ID A0A109MYM4_9BACI Unreviewed; 332 AA.
AC A0A109MYM4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=AS888_06350 {ECO:0000313|EMBL:KWW20038.1};
OS Peribacillus simplex.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1478 {ECO:0000313|EMBL:KWW20038.1, ECO:0000313|Proteomes:UP000064189};
RN [1] {ECO:0000313|EMBL:KWW20038.1, ECO:0000313|Proteomes:UP000064189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VanAntwerpen02 {ECO:0000313|EMBL:KWW20038.1,
RC ECO:0000313|Proteomes:UP000064189};
RA Couger M.B.;
RT "Genome Sequence of Bacillus simplex strain VanAntwerpen2.";
RL Submitted (NOV-2015) 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}.
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:KWW20038.1}.
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DR EMBL; LNNH01000019; KWW20038.1; -; Genomic_DNA.
DR RefSeq; WP_061142227.1; NZ_LNNH01000019.1.
DR AlphaFoldDB; A0A109MYM4; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000064189; 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}; Ligase {ECO:0000313|EMBL:KWW20038.1};
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};
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 11..49
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 332 AA; 37352 MW; 7121B1A723C9450C CRC64;
MIYELEFERP VTELRNKIKE LKALTKNADV DLTVEIETLE KRLEKLEADI YDHLKPWDRV
QIARHPARPT TLDYIPLLFN DFIEFHGDRY YGDDEAIVAG IAQFDGRSVT VIGHQRGKDT
KENIRRNFGM PHPEGYRKAL RLMKQAEKFN RPIICFIDTK GAFPGKAAEE RGQSEAIAKN
LFEMAGLKVP VISIVIGEGG SGGALALGVG DRIFMLENST YSVISPEGAA ALLWKDASQA
KRAAESMQIT APDLNRLGVI DEIIPEVKGG AHRNANVQAE AIKETLKRSF NELLPLKSED
LINQRYMKFK KIGEYEFAKQ SEGKPEDVKQ HS
//
