ACCA_ENT38
ID ACCA_ENT38 Reviewed; 319 AA.
AC A4W6T0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
DE Short=ACCase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
DE Short=Acetyl-CoA carboxylase carboxyltransferase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00823};
DE EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_00823};
GN Name=accA {ECO:0000255|HAMAP-Rule:MF_00823}; OrderedLocusNames=Ent638_0723;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
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:0000255|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:0000255|HAMAP-Rule:MF_00823};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00823}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00823}.
CC -!- SIMILARITY: Belongs to the AccA family. {ECO:0000255|HAMAP-
CC Rule:MF_00823}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000653; ABP59410.1; -; Genomic_DNA.
DR RefSeq; WP_012016131.1; NC_009436.1.
DR AlphaFoldDB; A4W6T0; -.
DR SMR; A4W6T0; -.
DR STRING; 399742.Ent638_0723; -.
DR EnsemblBacteria; ABP59410; ABP59410; Ent638_0723.
DR GeneID; 66412393; -.
DR KEGG; ent:Ent638_0723; -.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_0_2_6; -.
DR OMA; TPWQRVQ; -.
DR OrthoDB; 886663at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000000230; Chromosome.
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 PANTHER; PTHR42853; PTHR42853; 1.
DR Pfam; PF03255; ACCA; 1.
DR PRINTS; PR01069; ACCCTRFRASEA.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00513; accA; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; Transferase.
FT CHAIN 1..319
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha"
FT /id="PRO_1000062616"
FT DOMAIN 35..296
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ SEQUENCE 319 AA; 35324 MW; 47B633AB24D4BEDE CRC64;
MSLNFLDFEQ PIAELEAKID SLTAVSRQDE KLDINIDEEV HRLREKSVEL TRKIFADLGA
WQIAQLARHP QRPYTLDYVR LAFDEFDELA GDRAYADDKA IVGGIARLDG RPVMIIGHQK
GRETKEKIRR NFGMPAPEGY RKALRLMEMA ERFNMPIVTF IDTPGAYPGV GAEERGQSEA
IARNLREMSR LTVPVICTVI GEGGSGGALA IGVGDKVNML QYSTYSVISP EGCASILWKS
ADKAPLAAEA MGITAPRLKE LKLIDTVIPE PLGGAHRKPE VIAASLKAQL LADLADLDVL
SKEDLLNRRY QRLMNYGYA