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Conserved domains on  [gi|556425539|ref|WP_023310466|]
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MULTISPECIES: acetyl-CoA carboxylase carboxyl transferase subunit alpha [Enterobacter]

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 ...
 4-318 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: 637.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539   4 NFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQVAQLARHPQRPYTLDYVRLAF 83
Cdd:COG0825    1 NYLDFEKPIAELEAKIEELRALAEES---GVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  84 DEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITFIDT 163
Cdd:COG0825   78 TDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 164 PGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADK 243
Cdd:COG0825  158 PGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASK 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556425539 244 APLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSKDDLLNRRYQRLMTYGY 318
Cdd:COG0825  238 APEAAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGR 312
 
Name Accession Description Interval E-value
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 4-318 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: 637.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539   4 NFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQVAQLARHPQRPYTLDYVRLAF 83
Cdd:COG0825    1 NYLDFEKPIAELEAKIEELRALAEES---GVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  84 DEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITFIDT 163
Cdd:COG0825   78 TDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 164 PGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADK 243
Cdd:COG0825  158 PGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASK 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556425539 244 APLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSKDDLLNRRYQRLMTYGY 318
Cdd:COG0825  238 APEAAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGR 312
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 1-318 0e+00

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 636.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539   1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQVAQLARHPQRPYTLDYVR 80
Cdd:PRK05724   1 MMLNYLDFEKPIAELEAKIEELRAVAEDS---DVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  81 LAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITF 160
Cdd:PRK05724  78 LLFTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIITF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 161 IDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKS 240
Cdd:PRK05724 158 IDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWKD 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556425539 241 ADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSKDDLLNRRYQRLMTYGY 318
Cdd:PRK05724 238 ASKAPEAAEAMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAAALKEALLEALAELKGLSPEELLERRYEKFMSIGR 315
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: 581.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539    1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQVAQLARHPQRPYTLDYVR 80
Cdd:TIGR00513   1 MMANYLDFEKPIAELEAKIESLRARSRDE---DVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539   81 LAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITF 160
Cdd:TIGR00513  78 LIFDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  161 IDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKS 240
Cdd:TIGR00513 158 IDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556425539  241 ADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSKDDLLNRRYQRLMTYGYA 319
Cdd:TIGR00513 238 ASKAPKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
AccA_sub NF041504
carboxyltransferase subunit alpha;
61-312 6.85e-156

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 436.12  E-value: 6.85e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  61 WQVAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGY 140
Cdd:NF041504   1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 141 RKALRLMEMAERFNMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNML 220
Cdd:NF041504  81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 221 QYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRKPEVMAASLKAQLLADLADLDVL 300
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGL 240

                        250
                 ....*....|..
gi 556425539 301 SKDDLLNRRYQR 312
Cdd:NF041504 241 SADELIAQRREK 252
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 5-151 1.34e-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: 273.90  E-value: 1.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539    5 FLDFEQPIAELEAKIDSLTAVSrqdEKLDINIDEEVHRLREKSVELTRKIFADLGAWQVAQLARHPQRPYTLDYVRLAFD 84
Cdd:pfam03255   1 YLDFEKPIAELEAKIEELRKLA---EESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFD 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556425539   85 EFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAE 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 ...
 4-318 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: 637.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539   4 NFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQVAQLARHPQRPYTLDYVRLAF 83
Cdd:COG0825    1 NYLDFEKPIAELEAKIEELRALAEES---GVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  84 DEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITFIDT 163
Cdd:COG0825   78 TDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 164 PGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADK 243
Cdd:COG0825  158 PGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASK 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556425539 244 APLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSKDDLLNRRYQRLMTYGY 318
Cdd:COG0825  238 APEAAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGR 312
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 1-318 0e+00

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 636.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539   1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQVAQLARHPQRPYTLDYVR 80
Cdd:PRK05724   1 MMLNYLDFEKPIAELEAKIEELRAVAEDS---DVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  81 LAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITF 160
Cdd:PRK05724  78 LLFTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIITF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 161 IDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKS 240
Cdd:PRK05724 158 IDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWKD 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556425539 241 ADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSKDDLLNRRYQRLMTYGY 318
Cdd:PRK05724 238 ASKAPEAAEAMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAAALKEALLEALAELKGLSPEELLERRYEKFMSIGR 315
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: 581.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539    1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQVAQLARHPQRPYTLDYVR 80
Cdd:TIGR00513   1 MMANYLDFEKPIAELEAKIESLRARSRDE---DVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539   81 LAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITF 160
Cdd:TIGR00513  78 LIFDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  161 IDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKS 240
Cdd:TIGR00513 158 IDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556425539  241 ADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSKDDLLNRRYQRLMTYGYA 319
Cdd:TIGR00513 238 ASKAPKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
AccA_sub NF041504
carboxyltransferase subunit alpha;
61-312 6.85e-156

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 436.12  E-value: 6.85e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  61 WQVAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGY 140
Cdd:NF041504   1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 141 RKALRLMEMAERFNMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNML 220
Cdd:NF041504  81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 221 QYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRKPEVMAASLKAQLLADLADLDVL 300
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGL 240

                        250
                 ....*....|..
gi 556425539 301 SKDDLLNRRYQR 312
Cdd:NF041504 241 SADELIAQRREK 252
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 1-318 2.15e-133

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 381.85  E-value: 2.15e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539   1 MSLNFLDFEQPIAELEAKIDSLtavSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQVAQLARHPQRPYTLDYVR 80
Cdd:CHL00198   4 RKPHVPDFMKPLAELESQVEEL---SKLAPKNDKVINNKLKSFQRKLRILKKEIFYSLTPLQRLHLVRQSERPTTLDYIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  81 LAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITF 160
Cdd:CHL00198  81 YILDEWIELHGDRGGSDDPALVGGIGKINGRTIVFLGHQRGRNTKENVLRNFGMPSPGGYRKALRLMKHANKFGLPILTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 161 IDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKS 240
Cdd:CHL00198 161 IDTPGAWAGVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALGIGIGDSIMMLEYAVYTVATPEACAAILWKD 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556425539 241 ADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSKDDLLNRRYQRLMTYGY 318
Cdd:CHL00198 241 SKKSLDAAEALKITSEDLKVLGIIDEIIPEPIGGAQADPASASKILKKKLIRQLDFLKILSPSELKAHRYEKFRKLGA 318
PLN03230 PLN03230
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
 6-317 3.01e-118

acetyl-coenzyme A carboxylase carboxyl transferase; Provisional


Pssm-ID: 178769 [Multi-domain]  Cd Length: 431  Bit Score: 347.31  E-value: 3.01e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539   6 LDFEQPIAELEAKIDSLTAVSrqdEKLDINIDEEVHRLREKSVELTRKIFADLGAWQVAQLARHPQRPYTLDYVRLAFDE 85
Cdd:PLN03230  76 LPFEKPIVDLENRIDEVRELA---NKTGVDFSAQIAELEERYDQVRRELYSRLTPVQRLSVARHPNRPTFLDHVLNMTDK 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  86 FDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITFIDTPG 165
Cdd:PLN03230 153 WVELHGDRAGFDDPAIVCGIGSMEGMSFMFIGHQKGRNTKENIYRNFAMPQPNGYRKALRFMRHAEKFGFPILTFVDTPG 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 166 AYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAP 245
Cdd:PLN03230 233 AYAGIKAEELGQGEAIAFNLREMFGLRVPIIATVIGEGGSGGALAIGCGNRMLMMENAVYYVASPEACAAILWKSAAAAP 312

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556425539 246 LAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSKDDLLNRRYQRLMTYG 317
Cdd:PLN03230 313 KAAEALRITAAELVKLGVVDEIVPEPLGGAHSDPLQASKNIKEVILRHMKELMKMDPEELLQDRAAKFRKIG 384
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 62-316 8.77e-108

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 314.41  E-value: 8.77e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  62 QVAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYR 141
Cdd:PRK12319   6 RILKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAGQPVTVVGIQKGKNLQDNLKRNFGQPHPEGYR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 142 KALRLMEMAERFNMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQ 221
Cdd:PRK12319  86 KALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAVADQVWMLE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 222 YSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPlggAHRKPEVMaASLKAQLLADLADLDVLS 301
Cdd:PRK12319 166 NTMYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDKVIPEH---GYFSSEII-DMIKKNLIEELAQLSQKP 241

                        250
                 ....*....|....*
gi 556425539 302 KDDLLNRRYQRLMTY 316
Cdd:PRK12319 242 LEQLLEERYQRFRKY 256
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 6-309 3.59e-103

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 318.72  E-value: 3.59e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539   6 LDFEQPIAELEAKIdslTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQVAQLARHPQRPYTLDYVRLAFDE 85
Cdd:PLN03229  97 LDFEKPLVDLEKKI---VDVRKMANETGLDFSDQIISLESKYQQALKDLYTHLTPIQRVNIARHPNRPTFLDHIFNITDK 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  86 FDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITFIDTPG 165
Cdd:PLN03229 174 FVELHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGRNTKENIMRNFGMPTPHGYRKALRMMYYADHHGFPIVTFIDTPG 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 166 AYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAP 245
Cdd:PLN03229 254 AYADLKSEELGQGEAIAHNLRTMFGLKVPIVSIVIGEGGSGGALAIGCANKLLMLENAVFYVASPEACAAILWKSAKAAP 333

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556425539 246 LAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSKDDLLNRR 309
Cdd:PLN03229 334 KAAEKLRITAQELCRLQIADGIIPEPLGGAHADPSWTSQQIKIAINENMDELGKMDTEELLKHR 397
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 5-151 1.34e-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: 273.90  E-value: 1.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539    5 FLDFEQPIAELEAKIDSLTAVSrqdEKLDINIDEEVHRLREKSVELTRKIFADLGAWQVAQLARHPQRPYTLDYVRLAFD 84
Cdd:pfam03255   1 YLDFEKPIAELEAKIEELRKLA---EESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFD 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556425539   85 EFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAE 151
Cdd:pfam03255  78 DFIELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRLMKLAE 144
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 84-264 1.33e-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: 74.22  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539   84 DEFDELAGDRAyaddKAIVGGIARLDGRPVMIIGHQKGRETkekirrnfGMPAPEGYRKALRLMEMAERFNMPIITFIDT 163
Cdd:pfam01039 269 GEFFEIKPGYA----KTVVTGFARLGGIPVGVVANQPRVGA--------GVLFPDSADKAARFIRDCDAFNLPLVILADV 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  164 PGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIG----VGDKVNMLQYSTYSVISPEGCASILWK 239
Cdd:pfam01039 337 PGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDskinGADINFAWPTARIAVMGPEGAVEIKFR 416

                         170       180       190
                  ....*....|....*....|....*....|.
gi 556425539  240 SADKA------PLAAEAMGIIAPRLKELKLI 264
Cdd:pfam01039 417 KEKAAaemrgkDLAATRKQKIAEYEEELSPP 447
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
83-208 5.25e-12

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 66.20  E-value: 5.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  83 FDEFDELAGDRAYADDK-----AIVGGIARLDGRPVMIIGHQ---KGretkekirrnfGMPAPEGYRKALRLMEMAERFN 154
Cdd:COG4799   49 FLELGALAGHRMYDDDDrvpgdGVVTGIGTVDGRPVVVVANDftvKG-----------GSLGPMTAKKILRAQDIALENG 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 556425539 155 MPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLkVPVICTVIGEGGSGGA 208
Cdd:COG4799  118 LPVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGG-IPQISVIMGPCAAGGA 170
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
84-208 1.46e-11

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 64.66  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  84 DEFDELAGDraYAddKAIVGGIARLDGRPVMIIGHQKGRetkekirrNFGMPAPEGYRKALRLMEMAERFNMPIITFIDT 163
Cdd:COG4799  291 GSFFEFKPL--YG--PNIVTGFARIDGRPVGIVANQPMV--------LAGVLDIDAADKAARFIRLCDAFNIPLVFLVDV 358

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 556425539 164 PGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGeGGSGGA 208
Cdd:COG4799  359 PGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILR-KAYGAG 402
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 49-221 4.83e-08

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 54.04  E-value: 4.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  49 ELTRKIFADLGAWQVAqlaRHPQRPYTLDYVRL--------AFDEFDELAGDRAYADD---KAIVGGIARLDGRPVMIIG 117
Cdd:PLN02820  59 SHVAKVRAGGGPEAVK---RHRSRNKLLPRERIdrlldpgsPFLELSQLAGHELYGEDlpsGGIVTGIGPVHGRLCMFVA 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539 118 HQ---KGretkekirrnfGMPAPEGYRKALRLMEMAERFNMPIITFIDTPGAYPGVGAE---ERGQSEAIARNLREMSRL 191
Cdd:PLN02820 136 NDptvKG-----------GTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEvfpDRDHFGRIFYNQARMSSA 204

                        170       180       190
                 ....*....|....*....|....*....|
gi 556425539 192 KVPVICTVIGEGGSGGALAIGVGDKVNMLQ 221
Cdd:PLN02820 205 GIPQIALVLGSCTAGGAYVPAMADESVIVK 234
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 83-219 3.74e-05

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: 44.94  E-value: 3.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539   83 FDEFDELAGDRAYAD------DKAIVGGIARLDGRPVMIIGHQKgreTKekirrnFGMPAPEGY-RKALRLMEMAERFNM 155
Cdd:pfam01039  23 FGELEDLFFHRATEFgrkripRDGVVTGSGAVIGRAVEVVAQDF---TV------FGGSLGPAKgEKILRAMEIAIKTGL 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556425539  156 PIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRlKVPVICTVIGEGGSGGALAIGVGDKVNM 219
Cdd:pfam01039  94 PLIGINDSGGARIQEGVENLRGSGKIFGRNSLASG-VIPQISLIMGPCAGGGAYLPALGDFVIM 156
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 83-208 1.15e-04

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 43.64  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425539  83 FDEFDELAGDrayaddkAIVGGIARLDGRPVMIIGhqkgretkekirrNFGMPAPEGYRKALRLMEMAERFNMPIITFID 162
Cdd:PLN02820 350 FDEFKKNYGT-------TLVTGFARIYGQPVGIIG-------------NNGILFTESALKGAHFIELCAQRGIPLLFLQN 409

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 556425539 163 TPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIgeGGSGGA 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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