799   400 GAGYYAMCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAAAEDPEALRAELIAEYEEQ-ANPYYAAARGWIDDVID 478

                         490       500       510
                  ....*....|....*....|....*....|
gi 1167497201 476 PEESRGKLIQAFHMLAHKTEERPKKKHGNI 505
Cdd:COG4799   479 PRDTRRVLARALEAAANKPEERPPKKHGVI 508
mmdA TIGR01117
methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA ...
 3-507 0e+00

methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA decarboxylase aplha subunit in archaea and bacteria. Metylmalonyl-CoA decarboxylase Na+ pump is a representative of a class of Na+ transport decarboxylases that couples the energy derived by decarboxylation of carboxylic acid substrates to drive the extrusion of Na+ ion across the membrane. [Energy metabolism, ATP-proton motive force interconversion, Energy metabolism, Fermentation, Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130187  Cd Length: 512  Bit Score: 675.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201   3 EHMDHLYTKRKQAEEGGGREKLAQQRQKGKLTARERIIFLLDQDSFIELHPFMESQVLT---REQRMLGDGVVTGYGTID 79
Cdd:TIGR01117   1 EKIEELHEKKEKIKQGGGEKRIEKQHAQGKMTARERLALLFDPGSFVEIDQFVKHRCTNfgmDKKELPAEGVVTGYGTID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  80 GRSVYVFAQDFTVFGGALGETHARKICALMDLAAKNKAPIIGLNDSGGARIQEGVVSLDGYGHIFYRNVLYSGVIPQISV 159
Cdd:TIGR01117  81 GRLVYAFAQDFTVMGGSLGEMHAAKIVKIMDLAMKMGAPVVGLNDSGGARIQEAVDALKGYGDIFYRNTIASGVVPQISA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 160 ILGPCAGGAVYSPALTDFIFMAEQTGRMFITGPKVIEKVTGEQVDAGSLGGAGIHNAVSGNAHFSGHTEKEVLTGVRKLL 239
Cdd:TIGR01117 161 IMGPCAGGAVYSPALTDFIYMVDNTSQMFITGPQVIKTVTGEEVTAEQLGGAMAHNSVSGVAHFIAEDDDDCIMLIRRLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 240 SYLPLNGRTTEP--KPEKEASR--PLLNHLVPADTTKPYDVRKVIRELADPQSFFEIQPFFAKNIVIGFARLGEKAIGIV 315
Cdd:TIGR01117 241 SFLPSNNMEKAPlvKTGDDPTRetPELYDLLPDNPNKPYDMRDVITAIVDNGDYLEVQPYYAPNIITCFARINGQSVGII 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 316 ASQPKHLAGSLTIDAADKAARFIRFCDAFDIPLLTVEDVPGFLPGIQQEHNGIIRHGAKLLFAYAEATVPKVTLIIRKAY 395
Cdd:TIGR01117 321 ANQPKVMAGCLDIDSSDKIARFIRFCDAFNIPIVTFVDVPGFLPGVNQEYGGIIRHGAKVLYAYSEATVPKVTIITRKAY 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 396 GGAYVAMNSKAIGADLVFAWPNAEIAVMGPEGAASILYEKEIKASADPQKTKREKTAEYKKQNAGPYKAAACGMVDDIIL 475
Cdd:TIGR01117 401 GGAYLAMCSKHLGADQVYAWPTAEIAVMGPAGAANIIFRKDIKEAKDPAATRKQKIAEYREEFANPYKAAARGYVDDVIE 480

                         490       500       510
                  ....*....|....*....|....*....|..
gi 1167497201 476 PEESRGKLIQAFHMLAHKTEERPKKKHGNIPL 507
Cdd:TIGR01117 481 PKQTRPKIVNALAMLESKREKLPPKKHGNIPL 512
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 26-505 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: 673.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  26 QQRQKGKLTARERIIFLLDQDSFIELHPFMESQVLTRE-QRMLGDGVVTGYGTIDGRSVYVFAQDFTVFGGALGETHARK 104
Cdd:pfam01039   1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGrKRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 105 ICALMDLAAKNKAPIIGLNDSGGARIQEGVVSLDGYGHIFYRNVLYSGVIPQISVILGPCAGGAVYSPALTDFIFMAEQT 184
Cdd:pfam01039  81 ILRAMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGGAYLPALGDFVIMVEGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 185 GRMFITGPKVIEKVTGEQVDAGSLGGAGIHNAVSGNAHFSGHTEKEVLTGVRKLLSYLPL---NGRTTEPKPEKEAS--- 258
Cdd:pfam01039 161 SPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKpapNNREPVPIVPTKDPpdr 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 259 RPLLNHLVPADTTKPYDVRKVIRELADPQSFFEIQPFFAKNIVIGFARLGEKAIGIVASQPKHLAGSLTIDAADKAARFI 338
Cdd:pfam01039 241 DAPLVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQPRVGAGVLFPDSADKAARFI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 339 RFCDAFDIPLLTVEDVPGFLPGIQQEHNGIIRHGAKLLFAYAEATVPKVTLIIRKAYGGAYVAMNSKAIGADLVFAWPNA 418
Cdd:pfam01039 321 RDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDSKINGADINFAWPTA 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 419 EIAVMGPEGAASILYEKEIKAS----ADPQKTKREKTAEYKKQNAGPYKAAACGMVDDIILPEESRGKLIQAFHMLAHKT 494
Cdd:pfam01039 401 RIAVMGPEGAVEIKFRKEKAAAemrgKDLAATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKP 480

                         490
                  ....*....|.
gi 1167497201 495 EERPKKKHGNI 505
Cdd:pfam01039 481 RFFPWRKHGNI 491
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 1-480 7.06e-92

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 290.94  E-value: 7.06e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201   1 MNEHMDHLYTKRKQAEEGGGREKLAQQRQKGKLTARERIIFLLDQDS-FIELHPFMESQVLtrEQRMLGDGVVTGYGTID 79
Cdd:PLN02820   50 MEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSpFLELSQLAGHELY--GEDLPSGGIVTGIGPVH 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  80 GRSVYVFAQDFTVFGGALGETHARKICALMDLAAKNKAPIIGLNDSGGA---RIQEGVVSLDGYGHIFY-RNVLYSGVIP 155
Cdd:PLN02820  128 GRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGAnlpRQAEVFPDRDHFGRIFYnQARMSSAGIP 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 156 QISVILGPCAGGAVYSPALTDFIFMAEQTGRMFITGPKVIEKVTGEQVDAGSLGGAGIHNAVSGNAHFSGHTEKEVLTGV 235
Cdd:PLN02820  208 QIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSDHFAQDELHALAIG 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 236 RKLLSYLPLNGRTTEPKPEKEAS----RPL-----LNHLVPADTTKPYDVRKVIRELADPQSFFEIQPFFAKNIVIGFAR 306
Cdd:PLN02820  288 RNIVKNLHLAAKQGMENTLGSKNpeykEPLydvkeLRGIVPADHKQSFDVRSVIARIVDGSEFDEFKKNYGTTLVTGFAR 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 307 LGEKAIGIVASQpkhlaGSLTIDAADKAARFIRFCDAFDIPLLTVEDVPGFLPGIQQEHNGIIRHGAKLLFAYAEATVPK 386
Cdd:PLN02820  368 IYGQPVGIIGNN-----GILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMVMAVACAKVPK 442

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 387 VTLIIRKAYGGAYVAMNSKAIGADLVFAWPNAEIAVMGPEGAASILYEKE--------IKASADPQKTKREKTAEYKKQN 458
Cdd:PLN02820  443 ITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQIErenkkrqgIQWSKEEEEAFKAKTVEAYERE 522

                         490       500
                  ....*....|....*....|..
gi 1167497201 459 AGPYKAAACGMVDDIILPEESR 480
Cdd:PLN02820  523 ANPYYSTARLWDDGVIDPADTR 544
 
Name Accession Description Interval E-value
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
1-505 0e+00

Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 803.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201   1 MNEHMDHLYTKRKQAEEGGGREKLAQQRQKGKLTARERIIFLLDQDSFIELHPFMESQVLTREQRMLGDGVVTGYGTIDG 80
Cdd:COG4799     2 MRALLAELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGSFLELGALAGHRMYDDDDRVPGDGVVTGIGTVDG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  81 RSVYVFAQDFTVFGGALGETHARKICALMDLAAKNKAPIIGLNDSGGARIQEGVVSLDGYGHIFYRNVLYSGVIPQISVI 160
Cdd:COG4799    82 RPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGGIPQISVI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 161 LGPCAGGAVYSPALTDFIFMAEQTGRMFITGPKVIEKVTGEQVDAGSLGGAGIHNAVSGNAHFSGHTEKEVLTGVRKLLS 240
Cdd:COG4799   162 MGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 241 YLPLNGRttEPKPEKEASRPL-----LNHLVPADTTKPYDVRKVIRELADPQSFFEIQPFFAKNIVIGFARLGEKAIGIV 315
Cdd:COG4799   242 YLPSNNL--EDPPRAEPAPPArdpeeLYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 316 ASQPKHLAGSLTIDAADKAARFIRFCDAFDIPLLTVEDVPGFLPGIQQEHNGIIRHGAKLLFAYAEATVPKVTLIIRKAY 395
Cdd:COG4799   320 ANQPMVLAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAY 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 396 GGAYVAMNSKAIGADLVFAWPNAEIAVMGPEGAASILYEKEIKASADPQKTKREKTAEYKKQnAGPYKAAACGMVDDIIL 475
Cdd:COG4799   400 GAGYYAMCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAAAEDPEALRAELIAEYEEQ-ANPYYAAARGWIDDVID 478

                         490       500       510
                  ....*....|....*....|....*....|
gi 1167497201 476 PEESRGKLIQAFHMLAHKTEERPKKKHGNI 505
Cdd:COG4799   479 PRDTRRVLARALEAAANKPEERPPKKHGVI 508
mmdA TIGR01117
methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA ...
 3-507 0e+00

methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA decarboxylase aplha subunit in archaea and bacteria. Metylmalonyl-CoA decarboxylase Na+ pump is a representative of a class of Na+ transport decarboxylases that couples the energy derived by decarboxylation of carboxylic acid substrates to drive the extrusion of Na+ ion across the membrane. [Energy metabolism, ATP-proton motive force interconversion, Energy metabolism, Fermentation, Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130187  Cd Length: 512  Bit Score: 675.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201   3 EHMDHLYTKRKQAEEGGGREKLAQQRQKGKLTARERIIFLLDQDSFIELHPFMESQVLT---REQRMLGDGVVTGYGTID 79
Cdd:TIGR01117   1 EKIEELHEKKEKIKQGGGEKRIEKQHAQGKMTARERLALLFDPGSFVEIDQFVKHRCTNfgmDKKELPAEGVVTGYGTID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  80 GRSVYVFAQDFTVFGGALGETHARKICALMDLAAKNKAPIIGLNDSGGARIQEGVVSLDGYGHIFYRNVLYSGVIPQISV 159
Cdd:TIGR01117  81 GRLVYAFAQDFTVMGGSLGEMHAAKIVKIMDLAMKMGAPVVGLNDSGGARIQEAVDALKGYGDIFYRNTIASGVVPQISA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 160 ILGPCAGGAVYSPALTDFIFMAEQTGRMFITGPKVIEKVTGEQVDAGSLGGAGIHNAVSGNAHFSGHTEKEVLTGVRKLL 239
Cdd:TIGR01117 161 IMGPCAGGAVYSPALTDFIYMVDNTSQMFITGPQVIKTVTGEEVTAEQLGGAMAHNSVSGVAHFIAEDDDDCIMLIRRLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 240 SYLPLNGRTTEP--KPEKEASR--PLLNHLVPADTTKPYDVRKVIRELADPQSFFEIQPFFAKNIVIGFARLGEKAIGIV 315
Cdd:TIGR01117 241 SFLPSNNMEKAPlvKTGDDPTRetPELYDLLPDNPNKPYDMRDVITAIVDNGDYLEVQPYYAPNIITCFARINGQSVGII 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 316 ASQPKHLAGSLTIDAADKAARFIRFCDAFDIPLLTVEDVPGFLPGIQQEHNGIIRHGAKLLFAYAEATVPKVTLIIRKAY 395
Cdd:TIGR01117 321 ANQPKVMAGCLDIDSSDKIARFIRFCDAFNIPIVTFVDVPGFLPGVNQEYGGIIRHGAKVLYAYSEATVPKVTIITRKAY 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 396 GGAYVAMNSKAIGADLVFAWPNAEIAVMGPEGAASILYEKEIKASADPQKTKREKTAEYKKQNAGPYKAAACGMVDDIIL 475
Cdd:TIGR01117 401 GGAYLAMCSKHLGADQVYAWPTAEIAVMGPAGAANIIFRKDIKEAKDPAATRKQKIAEYREEFANPYKAAARGYVDDVIE 480

                         490       500       510
                  ....*....|....*....|....*....|..
gi 1167497201 476 PEESRGKLIQAFHMLAHKTEERPKKKHGNIPL 507
Cdd:TIGR01117 481 PKQTRPKIVNALAMLESKREKLPPKKHGNIPL 512
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 26-505 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: 673.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  26 QQRQKGKLTARERIIFLLDQDSFIELHPFMESQVLTRE-QRMLGDGVVTGYGTIDGRSVYVFAQDFTVFGGALGETHARK 104
Cdd:pfam01039   1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGrKRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 105 ICALMDLAAKNKAPIIGLNDSGGARIQEGVVSLDGYGHIFYRNVLYSGVIPQISVILGPCAGGAVYSPALTDFIFMAEQT 184
Cdd:pfam01039  81 ILRAMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGGAYLPALGDFVIMVEGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 185 GRMFITGPKVIEKVTGEQVDAGSLGGAGIHNAVSGNAHFSGHTEKEVLTGVRKLLSYLPL---NGRTTEPKPEKEAS--- 258
Cdd:pfam01039 161 SPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKpapNNREPVPIVPTKDPpdr 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 259 RPLLNHLVPADTTKPYDVRKVIRELADPQSFFEIQPFFAKNIVIGFARLGEKAIGIVASQPKHLAGSLTIDAADKAARFI 338
Cdd:pfam01039 241 DAPLVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQPRVGAGVLFPDSADKAARFI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 339 RFCDAFDIPLLTVEDVPGFLPGIQQEHNGIIRHGAKLLFAYAEATVPKVTLIIRKAYGGAYVAMNSKAIGADLVFAWPNA 418
Cdd:pfam01039 321 RDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDSKINGADINFAWPTA 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 419 EIAVMGPEGAASILYEKEIKAS----ADPQKTKREKTAEYKKQNAGPYKAAACGMVDDIILPEESRGKLIQAFHMLAHKT 494
Cdd:pfam01039 401 RIAVMGPEGAVEIKFRKEKAAAemrgKDLAATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKP 480

                         490
                  ....*....|.
gi 1167497201 495 EERPKKKHGNI 505
Cdd:pfam01039 481 RFFPWRKHGNI 491
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 1-480 7.06e-92

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 290.94  E-value: 7.06e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201   1 MNEHMDHLYTKRKQAEEGGGREKLAQQRQKGKLTARERIIFLLDQDS-FIELHPFMESQVLtrEQRMLGDGVVTGYGTID 79
Cdd:PLN02820   50 MEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSpFLELSQLAGHELY--GEDLPSGGIVTGIGPVH 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  80 GRSVYVFAQDFTVFGGALGETHARKICALMDLAAKNKAPIIGLNDSGGA---RIQEGVVSLDGYGHIFY-RNVLYSGVIP 155
Cdd:PLN02820  128 GRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGAnlpRQAEVFPDRDHFGRIFYnQARMSSAGIP 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 156 QISVILGPCAGGAVYSPALTDFIFMAEQTGRMFITGPKVIEKVTGEQVDAGSLGGAGIHNAVSGNAHFSGHTEKEVLTGV 235
Cdd:PLN02820  208 QIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSDHFAQDELHALAIG 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 236 RKLLSYLPLNGRTTEPKPEKEAS----RPL-----LNHLVPADTTKPYDVRKVIRELADPQSFFEIQPFFAKNIVIGFAR 306
Cdd:PLN02820  288 RNIVKNLHLAAKQGMENTLGSKNpeykEPLydvkeLRGIVPADHKQSFDVRSVIARIVDGSEFDEFKKNYGTTLVTGFAR 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 307 LGEKAIGIVASQpkhlaGSLTIDAADKAARFIRFCDAFDIPLLTVEDVPGFLPGIQQEHNGIIRHGAKLLFAYAEATVPK 386
Cdd:PLN02820  368 IYGQPVGIIGNN-----GILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMVMAVACAKVPK 442

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 387 VTLIIRKAYGGAYVAMNSKAIGADLVFAWPNAEIAVMGPEGAASILYEKE--------IKASADPQKTKREKTAEYKKQN 458
Cdd:PLN02820  443 ITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQIErenkkrqgIQWSKEEEEAFKAKTVEAYERE 522

                         490       500
                  ....*....|....*....|..
gi 1167497201 459 AGPYKAAACGMVDDIILPEESR 480
Cdd:PLN02820  523 ANPYYSTARLWDDGVIDPADTR 544
PRK07189 PRK07189
malonate decarboxylase subunit beta; Reviewed
 33-205 2.10e-22

malonate decarboxylase subunit beta; Reviewed


Pssm-ID: 235954  Cd Length: 301  Bit Score: 97.28  E-value: 2.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  33 LTARERIIFLLDQDSFIE-LHPF--MESQVLTR--EQRMLGDGVVTGYGTIDGRSVYVFAQDFTVFGGALGETHARKICA 107
Cdd:PRK07189   15 ASARERAAALLDAGSFRElLGPFerVMSPHLPLqgIPPQFDDGVVVGKGTLDGRPVVVAAQEGRFMGGSVGEVHGAKLAG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 108 LMDLAAKNK-----APIIGLNDSGGARIQEGVVSLDGYGHIFYRNVLYSGVIPQISVILGP--CAGGAVYSPALTDFIFM 180
Cdd:PRK07189   95 ALELAAEDNrngipTAVLLLFETGGVRLQEANAGLAAIAEIMRAIVDLRAAVPVIGLIGGRvgCFGGMGIAAALCSYLIV 174

                         170       180
                  ....*....|....*....|....*.
gi 1167497201 181 AEQtGRMFITGPKVIEKVTG-EQVDA 205
Cdd:PRK07189  175 SEE-GRLGLSGPEVIEQEAGvEEFDS 199
AccD COG0777
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 32-202 3.63e-21

Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase beta subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440540 [Multi-domain]  Cd Length: 280  Bit Score: 93.20  E-value: 3.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  32 KLTARERIIFLLDQDSFIELHPFMES-------------QVLTREQRMLG--DGVVTGYGTIDGRSVYVFAQDFTVFGG- 95
Cdd:COG0777    55 RISARERLELLLDEGSFEELDADLVPvdplkfkdskkykDRLKEAQKKTGlkDAVVTGTGTINGIPVVVAVMDFSFMGGs 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  96 ---ALGEtharKICALMDLAAKNKAPIIGLNDSGGARIQEGVVSL--------------DgyghifyRNVLYsgvipqIS 158
Cdd:COG0777   135 mgsVVGE----KITRAIERAIEKKLPLIIFSASGGARMQEGILSLmqmaktsaalarlsE-------AGLPY------IS 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1167497201 159 VILGPCAGGAVYSPA-LTDFIFmAEQTGR-MFiTGPKVIEKVTGEQ 202
Cdd:COG0777   198 VLTDPTTGGVTASFAmLGDIII-AEPGALiGF-AGPRVIEQTIREK 241
accD CHL00174
acetyl-CoA carboxylase beta subunit; Reviewed
 32-207 1.33e-12

acetyl-CoA carboxylase beta subunit; Reviewed


Pssm-ID: 214384 [Multi-domain]  Cd Length: 296  Bit Score: 68.39  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  32 KLTARERIIFLLDQDSFIELHPFMES--------------QVLTREQRMLG--DGVVTGYGTIDGRSVYVFAQDFTVFGG 95
Cdd:CHL00174   68 KMSSSDRIELLIDPGTWNPMDEDMVSldpiefhsdeepykDRIDSYQKKTGltDAVQTGIGQLNGIPVALGVMDFQFMGG 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  96 ALGETHARKICALMDLAAKNKAPIIGLNDSGGARIQEGVVSLDG--------YGHIFYRNVLYsgvipqISVILGPCAGG 167
Cdd:CHL00174  148 SMGSVVGEKITRLIEYATNESLPLIIVCASGGARMQEGSLSLMQmakissalYDYQSNKKLFY------ISILTSPTTGG 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1167497201 168 AVYSPALTDFIFMAEQTGRMFITGPKVIEKVTGEQVDAGS 207
Cdd:CHL00174  222 VTASFGMLGDIIIAEPNAYIAFAGKRVIEQTLNKTVPEGS 261
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 333-477 1.72e-07

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 52.84  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 333 KAARFIRFCDAFDIPLLTVEDVPGFLPGIQQEHNGIIRHGAKLLFAYAEATVPKVTLIIRK-AYGGAYvamnskAIG-AD 410
Cdd:PRK05724  139 KALRLMKMAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEgGSGGAL------AIGvGD 212

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167497201 411 LVFAWPNAEIAVMGPEGAASILYekeikasadpqktkreKTAEYKKQNAGPYKAAA-----CGMVDDIIlPE 477
Cdd:PRK05724  213 RVLMLEYSTYSVISPEGCASILW----------------KDASKAPEAAEAMKITAqdlkeLGIIDEII-PE 267
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 300-477 7.19e-06

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 47.46  E-value: 7.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 300 IVIGFARLGEKAIGIVASQP-KHLA-------GSLTIDAADKAARFIRFCDAFDIPLLTVEDVPGFLPGIQQEHNGIIRH 371
Cdd:PRK12319   45 VVGGIGYLAGQPVTVVGIQKgKNLQdnlkrnfGQPHPEGYRKALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEA 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 372 GAKLLFAYAEATVPKVTLIIRKAYGGAYVAMnskAIgADLVFAWPNAEIAVMGPEGAASILYEKEIKAsadpqktkrEKT 451
Cdd:PRK12319  125 IARNLMEMSDLKVPIIAIIIGEGGSGGALAL---AV-ADQVWMLENTMYAVLSPEGFASILWKDGSRA---------TEA 191

                         170       180
                  ....*....|....*....|....*.
gi 1167497201 452 AEYKKQNAGPYKAAacGMVDDIIlPE 477
Cdd:PRK12319  192 AELMKITAGELLEM--GVVDKVI-PE 214
PLN03230 PLN03230
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
 333-477 3.46e-05

acetyl-coenzyme A carboxylase carboxyl transferase; Provisional


Pssm-ID: 178769 [Multi-domain]  Cd Length: 431  Bit Score: 46.09  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 333 KAARFIRFCDAFDIPLLTVEDVPGFLPGIQQEHNGiirHGAKLLFAYAEA---TVPKVTLIIRKayGGAYVAMnskAIG- 408
Cdd:PLN03230  209 KALRFMRHAEKFGFPILTFVDTPGAYAGIKAEELG---QGEAIAFNLREMfglRVPIIATVIGE--GGSGGAL---AIGc 280

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167497201 409 ADLVFAWPNAEIAVMGPEGAASILYEkeiKASADPQKTK--REKTAEYKKqnagpykaaaCGMVDDIIlPE 477
Cdd:PLN03230  281 GNRMLMMENAVYYVASPEACAAILWK---SAAAAPKAAEalRITAAELVK----------LGVVDEIV-PE 337
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 333-477 9.71e-05

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 44.42  E-value: 9.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 333 KAARFIRFCDAFDIPLLTVEDVPGFLPGIQQEHNG---IIRHGAKLLFAYaeaTVPKVTLIIRKayGGAYVAMnskAIG- 408
Cdd:CHL00198  142 KALRLMKHANKFGLPILTFIDTPGAWAGVKAEKLGqgeAIAVNLREMFSF---EVPIICTIIGE--GGSGGAL---GIGi 213

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167497201 409 ADLVFAWPNAEIAVMGPEGAASILYeKEIKASADpqktkrekTAEYKKQNAGPYKaaACGMVDDIIlPE 477
Cdd:CHL00198  214 GDSIMMLEYAVYTVATPEACAAILW-KDSKKSLD--------AAEALKITSEDLK--VLGIIDEII-PE 270
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 333-477 1.77e-04

Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase alpha subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440587 [Multi-domain]  Cd Length: 315  Bit Score: 43.49  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 333 KAARFIRFCDAFDIPLLTVEDVPGFLPGIQQEHNGI---IrhgAKLLFAYAEATVPKVTLIIRK-AYGGAYvamnskAIG 408
Cdd:COG0825   136 KALRLMKLAEKFGLPIITFIDTPGAYPGIGAEERGQseaI---ARNLREMARLKVPIISVVIGEgGSGGAL------AIG 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 409 -ADLVFAWPNAEIAVMGPEGAASILYekeikasadpqktkreKTAEYKKQnagpykAAAC-----------GMVDDIIlP 476
Cdd:COG0825   207 vGDRVLMLEHSIYSVISPEGCASILW----------------KDASKAPE------AAEAlkitaqdlkelGIIDEII-P 263


                  .
gi 1167497201 477 E 477
Cdd:COG0825   264 E 264
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 24-184 9.81e-04

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 40.92  E-value: 9.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  24 LAQQRQKGKLTARE--RIIFlldqDSFIELHPfmesqvltrEQRMLGDG-VVTGYGTIDGRSVYVFA-------QD--FT 91
Cdd:PRK12319    8 LKEARDQGRLTTLDyaTLIF----DDFMELHG---------DRHFRDDGaVVGGIGYLAGQPVTVVGiqkgknlQDnlKR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  92 VFGGALGETHaRKICALMDLAAKNKAPIIGLNDSGGAriQEGVVSLD-GYGHIFYRNVLYSG--VIPQISVILGPCAGGA 168
Cdd:PRK12319   75 NFGQPHPEGY-RKALRLMKQAEKFGRPVVTFINTAGA--YPGVGAEErGQGEAIARNLMEMSdlKVPIIAIIIGEGGSGG 151

                         170
                  ....*....|....*.
gi 1167497201 169 VYSPALTDFIFMAEQT 184
Cdd:PRK12319  152 ALALAVADQVWMLENT 167
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 22-182 4.64e-03

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 39.02  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  22 EKLAQQRQKGKLTARERIIFLLDqdSFIELHpfmesqvltreqrmlGD-------GVVTGYGTIDGRSVYVFAQD----- 89
Cdd:CHL00198   62 QRLHLVRQSERPTTLDYIPYILD--EWIELH---------------GDrggsddpALVGGIGKINGRTIVFLGHQrgrnt 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201  90 ----FTVFGGALGETHaRKICALMDLAAKNKAPIIGLNDSGGAriQEGV-VSLDGYGHIFYRNV--LYSGVIPQISVILG 162
Cdd:CHL00198  125 kenvLRNFGMPSPGGY-RKALRLMKHANKFGLPILTFIDTPGA--WAGVkAEKLGQGEAIAVNLreMFSFEVPIICTIIG 201

                         170       180
                  ....*....|....*....|
gi 1167497201 163 PCAGGAVYSPALTDFIFMAE 182
Cdd:CHL00198  202 EGGSGGALGIGIGDSIMMLE 221
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 333-440 7.30e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 39.07  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167497201 333 KAARFIRFCDAFDIPLLTVEDVPGFLPGIQQEHNG---IIRHGAKLLFAYaeaTVPKVTLIIRKayGGAYVAMnskAIG- 408
Cdd:PLN03229  230 KALRMMYYADHHGFPIVTFIDTPGAYADLKSEELGqgeAIAHNLRTMFGL---KVPIVSIVIGE--GGSGGAL---AIGc 301

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1167497201 409 ADLVFAWPNAEIAVMGPEGAASILYeKEIKAS 440
Cdd:PLN03229  302 ANKLLMLENAVFYVASPEACAAILW-KSAKAA 332
 
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.
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