ID A0A919X921_9BACI Unreviewed; 317 AA.
AC A0A919X921;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 9.
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 ECO:0000313|EMBL:GIO27811.1};
GN ORFNames=J43TS3_24220 {ECO:0000313|EMBL:GIO27811.1};
OS Ornithinibacillus bavariensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Ornithinibacillus.
OX NCBI_TaxID=545502 {ECO:0000313|EMBL:GIO27811.1, ECO:0000313|Proteomes:UP000676917};
RN [1] {ECO:0000313|EMBL:GIO27811.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=J43TS3 {ECO:0000313|EMBL:GIO27811.1};
RA Okamoto M., Kumagai M., Kanamori H., Takamatsu D.;
RT "Antimicrobial resistance genes in bacteria isolated from Japanese honey,
RT and their potential for conferring macrolide and lincosamide resistance in
RT the American foulbrood pathogen Paenibacillus larvae.";
RL Submitted (MAR-2021) 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=N(6)-carboxybiotinyl-L-lysyl-[protein] + acetyl-CoA = N(6)-
CC biotinyl-L-lysyl-[protein] + malonyl-CoA; 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:ARBA00049152, 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GIO27811.1}.
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DR EMBL; BORP01000004; GIO27811.1; -; Genomic_DNA.
DR RefSeq; WP_212921266.1; NZ_BORP01000004.1.
DR Proteomes; UP000676917; 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-KW.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 1.
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 NCBIfam; NF004344; PRK05724.1; 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:UP000676917};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00823}.
FT DOMAIN 38..292
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT COILED 272..299
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 317 AA; 35708 MW; E6C5E04056088FFB CRC64;
MKQILEFEKP IMNLKEKIAE LKKFTGESEI DLTDEIATLE KRLAELEDNI YGNLKPWQRV
QMARHQDRPT TLDYISELFT DFLEFHGDRT FGDDEAIVTG IAYYKEVPIT VIGHQRGKNT
KENIRRNFGM PHPEGYRKAL RHMKQAEKFN RPIICFIDTK GADPGKESEE RGQSEAIARN
LMEMAGLKVP IICIVIGEGG SGGALALGVG DRIFMLENST YSVISPEGAA ALLWKDAGLA
QKAAESMKIT APDLFELGII DEIVPEPKGG AHRDIEQQAK NMDAVIEKAL KELADLTTEE
LLENRWEKYK QIGDFKE
//
