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Conserved domains on  [gi|815674382|ref|WP_046412208|]
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acyl-CoA carboxylase subunit beta [Barnesiella intestinihominis]

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];
5-515 0e+00

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


:

Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 892.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382   5 LEKVQELIELRAQARLGGGQKAIDKQHEKGKYTARERIAQLLDEGSFEELDMFVKHRCTNfgqEKKSFLGDGVVTGYGTI 84
Cdd:COG4799    3 RALLAELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGSFLELGALAGHRMYD---DDDRVPGDGVVTGIGTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  85 EGRLVYVFAQDFTVFGGSLSETMALKICKVMDMAMKMGAPCIGLNDSGGARIQEGINALAGYAEIFQRNIMASGVIPQIS 164
Cdd:COG4799   80 DGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGGIPQIS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 165 AILGPCAGGAVYSPALTDFTIMAKGISYMFLTGPKVVKTVTGEDVTQEALGGAEVHSAKSGVAHFAAENGEEALSIIRKL 244
Cdd:COG4799  160 VIMGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 245 ISYIPQNNLEEAPLVPCNDPiDRLEDSLNEIIPDSPNRPYDMYEVIGAIIDNGEFLEIQRDYAKNIIVGFARFNGQSVGI 324
Cdd:COG4799  240 LSYLPSNNLEDPPRAEPAPP-ARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGI 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 325 VANQPKYLAGVLDSNASRKAARFVRFCDAFNIPIVSLVDVPGFLPGTGQEYNGVILHGAKLLYAYGEATVPKVTITLRKS 404
Cdd:COG4799  319 VANQPMVLAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKA 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 405 YGGSHIVMSCKQLRGDMNYAWPTAEIAVMGGAGAVEVLYAKEAKEAEDPAKFMAEKEAEYTKlFANPYNAAKYGYIDDVI 484
Cdd:COG4799  399 YGAGYYAMCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAAAEDPEALRAELIAEYEE-QANPYYAAARGWIDDVI 477

                        490       500       510
                 ....*....|....*....|....*....|.
gi 815674382 485 EPRNTRFRIIRALQQLQTKKLTNPAKKHGNI 515
Cdd:COG4799  478 DPRDTRRVLARALEAAANKPEERPPKKHGVI 508
 
Name Accession Description Interval E-value
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
5-515 0e+00

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 892.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382   5 LEKVQELIELRAQARLGGGQKAIDKQHEKGKYTARERIAQLLDEGSFEELDMFVKHRCTNfgqEKKSFLGDGVVTGYGTI 84
Cdd:COG4799    3 RALLAELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGSFLELGALAGHRMYD---DDDRVPGDGVVTGIGTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  85 EGRLVYVFAQDFTVFGGSLSETMALKICKVMDMAMKMGAPCIGLNDSGGARIQEGINALAGYAEIFQRNIMASGVIPQIS 164
Cdd:COG4799   80 DGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGGIPQIS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 165 AILGPCAGGAVYSPALTDFTIMAKGISYMFLTGPKVVKTVTGEDVTQEALGGAEVHSAKSGVAHFAAENGEEALSIIRKL 244
Cdd:COG4799  160 VIMGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 245 ISYIPQNNLEEAPLVPCNDPiDRLEDSLNEIIPDSPNRPYDMYEVIGAIIDNGEFLEIQRDYAKNIIVGFARFNGQSVGI 324
Cdd:COG4799  240 LSYLPSNNLEDPPRAEPAPP-ARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGI 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 325 VANQPKYLAGVLDSNASRKAARFVRFCDAFNIPIVSLVDVPGFLPGTGQEYNGVILHGAKLLYAYGEATVPKVTITLRKS 404
Cdd:COG4799  319 VANQPMVLAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKA 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 405 YGGSHIVMSCKQLRGDMNYAWPTAEIAVMGGAGAVEVLYAKEAKEAEDPAKFMAEKEAEYTKlFANPYNAAKYGYIDDVI 484
Cdd:COG4799  399 YGAGYYAMCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAAAEDPEALRAELIAEYEE-QANPYYAAARGWIDDVI 477

                        490       500       510
                 ....*....|....*....|....*....|.
gi 815674382 485 EPRNTRFRIIRALQQLQTKKLTNPAKKHGNI 515
Cdd:COG4799  478 DPRDTRRVLARALEAAANKPEERPPKKHGVI 508
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 29-515 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: 691.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382   29 KQHEKGKYTARERIAQLLDEGSFEELDMFVKHRCTNFGQEKksFLGDGVVTGYGTIEGRLVYVFAQDFTVFGGSLSETMA 108
Cdd:pfam01039   1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR--IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  109 LKICKVMDMAMKMGAPCIGLNDSGGARIQEGINALAGYAEIFQRNIMASGVIPQISAILGPCAGGAVYSPALTDFTIMAK 188
Cdd:pfam01039  79 EKILRAMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGGAYLPALGDFVIMVE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  189 GISYMFLTGPKVVKTVTGEDVTQEALGGAEVHSAKSGVAHFAAENGEEALSIIRKLISYIP---QNNLEEAPLVPCNDPI 265
Cdd:pfam01039 159 GTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPkpaPNNREPVPIVPTKDPP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  266 DRLEDsLNEIIPDSPNRPYDMYEVIGAIIDNGEFLEIQRDYAKNIIVGFARFNGQSVGIVANQPKYLAGVLDSNASRKAA 345
Cdd:pfam01039 239 DRDAP-LVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQPRVGAGVLFPDSADKAA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  346 RFVRFCDAFNIPIVSLVDVPGFLPGTGQEYNGVILHGAKLLYAYGEATVPKVTITLRKSYGGSHIVMSCKQLRGDMNYAW 425
Cdd:pfam01039 318 RFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDSKINGADINFAW 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  426 PTAEIAVMGGAGAVEVLYAKEAKEAE----DPAKFMAEKEAEYTKLFANPYNAAKYGYIDDVIEPRNTRFRIIRALQQLQ 501
Cdd:pfam01039 398 PTARIAVMGPEGAVEIKFRKEKAAAEmrgkDLAATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALW 477

                         490
                  ....*....|....
gi 815674382  502 TKKLTNPAKKHGNI 515
Cdd:pfam01039 478 TKPRFFPWRKHGNI 491
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 8-490 4.46e-98

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 307.51  E-value: 4.46e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382   8 VQELIELRAQARLGGGQKAIDKQHEKGKYTARERIAQLLDEGS-FEELDMFVKHRCtnFGQEKKSflgDGVVTGYGTIEG 86
Cdd:PLN02820  54 LSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSpFLELSQLAGHEL--YGEDLPS---GGIVTGIGPVHG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  87 RLVYVFAQDFTVFGGSLSETMALKICKVMDMAMKMGAPCIGLNDSGGARiqeginaLAGYAEIF-----------QRNIM 155
Cdd:PLN02820 129 RLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGAN-------LPRQAEVFpdrdhfgrifyNQARM 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 156 ASGVIPQISAILGPCAGGAVYSPALTDFTIMAKGISYMFLTGPKVVKTVTGEDVTQEALGGAEVHSAKSGVAHFAAENGE 235
Cdd:PLN02820 202 SSAGIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSDHFAQDEL 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 236 EALSIIRKLISYIP------QNNLEEAPLVPCNDPIDRLEDsLNEIIPDSPNRPYDMYEVIGAIIDNGEFLEIQRDYAKN 309
Cdd:PLN02820 282 HALAIGRNIVKNLHlaakqgMENTLGSKNPEYKEPLYDVKE-LRGIVPADHKQSFDVRSVIARIVDGSEFDEFKKNYGTT 360

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 310 IIVGFARFNGQSVGIVANQpkylaGVLDSNASRKAARFVRFCDAFNIPIVSLVDVPGFLPGTGQEYNGVILHGAKLLYAY 389
Cdd:PLN02820 361 LVTGFARIYGQPVGIIGNN-----GILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMVMAV 435

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 390 GEATVPKVTITLRKSYGGSHIVMSCKQLRGDMNYAWPTAEIAVMGGAGAVEVLYAKEAKE---------AEDPAKFMAEK 460
Cdd:PLN02820 436 ACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQIERENkkrqgiqwsKEEEEAFKAKT 515

                        490       500       510
                 ....*....|....*....|....*....|
gi 815674382 461 EAEYTKLfANPYNAAKYGYIDDVIEPRNTR 490
Cdd:PLN02820 516 VEAYERE-ANPYYSTARLWDDGVIDPADTR 544
 
Name Accession Description Interval E-value
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
5-515 0e+00

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 892.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382   5 LEKVQELIELRAQARLGGGQKAIDKQHEKGKYTARERIAQLLDEGSFEELDMFVKHRCTNfgqEKKSFLGDGVVTGYGTI 84
Cdd:COG4799    3 RALLAELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGSFLELGALAGHRMYD---DDDRVPGDGVVTGIGTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  85 EGRLVYVFAQDFTVFGGSLSETMALKICKVMDMAMKMGAPCIGLNDSGGARIQEGINALAGYAEIFQRNIMASGVIPQIS 164
Cdd:COG4799   80 DGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGGIPQIS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 165 AILGPCAGGAVYSPALTDFTIMAKGISYMFLTGPKVVKTVTGEDVTQEALGGAEVHSAKSGVAHFAAENGEEALSIIRKL 244
Cdd:COG4799  160 VIMGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 245 ISYIPQNNLEEAPLVPCNDPiDRLEDSLNEIIPDSPNRPYDMYEVIGAIIDNGEFLEIQRDYAKNIIVGFARFNGQSVGI 324
Cdd:COG4799  240 LSYLPSNNLEDPPRAEPAPP-ARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGI 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 325 VANQPKYLAGVLDSNASRKAARFVRFCDAFNIPIVSLVDVPGFLPGTGQEYNGVILHGAKLLYAYGEATVPKVTITLRKS 404
Cdd:COG4799  319 VANQPMVLAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKA 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 405 YGGSHIVMSCKQLRGDMNYAWPTAEIAVMGGAGAVEVLYAKEAKEAEDPAKFMAEKEAEYTKlFANPYNAAKYGYIDDVI 484
Cdd:COG4799  399 YGAGYYAMCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAAAEDPEALRAELIAEYEE-QANPYYAAARGWIDDVI 477

                        490       500       510
                 ....*....|....*....|....*....|.
gi 815674382 485 EPRNTRFRIIRALQQLQTKKLTNPAKKHGNI 515
Cdd:COG4799  478 DPRDTRRVLARALEAAANKPEERPPKKHGVI 508
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 29-515 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: 691.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382   29 KQHEKGKYTARERIAQLLDEGSFEELDMFVKHRCTNFGQEKksFLGDGVVTGYGTIEGRLVYVFAQDFTVFGGSLSETMA 108
Cdd:pfam01039   1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR--IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  109 LKICKVMDMAMKMGAPCIGLNDSGGARIQEGINALAGYAEIFQRNIMASGVIPQISAILGPCAGGAVYSPALTDFTIMAK 188
Cdd:pfam01039  79 EKILRAMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGGAYLPALGDFVIMVE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  189 GISYMFLTGPKVVKTVTGEDVTQEALGGAEVHSAKSGVAHFAAENGEEALSIIRKLISYIP---QNNLEEAPLVPCNDPI 265
Cdd:pfam01039 159 GTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPkpaPNNREPVPIVPTKDPP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  266 DRLEDsLNEIIPDSPNRPYDMYEVIGAIIDNGEFLEIQRDYAKNIIVGFARFNGQSVGIVANQPKYLAGVLDSNASRKAA 345
Cdd:pfam01039 239 DRDAP-LVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQPRVGAGVLFPDSADKAA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  346 RFVRFCDAFNIPIVSLVDVPGFLPGTGQEYNGVILHGAKLLYAYGEATVPKVTITLRKSYGGSHIVMSCKQLRGDMNYAW 425
Cdd:pfam01039 318 RFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDSKINGADINFAW 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  426 PTAEIAVMGGAGAVEVLYAKEAKEAE----DPAKFMAEKEAEYTKLFANPYNAAKYGYIDDVIEPRNTRFRIIRALQQLQ 501
Cdd:pfam01039 398 PTARIAVMGPEGAVEIKFRKEKAAAEmrgkDLAATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALW 477

                         490
                  ....*....|....
gi 815674382  502 TKKLTNPAKKHGNI 515
Cdd:pfam01039 478 TKPRFFPWRKHGNI 491
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 8-490 4.46e-98

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 307.51  E-value: 4.46e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382   8 VQELIELRAQARLGGGQKAIDKQHEKGKYTARERIAQLLDEGS-FEELDMFVKHRCtnFGQEKKSflgDGVVTGYGTIEG 86
Cdd:PLN02820  54 LSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSpFLELSQLAGHEL--YGEDLPS---GGIVTGIGPVHG 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  87 RLVYVFAQDFTVFGGSLSETMALKICKVMDMAMKMGAPCIGLNDSGGARiqeginaLAGYAEIF-----------QRNIM 155
Cdd:PLN02820 129 RLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGAN-------LPRQAEVFpdrdhfgrifyNQARM 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 156 ASGVIPQISAILGPCAGGAVYSPALTDFTIMAKGISYMFLTGPKVVKTVTGEDVTQEALGGAEVHSAKSGVAHFAAENGE 235
Cdd:PLN02820 202 SSAGIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSDHFAQDEL 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 236 EALSIIRKLISYIP------QNNLEEAPLVPCNDPIDRLEDsLNEIIPDSPNRPYDMYEVIGAIIDNGEFLEIQRDYAKN 309
Cdd:PLN02820 282 HALAIGRNIVKNLHlaakqgMENTLGSKNPEYKEPLYDVKE-LRGIVPADHKQSFDVRSVIARIVDGSEFDEFKKNYGTT 360

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 310 IIVGFARFNGQSVGIVANQpkylaGVLDSNASRKAARFVRFCDAFNIPIVSLVDVPGFLPGTGQEYNGVILHGAKLLYAY 389
Cdd:PLN02820 361 LVTGFARIYGQPVGIIGNN-----GILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMVMAV 435

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 390 GEATVPKVTITLRKSYGGSHIVMSCKQLRGDMNYAWPTAEIAVMGGAGAVEVLYAKEAKE---------AEDPAKFMAEK 460
Cdd:PLN02820 436 ACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQIERENkkrqgiqwsKEEEEAFKAKT 515

                        490       500       510
                 ....*....|....*....|....*....|
gi 815674382 461 EAEYTKLfANPYNAAKYGYIDDVIEPRNTR 490
Cdd:PLN02820 516 VEAYERE-ANPYYSTARLWDDGVIDPADTR 544
AccD COG0777
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 37-143 2.67e-20

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: 90.89  E-value: 2.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  37 TARERIAQLLDEGSFEELDmfvKHRCT----NFGQEK-----------KSFLGDGVVTGYGTIEGRLVYVFAQDFTVFGG 101
Cdd:COG0777   57 SARERLELLLDEGSFEELD---ADLVPvdplKFKDSKkykdrlkeaqkKTGLKDAVVTGTGTINGIPVVVAVMDFSFMGG 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 815674382 102 SLSETMALKICKVMDMAMKMGAPCIGLNDSGGARIQEGINAL 143
Cdd:COG0777  134 SMGSVVGEKITRAIERAIEKKLPLIIFSASGGARMQEGILSL 175
PRK07189 PRK07189
malonate decarboxylase subunit beta; Reviewed
 37-208 2.53e-15

malonate decarboxylase subunit beta; Reviewed


Pssm-ID: 235954  Cd Length: 301  Bit Score: 76.48  E-value: 2.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  37 TARERIAQLLDEGSFEEL----DMFVKHRCTNFGQEKKSflGDGVVTGYGTIEGRLVYVFAQDFTVFGGSLSETMALKIC 112
Cdd:PRK07189  16 SARERAAALLDAGSFRELlgpfERVMSPHLPLQGIPPQF--DDGVVVGKGTLDGRPVVVAAQEGRFMGGSVGEVHGAKLA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 113 KVMDMAMKMG-----APCIGLNDSGGARIQEGiNA-LAGYAEIfQRNIM-ASGVIPQISAILGP--CAGGAVYSPALTDF 183
Cdd:PRK07189  94 GALELAAEDNrngipTAVLLLFETGGVRLQEA-NAgLAAIAEI-MRAIVdLRAAVPVIGLIGGRvgCFGGMGIAAALCSY 171

                        170       180
                 ....*....|....*....|....*..
gi 815674382 184 TIMAKG--ISymfLTGPKVVKTVTGED 208
Cdd:PRK07189 172 LIVSEEgrLG---LSGPEVIEQEAGVE 195
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 280-374 1.84e-09

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: 58.90  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 280 PNRPYdMYEVIGAIIDngEFLEIQ--RDYA--KNIIVGFARFNGQSVGIVANQ---------------PK---Ylagvld 337
Cdd:COG0825   64 PQRPY-TLDYIEAIFT--DFIELHgdRAFGddPAIVGGLARFDGRPVMVIGHQkgrdtkerikrnfgmPHpegY------ 134

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 815674382 338 snasRKAARFVRFCDAFNIPIVSLVDVPGFLPGTGQE 374
Cdd:COG0825  135 ----RKALRLMKLAEKFGLPIITFIDTPGAYPGIGAE 167
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 280-374 2.84e-09

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 58.62  E-value: 2.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 280 PNRPYDMyEVIGAIIDngEFLEIQ--RDYA--KNIIVGFARFNGQSVGIVANQ---------------PK---Ylagvld 337
Cdd:PRK05724  67 PQRPYTL-DYIELLFT--DFTELHgdRAFAddKAIVGGLARLNGRPVMVIGHQkgrdtkekirrnfgmPRpegY------ 137

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 815674382 338 snasRKAARFVRFCDAFNIPIVSLVDVPGFLPGTGQE 374
Cdd:PRK05724 138 ----RKALRLMKMAEKFGLPIITFIDTPGAYPGIGAE 170
accD CHL00174
acetyl-CoA carboxylase beta subunit; Reviewed
 35-149 1.28e-06

acetyl-CoA carboxylase beta subunit; Reviewed


Pssm-ID: 214384 [Multi-domain]  Cd Length: 296  Bit Score: 50.29  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382  35 KYTARERIAQLLDEGSFEELD--MF-------------VKHRCTnFGQEKKSfLGDGVVTGYGTIEGRLVYVFAQDFTVF 99
Cdd:CHL00174  68 KMSSSDRIELLIDPGTWNPMDedMVsldpiefhsdeepYKDRID-SYQKKTG-LTDAVQTGIGQLNGIPVALGVMDFQFM 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 815674382 100 GGSLSETMALKICKVMDMAMKMGAPCIGLNDSGGARIQEGINALAGYAEI 149
Cdd:CHL00174 146 GGSMGSVVGEKITRLIEYATNESLPLIIVCASGGARMQEGSLSLMQMAKI 195
PLN03230 PLN03230
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
 264-377 2.00e-04

acetyl-coenzyme A carboxylase carboxyl transferase; Provisional


Pssm-ID: 178769 [Multi-domain]  Cd Length: 431  Bit Score: 43.78  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 264 PIDRLEdslneiIPDSPNRPyDMYEVIGAIIDngEFLEIQRDYA----KNIIVGFARFNGQSVGIVANQPKYLA------ 333
Cdd:PLN03230 127 PVQRLS------VARHPNRP-TFLDHVLNMTD--KWVELHGDRAgfddPAIVCGIGSMEGMSFMFIGHQKGRNTkeniyr 197

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 815674382 334 --GVLDSNASRKAARFVRFCDAFNIPIVSLVDVPGFLPGTGQEYNG 377
Cdd:PLN03230 198 nfAMPQPNGYRKALRFMRHAEKFGFPILTFVDTPGAYAGIKAEELG 243
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 280-328 3.52e-04

Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A carboxylase carboxyltransferase is composed of an alpha and beta subunit.


Pssm-ID: 427221 [Multi-domain]  Cd Length: 144  Bit Score: 40.85  E-value: 3.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 815674382  280 PNRPYdMYEVIGAIIDngEFLEI--QRDYA--KNIIVGFARFNGQSVGIVANQ 328
Cdd:pfam03255  63 PERPY-TLDYIEALFD--DFIELhgDRLFGddPAIVGGLARFDGQPVMVIGHQ 112
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 298-511 4.08e-03

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 38.99  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 298 EFLEIQ--RDYAKN--IIVGFARFNGQSVGIVANQP-KYLAGVLDSN-------ASRKAARFVRFCDAFNIPIVSLVDVP 365
Cdd:PRK12319  29 DFMELHgdRHFRDDgaVVGGIGYLAGQPVTVVGIQKgKNLQDNLKRNfgqphpeGYRKALRLMKQAEKFGRPVVTFINTA 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815674382 366 GFLPGTGQEYNGVILHGAKLLYAYGEATVPKVTITLRKSYGGSHIVMSCkqlrGDMNYAWPTAEIAVMGGAGAVEVLYaK 445
Cdd:PRK12319 109 GAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAV----ADQVWMLENTMYAVLSPEGFASILW-K 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815674382 446 EAKEAEDPAKFMAEKEAEYTKLfanpynaakyGYIDDVIePRNTRF--RIIRALQQLQTKKLTNPAKK 511
Cdd:PRK12319 184 DGSRATEAAELMKITAGELLEM----------GVVDKVI-PEHGYFssEIIDMIKKNLIEELAQLSQK 240
 
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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