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Conserved domains on  [gi|498122364|ref|WP_010436520|]
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MULTISPECIES: acetyl-CoA carboxylase carboxyl transferase subunit alpha [Vibrio]

Protein Classification

acetyl-CoA carboxylase carboxyltransferase subunit alpha( domain architecture ID 10002787)

acetyl-CoA carboxylase carboxyltransferase subunit alpha (AccA) is a component of the acetyl coenzyme A carboxylase (ACC) complex that catalyzes the carboxylation of acetyl-CoA to form malonyl-CoA

CATH:  3.90.226.10
EC:  2.1.3.15
Gene Ontology:  GO:0003989|GO:0005524|GO:0016743|GO:0006633|GO:0005524|GO:0009317
PubMed:  1355089
SCOP:  4000456

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 4-319 0e+00

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: 628.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364   4 NFLEFEKPIAELEAKIEALRDVSRhggDAAVDLDKEIEQLEKKSLELKQKIFSDLGAWQVAQLARHPQRPYTKDYLEHAF 83
Cdd:COG0825    1 NYLDFEKPIAELEAKIEELRALAE---ESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  84 TEFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGYRKALRLMETAERFNMPIITFIDT 163
Cdd:COG0825   78 TDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 164 AGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIGVGDYVNMLQYSTYSVISPEGCASILWRDSDK 243
Cdd:COG0825  158 PGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASK 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498122364 244 APQAAEAMGLVAPRLKELELIDEIIPEPLGGAHRDPVQTAQNMKDMLVKQLEELEQFDNEALLERRYQRLMSYGYC 319
Cdd:COG0825  238 APEAAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGRF 313
 
Name Accession Description Interval E-value
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 4-319 0e+00

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: 628.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364   4 NFLEFEKPIAELEAKIEALRDVSRhggDAAVDLDKEIEQLEKKSLELKQKIFSDLGAWQVAQLARHPQRPYTKDYLEHAF 83
Cdd:COG0825    1 NYLDFEKPIAELEAKIEELRALAE---ESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  84 TEFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGYRKALRLMETAERFNMPIITFIDT 163
Cdd:COG0825   78 TDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 164 AGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIGVGDYVNMLQYSTYSVISPEGCASILWRDSDK 243
Cdd:COG0825  158 PGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASK 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498122364 244 APQAAEAMGLVAPRLKELELIDEIIPEPLGGAHRDPVQTAQNMKDMLVKQLEELEQFDNEALLERRYQRLMSYGYC 319
Cdd:COG0825  238 APEAAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGRF 313
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 1-319 0e+00

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 624.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364   1 MSLNFLEFEKPIAELEAKIEALRDVSRhggDAAVDLDKEIEQLEKKSLELKQKIFSDLGAWQVAQLARHPQRPYTKDYLE 80
Cdd:PRK05724   1 MMLNYLDFEKPIAELEAKIEELRAVAE---DSDVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  81 HAFTEFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGYRKALRLMETAERFNMPIITF 160
Cdd:PRK05724  78 LLFTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIITF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 161 IDTAGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIGVGDYVNMLQYSTYSVISPEGCASILWRD 240
Cdd:PRK05724 158 IDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWKD 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498122364 241 SDKAPQAAEAMGLVAPRLKELELIDEIIPEPLGGAHRDPVQTAQNMKDMLVKQLEELEQFDNEALLERRYQRLMSYGYC 319
Cdd:PRK05724 238 ASKAPEAAEAMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAAALKEALLEALAELKGLSPEELLERRYEKFMSIGRF 316
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 1-319 0e+00

acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the alpha chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273113 [Multi-domain]  Cd Length: 316  Bit Score: 534.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364    1 MSLNFLEFEKPIAELEAKIEALRDVSRhggDAAVDLDKEIEQLEKKSLELKQKIFSDLGAWQVAQLARHPQRPYTKDYLE 80
Cdd:TIGR00513   1 MMANYLDFEKPIAELEAKIESLRARSR---DEDVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364   81 HAFTEFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGYRKALRLMETAERFNMPIITF 160
Cdd:TIGR00513  78 LIFDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  161 IDTAGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIGVGDYVNMLQYSTYSVISPEGCASILWRD 240
Cdd:TIGR00513 158 IDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498122364  241 SDKAPQAAEAMGLVAPRLKELELIDEIIPEPLGGAHRDPVQTAQNMKDMLVKQLEELEQFDNEALLERRYQRLMSYGYC 319
Cdd:TIGR00513 238 ASKAPKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
AccA_sub NF041504
carboxyltransferase subunit alpha;
61-312 5.10e-156

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 436.50  E-value: 5.10e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  61 WQVAQLARHPQRPYTKDYLEHAFTEFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGY 140
Cdd:NF041504   1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 141 RKALRLMETAERFNMPIITFIDTAGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIGVGDYVNML 220
Cdd:NF041504  81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 221 QYSTYSVISPEGCASILWRDSDKAPQAAEAMGLVAPRLKELELIDEIIPEPLGGAHRDPVQTAQNMKDMLVKQLEELEQF 300
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGL 240

                        250
                 ....*....|..
gi 498122364 301 DNEALLERRYQR 312
Cdd:NF041504 241 SADELIAQRREK 252
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 5-151 7.26e-93

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: 271.97  E-value: 7.26e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364    5 FLEFEKPIAELEAKIEALRDVSRhggDAAVDLDKEIEQLEKKSLELKQKIFSDLGAWQVAQLARHPQRPYTKDYLEHAFT 84
Cdd:pfam03255   1 YLDFEKPIAELEAKIEELRKLAE---ESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFD 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498122364   85 EFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGYRKALRLMETAE 151
Cdd:pfam03255  78 DFIELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRLMKLAE 144
 
Name Accession Description Interval E-value
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 4-319 0e+00

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: 628.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364   4 NFLEFEKPIAELEAKIEALRDVSRhggDAAVDLDKEIEQLEKKSLELKQKIFSDLGAWQVAQLARHPQRPYTKDYLEHAF 83
Cdd:COG0825    1 NYLDFEKPIAELEAKIEELRALAE---ESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  84 TEFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGYRKALRLMETAERFNMPIITFIDT 163
Cdd:COG0825   78 TDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 164 AGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIGVGDYVNMLQYSTYSVISPEGCASILWRDSDK 243
Cdd:COG0825  158 PGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASK 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498122364 244 APQAAEAMGLVAPRLKELELIDEIIPEPLGGAHRDPVQTAQNMKDMLVKQLEELEQFDNEALLERRYQRLMSYGYC 319
Cdd:COG0825  238 APEAAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGRF 313
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 1-319 0e+00

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 624.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364   1 MSLNFLEFEKPIAELEAKIEALRDVSRhggDAAVDLDKEIEQLEKKSLELKQKIFSDLGAWQVAQLARHPQRPYTKDYLE 80
Cdd:PRK05724   1 MMLNYLDFEKPIAELEAKIEELRAVAE---DSDVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  81 HAFTEFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGYRKALRLMETAERFNMPIITF 160
Cdd:PRK05724  78 LLFTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIITF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 161 IDTAGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIGVGDYVNMLQYSTYSVISPEGCASILWRD 240
Cdd:PRK05724 158 IDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWKD 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498122364 241 SDKAPQAAEAMGLVAPRLKELELIDEIIPEPLGGAHRDPVQTAQNMKDMLVKQLEELEQFDNEALLERRYQRLMSYGYC 319
Cdd:PRK05724 238 ASKAPEAAEAMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAAALKEALLEALAELKGLSPEELLERRYEKFMSIGRF 316
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 1-319 0e+00

acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the alpha chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273113 [Multi-domain]  Cd Length: 316  Bit Score: 534.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364    1 MSLNFLEFEKPIAELEAKIEALRDVSRhggDAAVDLDKEIEQLEKKSLELKQKIFSDLGAWQVAQLARHPQRPYTKDYLE 80
Cdd:TIGR00513   1 MMANYLDFEKPIAELEAKIESLRARSR---DEDVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364   81 HAFTEFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGYRKALRLMETAERFNMPIITF 160
Cdd:TIGR00513  78 LIFDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  161 IDTAGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIGVGDYVNMLQYSTYSVISPEGCASILWRD 240
Cdd:TIGR00513 158 IDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498122364  241 SDKAPQAAEAMGLVAPRLKELELIDEIIPEPLGGAHRDPVQTAQNMKDMLVKQLEELEQFDNEALLERRYQRLMSYGYC 319
Cdd:TIGR00513 238 ASKAPKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
AccA_sub NF041504
carboxyltransferase subunit alpha;
61-312 5.10e-156

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 436.50  E-value: 5.10e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  61 WQVAQLARHPQRPYTKDYLEHAFTEFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGY 140
Cdd:NF041504   1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 141 RKALRLMETAERFNMPIITFIDTAGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIGVGDYVNML 220
Cdd:NF041504  81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 221 QYSTYSVISPEGCASILWRDSDKAPQAAEAMGLVAPRLKELELIDEIIPEPLGGAHRDPVQTAQNMKDMLVKQLEELEQF 300
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGL 240

                        250
                 ....*....|..
gi 498122364 301 DNEALLERRYQR 312
Cdd:NF041504 241 SADELIAQRREK 252
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 1-318 1.06e-128

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 369.91  E-value: 1.06e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364   1 MSLNFLEFEKPIAELEAKIEALrdvSRHGGDAAVDLDKEIEQLEKKSLELKQKIFSDLGAWQVAQLARHPQRPYTKDYLE 80
Cdd:CHL00198   4 RKPHVPDFMKPLAELESQVEEL---SKLAPKNDKVINNKLKSFQRKLRILKKEIFYSLTPLQRLHLVRQSERPTTLDYIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  81 HAFTEFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGYRKALRLMETAERFNMPIITF 160
Cdd:CHL00198  81 YILDEWIELHGDRGGSDDPALVGGIGKINGRTIVFLGHQRGRNTKENVLRNFGMPSPGGYRKALRLMKHANKFGLPILTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 161 IDTAGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIGVGDYVNMLQYSTYSVISPEGCASILWRD 240
Cdd:CHL00198 161 IDTPGAWAGVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALGIGIGDSIMMLEYAVYTVATPEACAAILWKD 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498122364 241 SDKAPQAAEAMGLVAPRLKELELIDEIIPEPLGGAHRDPVQTAQNMKDMLVKQLEELEQFDNEALLERRYQRLMSYGY 318
Cdd:CHL00198 241 SKKSLDAAEALKITSEDLKVLGIIDEIIPEPIGGAQADPASASKILKKKLIRQLDFLKILSPSELKAHRYEKFRKLGA 318
PLN03230 PLN03230
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
 6-317 1.04e-119

acetyl-coenzyme A carboxylase carboxyl transferase; Provisional


Pssm-ID: 178769 [Multi-domain]  Cd Length: 431  Bit Score: 351.17  E-value: 1.04e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364   6 LEFEKPIAELEAKIEALRDVSRHGGdaaVDLDKEIEQLEKKSLELKQKIFSDLGAWQVAQLARHPQRPYTKDYLEHAFTE 85
Cdd:PLN03230  76 LPFEKPIVDLENRIDEVRELANKTG---VDFSAQIAELEERYDQVRRELYSRLTPVQRLSVARHPNRPTFLDHVLNMTDK 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  86 FEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGYRKALRLMETAERFNMPIITFIDTAG 165
Cdd:PLN03230 153 WVELHGDRAGFDDPAIVCGIGSMEGMSFMFIGHQKGRNTKENIYRNFAMPQPNGYRKALRFMRHAEKFGFPILTFVDTPG 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 166 AYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIGVGDYVNMLQYSTYSVISPEGCASILWRDSDKAP 245
Cdd:PLN03230 233 AYAGIKAEELGQGEAIAFNLREMFGLRVPIIATVIGEGGSGGALAIGCGNRMLMMENAVYYVASPEACAAILWKSAAAAP 312

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498122364 246 QAAEAMGLVAPRLKELELIDEIIPEPLGGAHRDPVQTAQNMKDMLVKQLEELEQFDNEALLERRYQRLMSYG 317
Cdd:PLN03230 313 KAAEALRITAAELVKLGVVDEIVPEPLGGAHSDPLQASKNIKEVILRHMKELMKMDPEELLQDRAAKFRKIG 384
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 6-309 8.86e-102

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 315.26  E-value: 8.86e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364   6 LEFEKPIAELEAKIealRDVSRHGGDAAVDLDKEIEQLEKKSLELKQKIFSDLGAWQVAQLARHPQRPytkDYLEHAFT- 84
Cdd:PLN03229  97 LDFEKPLVDLEKKI---VDVRKMANETGLDFSDQIISLESKYQQALKDLYTHLTPIQRVNIARHPNRP---TFLDHIFNi 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  85 --EFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGYRKALRLMETAERFNMPIITFID 162
Cdd:PLN03229 171 tdKFVELHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGRNTKENIMRNFGMPTPHGYRKALRMMYYADHHGFPIVTFID 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 163 TAGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIGVGDYVNMLQYSTYSVISPEGCASILWRDSD 242
Cdd:PLN03229 251 TPGAYADLKSEELGQGEAIAHNLRTMFGLKVPIVSIVIGEGGSGGALAIGCANKLLMLENAVFYVASPEACAAILWKSAK 330

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498122364 243 KAPQAAEAMGLVAPRLKELELIDEIIPEPLGGAHRDPVQTAQNMKDMLVKQLEELEQFDNEALLERR 309
Cdd:PLN03229 331 AAPKAAEKLRITAQELCRLQIADGIIPEPLGGAHADPSWTSQQIKIAINENMDELGKMDTEELLKHR 397
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 62-316 1.71e-101

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 298.23  E-value: 1.71e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  62 QVAQLARHPQRPYTKDYLEHAFTEFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGYR 141
Cdd:PRK12319   6 RILKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAGQPVTVVGIQKGKNLQDNLKRNFGQPHPEGYR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 142 KALRLMETAERFNMPIITFIDTAGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIGVGDYVNMLQ 221
Cdd:PRK12319  86 KALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAVADQVWMLE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 222 YSTYSVISPEGCASILWRDSDKAPQAAEAMGLVAPRLKELELIDEIIPEpLGGAHRDPVQTaqnMKDMLVKQLEELEQFD 301
Cdd:PRK12319 166 NTMYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDKVIPE-HGYFSSEIIDM---IKKNLIEELAQLSQKP 241

                        250
                 ....*....|....*
gi 498122364 302 NEALLERRYQRLMSY 316
Cdd:PRK12319 242 LEQLLEERYQRFRKY 256
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 5-151 7.26e-93

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: 271.97  E-value: 7.26e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364    5 FLEFEKPIAELEAKIEALRDVSRhggDAAVDLDKEIEQLEKKSLELKQKIFSDLGAWQVAQLARHPQRPYTKDYLEHAFT 84
Cdd:pfam03255   1 YLDFEKPIAELEAKIEELRKLAE---ESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFD 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498122364   85 EFEEMAGDRAYADDKAIVGGMARLNGRPVMVIGHQKGRETKEKVIRNFGMPKPEGYRKALRLMETAE 151
Cdd:pfam03255  78 DFIELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRLMKLAE 144
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 85-269 2.07e-14

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: 73.45  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364   85 EFEEMAGDRAyaddKAIVGGMARLNGRPVMVIGHQKGRETkekvirnfGMPKPEGYRKALRLMETAERFNMPIITFIDTA 164
Cdd:pfam01039 270 EFFEIKPGYA----KTVVTGFARLGGIPVGVVANQPRVGA--------GVLFPDSADKAARFIRDCDAFNLPLVILADVP 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  165 GAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGALAIG----VGDYVNMLQYSTYSVISPEGCASILWRD 240
Cdd:pfam01039 338 GFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDskinGADINFAWPTARIAVMGPEGAVEIKFRK 417

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 498122364  241 SDKAPQ------AAEAMGLVAPRLKEL---------ELIDEIIP 269
Cdd:pfam01039 418 EKAAAEmrgkdlAATRKQKIAEYEEELsppyvaaarGFADAVID 461
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
85-282 1.88e-11

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 64.66  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  85 EFEEMAGDraYAddKAIVGGMARLNGRPVMVIGHQkgretkekvirnfgmPK-------PEGYRKALRLMETAERFNMPI 157
Cdd:COG4799  292 SFFEFKPL--YG--PNIVTGFARIDGRPVGIVANQ---------------PMvlagvldIDAADKAARFIRLCDAFNIPL 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364 158 ITFIDTAGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVGeGGSGGAL------AIGvGDYVNMLQYSTYSVISPE 231
Cdd:COG4799  353 VFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILR-KAYGAGYyamcgkALG-PDFLFAWPTAEIAVMGGE 430

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498122364 232 GCASILWR-DSDKAPQAAEAMglvAPRLKELE------------LIDEIIpeplggahrDPVQT 282
Cdd:COG4799  431 GAANVLYRrELAAAEDPEALR---AELIAEYEeqanpyyaaargWIDDVI---------DPRDT 482
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
83-208 4.76e-10

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 60.04  E-value: 4.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  83 FTEFEEMAGDRAYADDK-----AIVGGMARLNGRPVMVIGHQ---KGretkekvirnfGMPKPEGYRKALRLMETAERFN 154
Cdd:COG4799   49 FLELGALAGHRMYDDDDrvpgdGVVTGIGTVDGRPVVVVANDftvKG-----------GSLGPMTAKKILRAQDIALENG 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 498122364 155 MPIITFIDTAGAYPGVGAEERGQSEAIAKNLKVMAGLsVPVICNVVGEGGSGGA 208
Cdd:COG4799  118 LPVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGG-IPQISVIMGPCAAGGA 170
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 21-208 1.73e-06

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 49.42  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  21 ALRDVSRHGGDAAVDLDKEIEQLekkSLELKQKIFSDLGAWQVAQLARHPQR----PYTK-DYLEHA---FTEFEEMAGD 92
Cdd:PLN02820  31 VLPDGVDRNSDAFSANSKAMEGL---LSELRSHVAKVRAGGGPEAVKRHRSRnkllPRERiDRLLDPgspFLELSQLAGH 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  93 RAYADD---KAIVGGMARLNGRPVMVIGHQ---KGretkekvirnfGMPKPEGYRKALRLMETAERFNMPIITFIDTAGA 166
Cdd:PLN02820 108 ELYGEDlpsGGIVTGIGPVHGRLCMFVANDptvKG-----------GTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGA 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 498122364 167 YPGVGAE---ERGQSEAIAKNLKVMAGLSVPVICNVVGEGGSGGA 208
Cdd:PLN02820 177 NLPRQAEvfpDRDHFGRIFYNQARMSSAGIPQIALVLGSCTAGGA 221
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 83-277 2.20e-04

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: 42.63  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364   83 FTEFEEMAGDRAYAD------DKAIVGGMARLNGRPVMVIGHqkgretkEKVIRNfGMPKPEGYRKALRLMETAERFNMP 156
Cdd:pfam01039  23 FGELEDLFFHRATEFgrkripRDGVVTGSGAVIGRAVEVVAQ-------DFTVFG-GSLGPAKGEKILRAMEIAIKTGLP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  157 IITFIDTAGAYPGVGAEERGQSEAIAKNLKVMAGlSVPVICNVVGEGGSGGALAIGVGDYVNMLQYSTYsvispegcasi 236
Cdd:pfam01039  95 LIGINDSGGARIQEGVENLRGSGKIFGRNSLASG-VIPQISLIMGPCAGGGAYLPALGDFVIMVEGTSP----------- 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 498122364  237 lwrdsdkapqaaeaMGLVAPRLKELELIDEIIPEPLGGAHR 277
Cdd:pfam01039 163 --------------MFLTGPPVIKKVTGEEVTSEELGGATQ 189
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 83-208 8.50e-03

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 37.87  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498122364  83 FTEFEEMAGDrayaddkAIVGGMARLNGRPVMVIGhqkgretkekvirNFGMPKPEGYRKALRLMETAERFNMPIITFID 162
Cdd:PLN02820 350 FDEFKKNYGT-------TLVTGFARIYGQPVGIIG-------------NNGILFTESALKGAHFIELCAQRGIPLLFLQN 409

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 498122364 163 TAGAYPGVGAEERGQSEAIAKNLKVMAGLSVPVICNVVgeGGSGGA 208
Cdd:PLN02820 410 ITGFMVGSRSEASGIAKAGAKMVMAVACAKVPKITIIV--GGSFGA 453
 
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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