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Conserved domains on  [gi|1017634635|emb|CZY77551|]
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acetyl-CoA carboxylase carboxyltransferase subunit alpha [Enterobacter hormaechei]

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 1017634635   4 NFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAF 83
Cdd:COG0825     1 NYLDFEKPIAELEAKIEELRALAEES---GVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  84 DEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITFIDT 163
Cdd:COG0825    78 TDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 164 PGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADK 243
Cdd:COG0825   158 PGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1017634635 244 APLAAEAMGIIAPRLKELKLIDTVIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSTEDLLNRRYQRLMTYGY 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 1017634635   4 NFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAF 83
Cdd:COG0825     1 NYLDFEKPIAELEAKIEELRALAEES---GVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  84 DEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITFIDT 163
Cdd:COG0825    78 TDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 164 PGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADK 243
Cdd:COG0825   158 PGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1017634635 244 APLAAEAMGIIAPRLKELKLIDTVIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSTEDLLNRRYQRLMTYGY 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 1017634635   1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVR 80
Cdd:PRK05724    1 MMLNYLDFEKPIAELEAKIEELRAVAEDS---DVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  81 LAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITF 160
Cdd:PRK05724   78 LLFTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIITF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 161 IDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKS 240
Cdd:PRK05724  158 IDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWKD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1017634635 241 ADKAPLAAEAMGIIAPRLKELKLIDTVIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSTEDLLNRRYQRLMTYGY 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: 581.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635   1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVR 80
Cdd:TIGR00513   1 MMANYLDFEKPIAELEAKIESLRARSRDE---DVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  81 LAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITF 160
Cdd:TIGR00513  78 LIFDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 161 IDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKS 240
Cdd:TIGR00513 158 IDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1017634635 241 ADKAPLAAEAMGIIAPRLKELKLIDTVIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSTEDLLNRRYQRLMTYGYA 319
Cdd:TIGR00513 238 ASKAPKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
AccA_sub NF041504
carboxyltransferase subunit alpha;
61-312 1.13e-155

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 435.73  E-value: 1.13e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  61 WQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGY 140
Cdd:NF041504    1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 141 RKALRLMEMAERFNMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNML 220
Cdd:NF041504   81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 221 QYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDTVIPEPLGGAHRKPEVMAASLKAQLLADLADLDVL 300
Cdd:NF041504  161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGL 240

                         250
                  ....*....|..
gi 1017634635 301 STEDLLNRRYQR 312
Cdd:NF041504  241 SADELIAQRREK 252
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 5-151 4.15e-94

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: 275.44  E-value: 4.15e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635   5 FLDFEQPIAELEAKIDSLTAVSrqdEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFD 84
Cdd:pfam03255   1 YLDFEKPIAELEAKIEELRKLA---EESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFD 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1017634635  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 1017634635   4 NFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAF 83
Cdd:COG0825     1 NYLDFEKPIAELEAKIEELRALAEES---GVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  84 DEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITFIDT 163
Cdd:COG0825    78 TDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 164 PGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADK 243
Cdd:COG0825   158 PGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1017634635 244 APLAAEAMGIIAPRLKELKLIDTVIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSTEDLLNRRYQRLMTYGY 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 1017634635   1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVR 80
Cdd:PRK05724    1 MMLNYLDFEKPIAELEAKIEELRAVAEDS---DVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  81 LAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITF 160
Cdd:PRK05724   78 LLFTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIITF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 161 IDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKS 240
Cdd:PRK05724  158 IDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWKD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1017634635 241 ADKAPLAAEAMGIIAPRLKELKLIDTVIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSTEDLLNRRYQRLMTYGY 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: 581.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635   1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDeklDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVR 80
Cdd:TIGR00513   1 MMANYLDFEKPIAELEAKIESLRARSRDE---DVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  81 LAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITF 160
Cdd:TIGR00513  78 LIFDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 161 IDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKS 240
Cdd:TIGR00513 158 IDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1017634635 241 ADKAPLAAEAMGIIAPRLKELKLIDTVIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSTEDLLNRRYQRLMTYGYA 319
Cdd:TIGR00513 238 ASKAPKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
AccA_sub NF041504
carboxyltransferase subunit alpha;
61-312 1.13e-155

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 435.73  E-value: 1.13e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  61 WQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGY 140
Cdd:NF041504    1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 141 RKALRLMEMAERFNMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNML 220
Cdd:NF041504   81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 221 QYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDTVIPEPLGGAHRKPEVMAASLKAQLLADLADLDVL 300
Cdd:NF041504  161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGL 240

                         250
                  ....*....|..
gi 1017634635 301 STEDLLNRRYQR 312
Cdd:NF041504  241 SADELIAQRREK 252
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 1-318 1.32e-132

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 379.93  E-value: 1.32e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635   1 MSLNFLDFEQPIAELEAKIDSLtavSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVR 80
Cdd:CHL00198    4 RKPHVPDFMKPLAELESQVEEL---SKLAPKNDKVINNKLKSFQRKLRILKKEIFYSLTPLQRLHLVRQSERPTTLDYIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  81 LAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITF 160
Cdd:CHL00198   81 YILDEWIELHGDRGGSDDPALVGGIGKINGRTIVFLGHQRGRNTKENVLRNFGMPSPGGYRKALRLMKHANKFGLPILTF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 161 IDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKS 240
Cdd:CHL00198  161 IDTPGAWAGVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALGIGIGDSIMMLEYAVYTVATPEACAAILWKD 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1017634635 241 ADKAPLAAEAMGIIAPRLKELKLIDTVIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSTEDLLNRRYQRLMTYGY 318
Cdd:CHL00198  241 SKKSLDAAEALKITSEDLKVLGIIDEIIPEPIGGAQADPASASKILKKKLIRQLDFLKILSPSELKAHRYEKFRKLGA 318
PLN03230 PLN03230
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
 6-317 6.15e-119

acetyl-coenzyme A carboxylase carboxyl transferase; Provisional


Pssm-ID: 178769 [Multi-domain]  Cd Length: 431  Bit Score: 349.24  E-value: 6.15e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635   6 LDFEQPIAELEAKIDSLTAVSrqdEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDE 85
Cdd:PLN03230   76 LPFEKPIVDLENRIDEVRELA---NKTGVDFSAQIAELEERYDQVRRELYSRLTPVQRLSVARHPNRPTFLDHVLNMTDK 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  86 FDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITFIDTPG 165
Cdd:PLN03230  153 WVELHGDRAGFDDPAIVCGIGSMEGMSFMFIGHQKGRNTKENIYRNFAMPQPNGYRKALRFMRHAEKFGFPILTFVDTPG 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 166 AYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAP 245
Cdd:PLN03230  233 AYAGIKAEELGQGEAIAFNLREMFGLRVPIIATVIGEGGSGGALAIGCGNRMLMMENAVYYVASPEACAAILWKSAAAAP 312

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1017634635 246 LAAEAMGIIAPRLKELKLIDTVIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSTEDLLNRRYQRLMTYG 317
Cdd:PLN03230  313 KAAEALRITAAELVKLGVVDEIVPEPLGGAHSDPLQASKNIKEVILRHMKELMKMDPEELLQDRAAKFRKIG 384
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 62-316 1.11e-109

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 319.03  E-value: 1.11e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  62 QIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYR 141
Cdd:PRK12319    6 RILKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAGQPVTVVGIQKGKNLQDNLKRNFGQPHPEGYR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 142 KALRLMEMAERFNMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQ 221
Cdd:PRK12319   86 KALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAVADQVWMLE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 222 YSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDTVIPEPlggAHRKPEVMaASLKAQLLADLADLDVLS 301
Cdd:PRK12319  166 NTMYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDKVIPEH---GYFSSEII-DMIKKNLIEELAQLSQKP 241

                         250
                  ....*....|....*
gi 1017634635 302 TEDLLNRRYQRLMTY 316
Cdd:PRK12319  242 LEQLLEERYQRFRKY 256
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 6-309 5.44e-104

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 321.03  E-value: 5.44e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635   6 LDFEQPIAELEAKIdslTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDE 85
Cdd:PLN03229   97 LDFEKPLVDLEKKI---VDVRKMANETGLDFSDQIISLESKYQQALKDLYTHLTPIQRVNIARHPNRPTFLDHIFNITDK 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  86 FDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITFIDTPG 165
Cdd:PLN03229  174 FVELHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGRNTKENIMRNFGMPTPHGYRKALRMMYYADHHGFPIVTFIDTPG 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 166 AYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAP 245
Cdd:PLN03229  254 AYADLKSEELGQGEAIAHNLRTMFGLKVPIVSIVIGEGGSGGALAIGCANKLLMLENAVFYVASPEACAAILWKSAKAAP 333

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017634635 246 LAAEAMGIIAPRLKELKLIDTVIPEPLGGAHRKPEVMAASLKAQLLADLADLDVLSTEDLLNRR 309
Cdd:PLN03229  334 KAAEKLRITAQELCRLQIADGIIPEPLGGAHADPSWTSQQIKIAINENMDELGKMDTEELLKHR 397
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 5-151 4.15e-94

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: 275.44  E-value: 4.15e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635   5 FLDFEQPIAELEAKIDSLTAVSrqdEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFD 84
Cdd:pfam03255   1 YLDFEKPIAELEAKIEELRKLA---EESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFD 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1017634635  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 1.38e-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: 73.83  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  84 DEFDELAGDRAyaddKAIVGGIARLDGRPVMIIGHQKGRETkekirrnfGMPAPEGYRKALRLMEMAERFNMPIITFIDT 163
Cdd:pfam01039 269 GEFFEIKPGYA----KTVVTGFARLGGIPVGVVANQPRVGA--------GVLFPDSADKAARFIRDCDAFNLPLVILADV 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 164 PGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIG----VGDKVNMLQYSTYSVISPEGCASILWK 239
Cdd:pfam01039 337 PGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDskinGADINFAWPTARIAVMGPEGAVEIKFR 416

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1017634635 240 SADKA------PLAAEAMGIIAPRLKELKLI 264
Cdd:pfam01039 417 KEKAAaemrgkDLAATRKQKIAEYEEELSPP 447
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
83-208 5.30e-12

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 66.20  E-value: 5.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  83 FDEFDELAGDRAYADDK-----AIVGGIARLDGRPVMIIGHQ---KGretkekirrnfGMPAPEGYRKALRLMEMAERFN 154
Cdd:COG4799    49 FLELGALAGHRMYDDDDrvpgdGVVTGIGTVDGRPVVVVANDftvKG-----------GSLGPMTAKKILRAQDIALENG 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1017634635 155 MPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLkVPVICTVIGEGGSGGA 208
Cdd:COG4799   118 LPVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGG-IPQISVIMGPCAAGGA 170
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
84-208 1.47e-11

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 64.66  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  84 DEFDELAGDraYAddKAIVGGIARLDGRPVMIIGHQKGRetkekirrNFGMPAPEGYRKALRLMEMAERFNMPIITFIDT 163
Cdd:COG4799   291 GSFFEFKPL--YG--PNIVTGFARIDGRPVGIVANQPMV--------LAGVLDIDAADKAARFIRLCDAFNIPLVFLVDV 358

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1017634635 164 PGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGeGGSGGA 208
Cdd:COG4799   359 PGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILR-KAYGAG 402
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 49-221 4.91e-08

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 54.04  E-value: 4.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  49 ELTRKIFADLGAwqiAQLARHPQRPYTLDYVRL--------AFDEFDELAGDRAYADD---KAIVGGIARLDGRPVMIIG 117
Cdd:PLN02820   59 SHVAKVRAGGGP---EAVKRHRSRNKLLPRERIdrlldpgsPFLELSQLAGHELYGEDlpsGGIVTGIGPVHGRLCMFVA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 118 HQ---KGretkekirrnfGMPAPEGYRKALRLMEMAERFNMPIITFIDTPGAYPGVGAE---ERGQSEAIARNLREMSRL 191
Cdd:PLN02820  136 NDptvKG-----------GTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEvfpDRDHFGRIFYNQARMSSA 204

                         170       180       190
                  ....*....|....*....|....*....|
gi 1017634635 192 KVPVICTVIGEGGSGGALAIGVGDKVNMLQ 221
Cdd:PLN02820  205 GIPQIALVLGSCTAGGAYVPAMADESVIVK 234
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 83-277 3.33e-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: 45.33  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635  83 FDEFDELAGDRAYAD------DKAIVGGIARLDGRPVMIIGHQKgreTKekirrnFGMPAPEGY-RKALRLMEMAERFNM 155
Cdd:pfam01039  23 FGELEDLFFHRATEFgrkripRDGVVTGSGAVIGRAVEVVAQDF---TV------FGGSLGPAKgEKILRAMEIAIKTGL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017634635 156 PIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRlKVPVICTVIGEGGSGGALAIGVGDKVNMLqystysvispegcas 235
Cdd:pfam01039  94 PLIGINDSGGARIQEGVENLRGSGKIFGRNSLASG-VIPQISLIMGPCAGGGAYLPALGDFVIMV--------------- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1017634635 236 ilwksADKAPlaaeaMGIIAPRLKELKLIDTVIPEPLGGAHR 277
Cdd:pfam01039 158 -----EGTSP-----MFLTGPPVIKKVTGEEVTSEELGGATQ 189
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 1017634635  83 FDEFDELAGDrayaddkAIVGGIARLDGRPVMIIGhqkgretkekirrNFGMPAPEGYRKALRLMEMAERFNMPIITFID 162
Cdd:PLN02820  350 FDEFKKNYGT-------TLVTGFARIYGQPVGIIG-------------NNGILFTESALKGAHFIELCAQRGIPLLFLQN 409

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1017634635 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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