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Conserved domains on  [gi|502035729|ref|WP_012702398|]
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MULTISPECIES: acetyl-CoA carboxylase carboxyltransferase subunit alpha [Azotobacter]

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 ...
 4-315 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: 617.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729   4 NFLDFEQPIADLQAKIEELRLVGDDNALNISDEISRLQDKSHALTASIFGNLTSWQIAQLARHPRRPYTLDYLEHIFTEF 83
Cdd:COG0825    1 NYLDFEKPIAELEAKIEELRALAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIFTDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  84 EELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGYRKACRLMEMAERFKLPILTFIDTPGA 163
Cdd:COG0825   81 IELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDTPGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 164 YPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIGVCDRLNMLQYSTYAVISPEGCASILWRTAEKAAD 243
Cdd:COG0825  161 YPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASKAPE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502035729 244 AAEAMGITAARLRELGIVDEVIGEPLGGAHRNPAATAESVRQTLLAQLESLRGLDADSLLEQRYERLMSYGR 315
Cdd:COG0825  241 AAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGR 312
 
Name Accession Description Interval E-value
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 4-315 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: 617.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729   4 NFLDFEQPIADLQAKIEELRLVGDDNALNISDEISRLQDKSHALTASIFGNLTSWQIAQLARHPRRPYTLDYLEHIFTEF 83
Cdd:COG0825    1 NYLDFEKPIAELEAKIEELRALAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIFTDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  84 EELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGYRKACRLMEMAERFKLPILTFIDTPGA 163
Cdd:COG0825   81 IELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDTPGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 164 YPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIGVCDRLNMLQYSTYAVISPEGCASILWRTAEKAAD 243
Cdd:COG0825  161 YPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASKAPE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502035729 244 AAEAMGITAARLRELGIVDEVIGEPLGGAHRNPAATAESVRQTLLAQLESLRGLDADSLLEQRYERLMSYGR 315
Cdd:COG0825  241 AAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGR 312
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 1-315 0e+00

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 615.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729   1 MNPNFLDFEQPIADLQAKIEELRLVGDDNALNISDEISRLQDKSHALTASIFGNLTSWQIAQLARHPRRPYTLDYLEHIF 80
Cdd:PRK05724   1 MMLNYLDFEKPIAELEAKIEELRAVAEDSDVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIELLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  81 TEFEELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGYRKACRLMEMAERFKLPILTFIDT 160
Cdd:PRK05724  81 TDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIITFIDT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 161 PGAYPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIGVCDRLNMLQYSTYAVISPEGCASILWRTAEK 240
Cdd:PRK05724 161 PGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWKDASK 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502035729 241 AADAAEAMGITAARLRELGIVDEVIGEPLGGAHRNPAATAESVRQTLLAQLESLRGLDADSLLEQRYERLMSYGR 315
Cdd:PRK05724 241 APEAAEAMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAAALKEALLEALAELKGLSPEELLERRYEKFMSIGR 315
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 1-316 2.06e-180

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: 500.49  E-value: 2.06e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729    1 MNPNFLDFEQPIADLQAKIEELRLVGDDNALNISDEISRLQDKSHALTASIFGNLTSWQIAQLARHPRRPYTLDYLEHIF 80
Cdd:TIGR00513   1 MMANYLDFEKPIAELEAKIESLRARSRDEDVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIELIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729   81 TEFEELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGYRKACRLMEMAERFKLPILTFIDT 160
Cdd:TIGR00513  81 DDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITFIDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  161 PGAYPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIGVCDRLNMLQYSTYAVISPEGCASILWRTAEK 240
Cdd:TIGR00513 161 PGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKDASK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502035729  241 AADAAEAMGITAARLRELGIVDEVIGEPLGGAHRNPAATAESVRQTLLAQLESLRGLDADSLLEQRYERLMSYGRA 316
Cdd:TIGR00513 241 APKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
AccA_sub NF041504
carboxyltransferase subunit alpha;
58-309 7.14e-149

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 418.40  E-value: 7.14e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  58 WQIAQLARHPRRPYTLDYLEHIFTEFEELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGY 137
Cdd:NF041504   1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 138 RKACRLMEMAERFKLPILTFIDTPGAYPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIGVCDRLNML 217
Cdd:NF041504  81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 218 QYSTYAVISPEGCASILWRTAEKAADAAEAMGITAARLRELGIVDEVIGEPLGGAHRNPAATAESVRQTLLAQLESLRGL 297
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGL 240

                        250
                 ....*....|..
gi 502035729 298 DADSLLEQRYER 309
Cdd:NF041504 241 SADELIAQRREK 252
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 5-148 1.78e-98

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: 286.22  E-value: 1.78e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729    5 FLDFEQPIADLQAKIEELRLVGDDNALNISDEISRLQDKSHALTASIFGNLTSWQIAQLARHPRRPYTLDYLEHIFTEFE 84
Cdd:pfam03255   1 YLDFEKPIAELEAKIEELRKLAEESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFDDFI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502035729   85 ELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGYRKACRLMEMAE 148
Cdd:pfam03255  81 ELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRLMKLAE 144
 
Name Accession Description Interval E-value
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 4-315 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: 617.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729   4 NFLDFEQPIADLQAKIEELRLVGDDNALNISDEISRLQDKSHALTASIFGNLTSWQIAQLARHPRRPYTLDYLEHIFTEF 83
Cdd:COG0825    1 NYLDFEKPIAELEAKIEELRALAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIFTDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  84 EELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGYRKACRLMEMAERFKLPILTFIDTPGA 163
Cdd:COG0825   81 IELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDTPGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 164 YPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIGVCDRLNMLQYSTYAVISPEGCASILWRTAEKAAD 243
Cdd:COG0825  161 YPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASKAPE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502035729 244 AAEAMGITAARLRELGIVDEVIGEPLGGAHRNPAATAESVRQTLLAQLESLRGLDADSLLEQRYERLMSYGR 315
Cdd:COG0825  241 AAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGR 312
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 1-315 0e+00

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 615.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729   1 MNPNFLDFEQPIADLQAKIEELRLVGDDNALNISDEISRLQDKSHALTASIFGNLTSWQIAQLARHPRRPYTLDYLEHIF 80
Cdd:PRK05724   1 MMLNYLDFEKPIAELEAKIEELRAVAEDSDVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIELLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  81 TEFEELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGYRKACRLMEMAERFKLPILTFIDT 160
Cdd:PRK05724  81 TDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIITFIDT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 161 PGAYPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIGVCDRLNMLQYSTYAVISPEGCASILWRTAEK 240
Cdd:PRK05724 161 PGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWKDASK 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502035729 241 AADAAEAMGITAARLRELGIVDEVIGEPLGGAHRNPAATAESVRQTLLAQLESLRGLDADSLLEQRYERLMSYGR 315
Cdd:PRK05724 241 APEAAEAMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAAALKEALLEALAELKGLSPEELLERRYEKFMSIGR 315
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 1-316 2.06e-180

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: 500.49  E-value: 2.06e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729    1 MNPNFLDFEQPIADLQAKIEELRLVGDDNALNISDEISRLQDKSHALTASIFGNLTSWQIAQLARHPRRPYTLDYLEHIF 80
Cdd:TIGR00513   1 MMANYLDFEKPIAELEAKIESLRARSRDEDVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIELIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729   81 TEFEELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGYRKACRLMEMAERFKLPILTFIDT 160
Cdd:TIGR00513  81 DDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITFIDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  161 PGAYPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIGVCDRLNMLQYSTYAVISPEGCASILWRTAEK 240
Cdd:TIGR00513 161 PGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKDASK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502035729  241 AADAAEAMGITAARLRELGIVDEVIGEPLGGAHRNPAATAESVRQTLLAQLESLRGLDADSLLEQRYERLMSYGRA 316
Cdd:TIGR00513 241 APKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
AccA_sub NF041504
carboxyltransferase subunit alpha;
58-309 7.14e-149

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 418.40  E-value: 7.14e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  58 WQIAQLARHPRRPYTLDYLEHIFTEFEELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGY 137
Cdd:NF041504   1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 138 RKACRLMEMAERFKLPILTFIDTPGAYPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIGVCDRLNML 217
Cdd:NF041504  81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 218 QYSTYAVISPEGCASILWRTAEKAADAAEAMGITAARLRELGIVDEVIGEPLGGAHRNPAATAESVRQTLLAQLESLRGL 297
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGL 240

                        250
                 ....*....|..
gi 502035729 298 DADSLLEQRYER 309
Cdd:NF041504 241 SADELIAQRREK 252
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 1-314 2.61e-125

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 361.05  E-value: 2.61e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729   1 MNPNFLDFEQPIADLQAKIEELRLVGDDNALNISDEISRLQDKSHALTASIFGNLTSWQIAQLARHPRRPYTLDYLEHIF 80
Cdd:CHL00198   4 RKPHVPDFMKPLAELESQVEELSKLAPKNDKVINNKLKSFQRKLRILKKEIFYSLTPLQRLHLVRQSERPTTLDYIPYIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  81 TEFEELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGYRKACRLMEMAERFKLPILTFIDT 160
Cdd:CHL00198  84 DEWIELHGDRGGSDDPALVGGIGKINGRTIVFLGHQRGRNTKENVLRNFGMPSPGGYRKALRLMKHANKFGLPILTFIDT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 161 PGAYPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIGVCDRLNMLQYSTYAVISPEGCASILWRTAEK 240
Cdd:CHL00198 164 PGAWAGVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALGIGIGDSIMMLEYAVYTVATPEACAAILWKDSKK 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502035729 241 AADAAEAMGITAARLRELGIVDEVIGEPLGGAHRNPAATAESVRQTLLAQLESLRGLDADSLLEQRYERLMSYG 314
Cdd:CHL00198 244 SLDAAEALKITSEDLKVLGIIDEIIPEPIGGAQADPASASKILKKKLIRQLDFLKILSPSELKAHRYEKFRKLG 317
PLN03230 PLN03230
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
 3-314 2.94e-120

acetyl-coenzyme A carboxylase carboxyl transferase; Provisional


Pssm-ID: 178769 [Multi-domain]  Cd Length: 431  Bit Score: 352.32  E-value: 2.94e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729   3 PNFLDFEQPIADLQAKIEELRLVGDDNALNISDEISRLQDKSHALTASIFGNLTSWQIAQLARHPRRPYTLDYLEHIFTE 82
Cdd:PLN03230  73 PVTLPFEKPIVDLENRIDEVRELANKTGVDFSAQIAELEERYDQVRRELYSRLTPVQRLSVARHPNRPTFLDHVLNMTDK 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  83 FEELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGYRKACRLMEMAERFKLPILTFIDTPG 162
Cdd:PLN03230 153 WVELHGDRAGFDDPAIVCGIGSMEGMSFMFIGHQKGRNTKENIYRNFAMPQPNGYRKALRFMRHAEKFGFPILTFVDTPG 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 163 AYPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIGVCDRLNMLQYSTYAVISPEGCASILWRTAEKAA 242
Cdd:PLN03230 233 AYAGIKAEELGQGEAIAFNLREMFGLRVPIIATVIGEGGSGGALAIGCGNRMLMMENAVYYVASPEACAAILWKSAAAAP 312

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502035729 243 DAAEAMGITAARLRELGIVDEVIGEPLGGAHRNPAATAESVRQTLLAQLESLRGLDADSLLEQRYERLMSYG 314
Cdd:PLN03230 313 KAAEALRITAAELVKLGVVDEIVPEPLGGAHSDPLQASKNIKEVILRHMKELMKMDPEELLQDRAAKFRKIG 384
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 3-306 5.84e-104

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 320.65  E-value: 5.84e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729   3 PNFLDFEQPIADLQAKIEELRLVGDDNALNISDEISRLQDKSHALTASIFGNLTSWQIAQLARHPRRPYTLDYLEHIFTE 82
Cdd:PLN03229  94 PVTLDFEKPLVDLEKKIVDVRKMANETGLDFSDQIISLESKYQQALKDLYTHLTPIQRVNIARHPNRPTFLDHIFNITDK 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  83 FEELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGYRKACRLMEMAERFKLPILTFIDTPG 162
Cdd:PLN03229 174 FVELHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGRNTKENIMRNFGMPTPHGYRKALRMMYYADHHGFPIVTFIDTPG 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 163 AYPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIGVCDRLNMLQYSTYAVISPEGCASILWRTAEKAA 242
Cdd:PLN03229 254 AYADLKSEELGQGEAIAHNLRTMFGLKVPIVSIVIGEGGSGGALAIGCANKLLMLENAVFYVASPEACAAILWKSAKAAP 333

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502035729 243 DAAEAMGITAARLRELGIVDEVIGEPLGGAHRNPAATAESVRQTLLAQLESLRGLDADSLLEQR 306
Cdd:PLN03229 334 KAAEKLRITAQELCRLQIADGIIPEPLGGAHADPSWTSQQIKIAINENMDELGKMDTEELLKHR 397
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 59-313 3.33e-101

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 297.46  E-value: 3.33e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  59 QIAQLARHPRRPYTLDYLEHIFTEFEELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGYR 138
Cdd:PRK12319   6 RILKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAGQPVTVVGIQKGKNLQDNLKRNFGQPHPEGYR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 139 KACRLMEMAERFKLPILTFIDTPGAYPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIGVCDRLNMLQ 218
Cdd:PRK12319  86 KALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAVADQVWMLE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 219 YSTYAVISPEGCASILWRTAEKAADAAEAMGITAARLRELGIVDEVIGEplggAHRNPAATAESVRQTLLAQLESLRGLD 298
Cdd:PRK12319 166 NTMYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDKVIPE----HGYFSSEIIDMIKKNLIEELAQLSQKP 241

                        250
                 ....*....|....*
gi 502035729 299 ADSLLEQRYERLMSY 313
Cdd:PRK12319 242 LEQLLEERYQRFRKY 256
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 5-148 1.78e-98

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: 286.22  E-value: 1.78e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729    5 FLDFEQPIADLQAKIEELRLVGDDNALNISDEISRLQDKSHALTASIFGNLTSWQIAQLARHPRRPYTLDYLEHIFTEFE 84
Cdd:pfam03255   1 YLDFEKPIAELEAKIEELRKLAEESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFDDFI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502035729   85 ELHGDRHFTDDAAIVGGVARLDDQPVMVIGHQKGRDVREKVRRNFGMPRPEGYRKACRLMEMAE 148
Cdd:pfam03255  81 ELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRLMKLAE 144
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 82-236 4.56e-11

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: 63.43  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729   82 EFEELHGDRHFTddaaIVGGVARLDDQPVMVIGHQKgrdvrekvRRNFGMPRPEGYRKACRLMEMAERFKLPILTFIDTP 161
Cdd:pfam01039 270 EFFEIKPGYAKT----VVTGFARLGGIPVGVVANQP--------RVGAGVLFPDSADKAARFIRDCDAFNLPLVILADVP 337

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502035729  162 GAYPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGALAIG----VCDRLNMLQYSTYAVISPEGCASILWR 236
Cdd:pfam01039 338 GFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDskinGADINFAWPTARIAVMGPEGAVEIKFR 416
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
67-236 2.04e-07

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 51.95  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  67 PRRPY-TLDYLEHIF--TEFEELHgdRHFtdDAAIVGGVARLDDQPVMVIGHQKGR-----DvrekvrrnfgmprPEGYR 138
Cdd:COG4799  274 PRKPYdMREVIARLVdgGSFFEFK--PLY--GPNIVTGFARIDGRPVGIVANQPMVlagvlD-------------IDAAD 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729 139 KACRLMEMAERFKLPILTFIDTPGAYPGIDAEErnqsEAIAWN----LRVMARLKTPIVSTVIGeGGSGGAlAIGVCDRl 214
Cdd:COG4799  337 KAARFIRLCDAFNIPLVFLVDVPGFMVGTEQER----GGIIRHgaklLYAVAEATVPKITVILR-KAYGAG-YYAMCGK- 409

                        170       180       190
                 ....*....|....*....|....*....|..
gi 502035729 215 nmlQYST----------YAVISPEGCASILWR 236
Cdd:COG4799  410 ---ALGPdflfawptaeIAVMGGEGAANVLYR 438
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
7-166 8.88e-05

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 43.86  E-value: 8.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729   7 DFEQPIADLQAKIEELRLVGDDNALnisdeisrlqDKSHALtasifGNLTSWQ-IAQLarhprrpytLDylEHIFTEFEE 85
Cdd:COG4799    1 AMRALLAELRARREEALLGGGEKAI----------ERQHAR-----GKLTARErIDLL---------LD--PGSFLELGA 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  86 LHGDRHFTDD-----AAIVGGVARLDDQPVMVIGHQ---KGrdvrekvrrnfGMPRPEGYRKACRLMEMAERFKLPILTF 157
Cdd:COG4799   55 LAGHRMYDDDdrvpgDGVVTGIGTVDGRPVVVVANDftvKG-----------GSLGPMTAKKILRAQDIALENGLPVIYL 123


                 ....*....
gi 502035729 158 IDTPGAYPG 166
Cdd:COG4799  124 VDSGGARLQ 132
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 80-205 9.95e-04

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 40.56  E-value: 9.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  80 FTEFEELHGDRHFTDD---AAIVGGVARLDDQPVMVIGHQ---KGrdvrekvrrnfGMPRPEGYRKACRLMEMAERFKLP 153
Cdd:PLN02820  98 FLELSQLAGHELYGEDlpsGGIVTGIGPVHGRLCMFVANDptvKG-----------GTYYPITVKKHLRAQEIAAQCRLP 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502035729 154 ILTFIDTPGAYPGIDAE---ERNQSEAIAWNLRVMARLKTPIVSTVIGEGGSGGA 205
Cdd:PLN02820 167 CIYLVDSGGANLPRQAEvfpDRDHFGRIFYNQARMSSAGIPQIALVLGSCTAGGA 221
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 80-213 3.50e-03

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 39.02  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502035729  80 FTEFEELHGDrhftddaAIVGGVARLDDQPVMVIGhqkgrdvrekvrrNFGMPRPEGYRKACRLMEMAERFKLPILTFID 159
Cdd:PLN02820 350 FDEFKKNYGT-------TLVTGFARIYGQPVGIIG-------------NNGILFTESALKGAHFIELCAQRGIPLLFLQN 409

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502035729 160 TPGAYPGIDAEERNQSEAIAWNLRVMARLKTPIVSTVIgeGGSGGALAIGVCDR 213
Cdd:PLN02820 410 ITGFMVGSRSEASGIAKAGAKMVMAVACAKVPKITIIV--GGSFGAGNYGMCGR 461
 
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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