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Conserved domains on  [gi|491994837|ref|WP_005711455|]
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acetyl-CoA carboxylase carboxyl transferase subunit alpha [Glaesserella parasuis]

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 ...
 5-316 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: 645.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837   5 YLDFELPIAELEAKIEALRsAVGNDNKINLDDEIARLQKKSEELTKKTFSDLDAWQISRMARHPSRPYTLDYIERIFTEF 84
Cdd:COG0825    2 YLDFEKPIAELEAKIEELR-ALAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIFTDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  85 DELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGYRKALRLMQMAERFNMPIITFIDTPGA 164
Cdd:COG0825   81 IELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDTPGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 165 YPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEKAST 244
Cdd:COG0825  161 YPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASKAPE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491994837 245 AAEVMGLTAPRLKELELIDNIVPEPLGGAHRNFDEMAANLKQRLLEDLADLDPLNAEALLDRRYQRLMGYGY 316
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 ...
 5-316 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: 645.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837   5 YLDFELPIAELEAKIEALRsAVGNDNKINLDDEIARLQKKSEELTKKTFSDLDAWQISRMARHPSRPYTLDYIERIFTEF 84
Cdd:COG0825    2 YLDFEKPIAELEAKIEELR-ALAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIFTDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  85 DELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGYRKALRLMQMAERFNMPIITFIDTPGA 164
Cdd:COG0825   81 IELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDTPGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 165 YPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEKAST 244
Cdd:COG0825  161 YPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASKAPE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491994837 245 AAEVMGLTAPRLKELELIDNIVPEPLGGAHRNFDEMAANLKQRLLEDLADLDPLNAEALLDRRYQRLMGYGY 316
Cdd:COG0825  241 AAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGR 312
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 1-317 0e+00

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 639.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837   1 MTTEYLDFELPIAELEAKIEALRsAVGNDNKINLDDEIARLQKKSEELTKKTFSDLDAWQISRMARHPSRPYTLDYIERI 80
Cdd:PRK05724   1 MMLNYLDFEKPIAELEAKIEELR-AVAEDSDVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIELL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  81 FTEFDELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGYRKALRLMQMAERFNMPIITFID 160
Cdd:PRK05724  80 FTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIITFID 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 161 TPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAE 240
Cdd:PRK05724 160 TPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWKDAS 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491994837 241 KASTAAEVMGLTAPRLKELELIDNIVPEPLGGAHRNFDEMAANLKQRLLEDLADLDPLNAEALLDRRYQRLMGYGYV 317
Cdd:PRK05724 240 KAPEAAEAMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAAALKEALLEALAELKGLSPEELLERRYEKFMSIGRF 316
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 1-317 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: 565.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837    1 MTTEYLDFELPIAELEAKIEALRsAVGNDNKINLDDEIARLQKKSEELTKKTFSDLDAWQISRMARHPSRPYTLDYIERI 80
Cdd:TIGR00513   1 MMANYLDFEKPIAELEAKIESLR-ARSRDEDVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIELI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837   81 FTEFDELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGYRKALRLMQMAERFNMPIITFID 160
Cdd:TIGR00513  80 FDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITFID 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  161 TPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAE 240
Cdd:TIGR00513 160 TPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKDAS 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491994837  241 KASTAAEVMGLTAPRLKELELIDNIVPEPLGGAHRNFDEMAANLKQRLLEDLADLDPLNAEALLDRRYQRLMGYGYV 317
Cdd:TIGR00513 240 KAPKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
AccA_sub NF041504
carboxyltransferase subunit alpha;
59-310 1.79e-159

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 444.97  E-value: 1.79e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  59 WQISRMARHPSRPYTLDYIERIFTEFDELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGY 138
Cdd:NF041504   1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 139 RKALRLMQMAERFNMPIITFIDTPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNML 218
Cdd:NF041504  81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 219 QYSTYSVISPEGCASILWKSAEKASTAAEVMGLTAPRLKELELIDNIVPEPLGGAHRNFDEMAANLKQRLLEDLADLDPL 298
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGL 240

                        250
                 ....*....|..
gi 491994837 299 NAEALLDRRYQR 310
Cdd:NF041504 241 SADELIAQRREK 252
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 5-149 2.28e-96

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: 280.83  E-value: 2.28e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837    5 YLDFELPIAELEAKIEALRsAVGNDNKINLDDEIARLQKKSEELTKKTFSDLDAWQISRMARHPSRPYTLDYIERIFTEF 84
Cdd:pfam03255   1 YLDFEKPIAELEAKIEELR-KLAEESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFDDF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491994837   85 DELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGYRKALRLMQMAE 149
Cdd:pfam03255  80 IELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRLMKLAE 144
 
Name Accession Description Interval E-value
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 5-316 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: 645.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837   5 YLDFELPIAELEAKIEALRsAVGNDNKINLDDEIARLQKKSEELTKKTFSDLDAWQISRMARHPSRPYTLDYIERIFTEF 84
Cdd:COG0825    2 YLDFEKPIAELEAKIEELR-ALAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIFTDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  85 DELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGYRKALRLMQMAERFNMPIITFIDTPGA 164
Cdd:COG0825   81 IELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDTPGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 165 YPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEKAST 244
Cdd:COG0825  161 YPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASKAPE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491994837 245 AAEVMGLTAPRLKELELIDNIVPEPLGGAHRNFDEMAANLKQRLLEDLADLDPLNAEALLDRRYQRLMGYGY 316
Cdd:COG0825  241 AAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGR 312
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 1-317 0e+00

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 639.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837   1 MTTEYLDFELPIAELEAKIEALRsAVGNDNKINLDDEIARLQKKSEELTKKTFSDLDAWQISRMARHPSRPYTLDYIERI 80
Cdd:PRK05724   1 MMLNYLDFEKPIAELEAKIEELR-AVAEDSDVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIELL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  81 FTEFDELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGYRKALRLMQMAERFNMPIITFID 160
Cdd:PRK05724  80 FTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIITFID 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 161 TPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAE 240
Cdd:PRK05724 160 TPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWKDAS 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491994837 241 KASTAAEVMGLTAPRLKELELIDNIVPEPLGGAHRNFDEMAANLKQRLLEDLADLDPLNAEALLDRRYQRLMGYGYV 317
Cdd:PRK05724 240 KAPEAAEAMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAAALKEALLEALAELKGLSPEELLERRYEKFMSIGRF 316
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 1-317 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: 565.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837    1 MTTEYLDFELPIAELEAKIEALRsAVGNDNKINLDDEIARLQKKSEELTKKTFSDLDAWQISRMARHPSRPYTLDYIERI 80
Cdd:TIGR00513   1 MMANYLDFEKPIAELEAKIESLR-ARSRDEDVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIELI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837   81 FTEFDELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGYRKALRLMQMAERFNMPIITFID 160
Cdd:TIGR00513  80 FDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITFID 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  161 TPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAE 240
Cdd:TIGR00513 160 TPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKDAS 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491994837  241 KASTAAEVMGLTAPRLKELELIDNIVPEPLGGAHRNFDEMAANLKQRLLEDLADLDPLNAEALLDRRYQRLMGYGYV 317
Cdd:TIGR00513 240 KAPKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
AccA_sub NF041504
carboxyltransferase subunit alpha;
59-310 1.79e-159

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 444.97  E-value: 1.79e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  59 WQISRMARHPSRPYTLDYIERIFTEFDELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGY 138
Cdd:NF041504   1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 139 RKALRLMQMAERFNMPIITFIDTPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNML 218
Cdd:NF041504  81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 219 QYSTYSVISPEGCASILWKSAEKASTAAEVMGLTAPRLKELELIDNIVPEPLGGAHRNFDEMAANLKQRLLEDLADLDPL 298
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGL 240

                        250
                 ....*....|..
gi 491994837 299 NAEALLDRRYQR 310
Cdd:NF041504 241 SADELIAQRREK 252
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 1-316 5.23e-132

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 378.38  E-value: 5.23e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837   1 MTTEYLDFELPIAELEAKIEALRSAVGNDNKInLDDEIARLQKKSEELTKKTFSDLDAWQISRMARHPSRPYTLDYIERI 80
Cdd:CHL00198   4 RKPHVPDFMKPLAELESQVEELSKLAPKNDKV-INNKLKSFQRKLRILKKEIFYSLTPLQRLHLVRQSERPTTLDYIPYI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  81 FTEFDELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGYRKALRLMQMAERFNMPIITFID 160
Cdd:CHL00198  83 LDEWIELHGDRGGSDDPALVGGIGKINGRTIVFLGHQRGRNTKENVLRNFGMPSPGGYRKALRLMKHANKFGLPILTFID 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 161 TPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAE 240
Cdd:CHL00198 163 TPGAWAGVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALGIGIGDSIMMLEYAVYTVATPEACAAILWKDSK 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491994837 241 KASTAAEVMGLTAPRLKELELIDNIVPEPLGGAHRNFDEMAANLKQRLLEDLADLDPLNAEALLDRRYQRL--MGYGY 316
Cdd:CHL00198 243 KSLDAAEALKITSEDLKVLGIIDEIIPEPIGGAQADPASASKILKKKLIRQLDFLKILSPSELKAHRYEKFrkLGAFY 320
PLN03230 PLN03230
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
 6-317 7.36e-118

acetyl-coenzyme A carboxylase carboxyl transferase; Provisional


Pssm-ID: 178769 [Multi-domain]  Cd Length: 431  Bit Score: 346.16  E-value: 7.36e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837   6 LDFELPIAELEAKIEALRSaVGNDNKINLDDEIARLQKKSEELTKKTFSDLDAWQISRMARHPSRPYTLDYIERIFTEFD 85
Cdd:PLN03230  76 LPFEKPIVDLENRIDEVRE-LANKTGVDFSAQIAELEERYDQVRRELYSRLTPVQRLSVARHPNRPTFLDHVLNMTDKWV 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  86 ELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGYRKALRLMQMAERFNMPIITFIDTPGAY 165
Cdd:PLN03230 155 ELHGDRAGFDDPAIVCGIGSMEGMSFMFIGHQKGRNTKENIYRNFAMPQPNGYRKALRFMRHAEKFGFPILTFVDTPGAY 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 166 PGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEKASTA 245
Cdd:PLN03230 235 AGIKAEELGQGEAIAFNLREMFGLRVPIIATVIGEGGSGGALAIGCGNRMLMMENAVYYVASPEACAAILWKSAAAAPKA 314

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491994837 246 AEVMGLTAPRLKELELIDNIVPEPLGGAHRNFDEMAANLKQRLLEDLADLDPLNAEALLDRRYQRLMGYGYV 317
Cdd:PLN03230 315 AEALRITAAELVKLGVVDEIVPEPLGGAHSDPLQASKNIKEVILRHMKELMKMDPEELLQDRAAKFRKIGEF 386
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 57-314 1.41e-113

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 329.04  E-value: 1.41e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  57 DAWQISRMARHPSRPYTLDYIERIFTEFDELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPE 136
Cdd:PRK12319   3 DVARILKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAGQPVTVVGIQKGKNLQDNLKRNFGQPHPE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 137 GYRKALRLMQMAERFNMPIITFIDTPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVN 216
Cdd:PRK12319  83 GYRKALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAVADQVW 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 217 MLQYSTYSVISPEGCASILWKSAEKASTAAEVMGLTAPRLKELELIDNIVPEplggAHRNFDEMAANLKQRLLEDLADLD 296
Cdd:PRK12319 163 MLENTMYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDKVIPE----HGYFSSEIIDMIKKNLIEELAQLS 238

                        250
                 ....*....|....*...
gi 491994837 297 PLNAEALLDRRYQRLMGY 314
Cdd:PRK12319 239 QKPLEQLLEERYQRFRKY 256
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 6-307 3.63e-104

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 321.03  E-value: 3.63e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837   6 LDFELPIAELEAKIEALRSaVGNDNKINLDDEIARLQKKSEELTKKTFSDLDAWQISRMARHPSRPYTLDYIERIFTEFD 85
Cdd:PLN03229  97 LDFEKPLVDLEKKIVDVRK-MANETGLDFSDQIISLESKYQQALKDLYTHLTPIQRVNIARHPNRPTFLDHIFNITDKFV 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  86 ELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGYRKALRLMQMAERFNMPIITFIDTPGAY 165
Cdd:PLN03229 176 ELHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGRNTKENIMRNFGMPTPHGYRKALRMMYYADHHGFPIVTFIDTPGAY 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 166 PGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEKASTA 245
Cdd:PLN03229 256 ADLKSEELGQGEAIAHNLRTMFGLKVPIVSIVIGEGGSGGALAIGCANKLLMLENAVFYVASPEACAAILWKSAKAAPKA 335

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491994837 246 AEVMGLTAPRLKELELIDNIVPEPLGGAHRNFDEMAANLKQRLLEDLADLDPLNAEALLDRR 307
Cdd:PLN03229 336 AEKLRITAQELCRLQIADGIIPEPLGGAHADPSWTSQQIKIAINENMDELGKMDTEELLKHR 397
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 5-149 2.28e-96

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: 280.83  E-value: 2.28e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837    5 YLDFELPIAELEAKIEALRsAVGNDNKINLDDEIARLQKKSEELTKKTFSDLDAWQISRMARHPSRPYTLDYIERIFTEF 84
Cdd:pfam03255   1 YLDFEKPIAELEAKIEELR-KLAEESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFDDF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491994837   85 DELAGDRAFADDKAIVGGIARLDGRPVMVIGHQKGRTVKEKVKRNFGMPAPEGYRKALRLMQMAE 149
Cdd:pfam03255  80 IELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRLMKLAE 144
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 55-260 2.92e-16

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: 78.84  E-value: 2.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837   55 DLDAWQISRMARHPSRPYTL-DYIERIFT--EFDELAGDRAfaddKAIVGGIARLDGRPVMVIGHQKgrtvkekvKRNFG 131
Cdd:pfam01039 239 DRDAPLVSIVPDDPKKPYDVrEVIAGIVDegEFFEIKPGYA----KTVVTGFARLGGIPVGVVANQP--------RVGAG 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  132 MPAPEGYRKALRLMQMAERFNMPIITFIDTPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIG- 210
Cdd:pfam01039 307 VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDs 386

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 491994837  211 ---VGDKVNMLQYSTYSVISPEGCASILWKSAEKASTA--AEVMGLTAPRLKELE 260
Cdd:pfam01039 387 kinGADINFAWPTARIAVMGPEGAVEIKFRKEKAAAEMrgKDLAATRKQKIAEYE 441
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
68-206 2.58e-13

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 70.06  E-value: 2.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  68 PSRPY-TLDYIERIF--TEFDELAGDRAfaddKAIVGGIARLDGRPVMVIGHQKgrtvkekvKRNFGMPAPEGYRKALRL 144
Cdd:COG4799  274 PRKPYdMREVIARLVdgGSFFEFKPLYG----PNIVTGFARIDGRPVGIVANQP--------MVLAGVLDIDAADKAARF 341

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491994837 145 MQMAERFNMPIITFIDTPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGeGGSGGA 206
Cdd:COG4799  342 IRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILR-KAYGAG 402
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
12-206 2.16e-12

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 67.36  E-value: 2.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  12 IAELEAKIEALRSAVGndnkinlDDEIARlQKKSEELTkktfsdldawqisrmARhpsrpytldyiERI--------FTE 83
Cdd:COG4799    6 LAELRARREEALLGGG-------EKAIER-QHARGKLT---------------AR-----------ERIdllldpgsFLE 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  84 FDELAGDRAFADDK-----AIVGGIARLDGRPVMVIGHQKgrTVKEkvkrnfGMPAPEGYRKALRLMQMAERFNMPIITF 158
Cdd:COG4799   52 LGALAGHRMYDDDDrvpgdGVVTGIGTVDGRPVVVVANDF--TVKG------GSLGPMTAKKILRAQDIALENGLPVIYL 123

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 491994837 159 IDTPGAYPGIGAEERGQSEAIARNLREMStLKVPVICTVIGEGGSGGA 206
Cdd:COG4799  124 VDSGGARLQEGVESFAGYGRIFYRNARSS-GGIPQISVIMGPCAAGGA 170
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 64-219 9.87e-09

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 56.35  E-value: 9.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  64 MARHPSRPYTL--DYIERI------FTEFDELAGDRAFADD---KAIVGGIARLDGRPVMVIGHQKgrTVKEkvkrnfGM 132
Cdd:PLN02820  73 VKRHRSRNKLLprERIDRLldpgspFLELSQLAGHELYGEDlpsGGIVTGIGPVHGRLCMFVANDP--TVKG------GT 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837 133 PAPEGYRKALRLMQMAERFNMPIITFIDTPGAYPGIGAE---ERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAI 209
Cdd:PLN02820 145 YYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEvfpDRDHFGRIFYNQARMSSAGIPQIALVLGSCTAGGAYVP 224

                        170
                 ....*....|
gi 491994837 210 GVGDKVNMLQ 219
Cdd:PLN02820 225 AMADESVIVK 234
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 81-275 3.96e-06

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: 48.02  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837   81 FTEFDELAGDRA-------FADDkAIVGGIARLDGRPVMVIGHQKgrTVkekvkrnFGMPAPEGY-RKALRLMQMAERFN 152
Cdd:pfam01039  23 FGELEDLFFHRAtefgrkrIPRD-GVVTGSGAVIGRAVEVVAQDF--TV-------FGGSLGPAKgEKILRAMEIAIKTG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  153 MPIITFIDTPGAYPGIGAEERGQSEAIARNLREMSTlKVPVICTVIGEGGSGGALAIGVGDKVNMlqystysvispegca 232
Cdd:pfam01039  93 LPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASG-VIPQISLIMGPCAGGGAYLPALGDFVIM--------------- 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 491994837  233 silwksAEKASTaaevMGLTAPRLKELELIDNIVPEPLGGAHR 275
Cdd:pfam01039 157 ------VEGTSP----MFLTGPPVIKKVTGEEVTSEELGGATQ 189
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 81-206 3.41e-04

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 42.10  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994837  81 FTEFDELAGDrafaddkAIVGGIARLDGRPVMVIGhqkgrtvkekvkrNFGMPAPEGYRKALRLMQMAERFNMPIITFID 160
Cdd:PLN02820 350 FDEFKKNYGT-------TLVTGFARIYGQPVGIIG-------------NNGILFTESALKGAHFIELCAQRGIPLLFLQN 409

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 491994837 161 TPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIgeGGSGGA 206
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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