ID A0A1I4RQ94_ECTMO Unreviewed; 316 AA.
AC A0A1I4RQ94;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
DE Short=ACCase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00823};
DE EC=2.1.3.15 {ECO:0000256|HAMAP-Rule:MF_00823};
GN Name=accA {ECO:0000256|HAMAP-Rule:MF_00823};
GN ORFNames=SAMN05421721_10922 {ECO:0000313|EMBL:SFM54452.1};
OS Ectothiorhodospira mobilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=195064 {ECO:0000313|EMBL:SFM54452.1, ECO:0000313|Proteomes:UP000199556};
RN [1] {ECO:0000313|EMBL:SFM54452.1, ECO:0000313|Proteomes:UP000199556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4180 {ECO:0000313|EMBL:SFM54452.1,
RC ECO:0000313|Proteomes:UP000199556};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC First, biotin carboxylase catalyzes the carboxylation of biotin on its
CC carrier protein (BCCP) and then the CO(2) group is transferred by the
CC carboxyltransferase to acetyl-CoA to form malonyl-CoA.
CC {ECO:0000256|HAMAP-Rule:MF_00823}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001072, ECO:0000256|HAMAP-
CC Rule:MF_00823};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956,
CC ECO:0000256|HAMAP-Rule:MF_00823}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two
CC subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta
CC (AccD). {ECO:0000256|HAMAP-Rule:MF_00823}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00823}.
CC -!- SIMILARITY: Belongs to the AccA family. {ECO:0000256|HAMAP-
CC Rule:MF_00823}.
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DR EMBL; FOUO01000009; SFM54452.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4RQ94; -.
DR STRING; 195064.SAMN05421721_10922; -.
DR OrthoDB; 9808023at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000199556; Unassembled WGS sequence.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00823; AcetylCoA_CT_alpha; 1.
DR InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR NCBIfam; TIGR00513; accA; 1.
DR NCBIfam; NF041504; AccA_sub; 1.
DR PANTHER; PTHR42853; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR42853:SF3; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA, CHLOROPLASTIC; 1.
DR Pfam; PF03255; ACCA; 1.
DR PRINTS; PR01069; ACCCTRFRASEA.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00823}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00823};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_00823};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_00823};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00823};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00823};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00823}; Reference proteome {ECO:0000313|Proteomes:UP000199556};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00823}.
FT DOMAIN 39..293
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT COILED 12..50
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 316 AA; 34908 MW; FB1F5EBB3D4D19DB CRC64;
MNPDFLDFEQ PIAELEAKIE ELRRVSDDAE VNIQDEINRL EAKCKSLTES IFSKLSAWQV
AQLARHPRRP YTLDYVAHML TDFEELHGDR AFADDPAIVG GVGRLAGKPV MVIGHQKGRD
TREKIHRNFG MPRPEGYRKA LRLMQTAERF GLPIITFIDT PGAYPGVGAE ERGQSEAIAR
NLMEMSRLRT PIVCTVVGEG GSGGALAVGV GDQVQMLRYS TYAVISPEGC ASILWKSAEK
APEAAEAMGI TSTRLKELGL IDRVIDEPLG GAHRDPAAMA HTLKNQLVET LDELQCKDPD
ALVEARYQRI LKYGQV
//
