ID   ACCA_ERWT9              Reviewed;         319 AA.
AC   B2VHY2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=ETA_09060;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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}.
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DR   EMBL; CU468135; CAO95952.1; -; Genomic_DNA.
DR   RefSeq; WP_012440654.1; NC_010694.1.
DR   AlphaFoldDB; B2VHY2; -.
DR   SMR; B2VHY2; -.
DR   STRING; 465817.ETA_09060; -.
DR   PRIDE; B2VHY2; -.
DR   EnsemblBacteria; CAO95952; CAO95952; ETA_09060.
DR   KEGG; eta:ETA_09060; -.
DR   eggNOG; COG0825; Bacteria.
DR   HOGENOM; CLU_015486_0_2_6; -.
DR   OMA; TPWQRVQ; -.
DR   OrthoDB; 886663at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001726; 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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..319
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit alpha"
FT                   /id="PRO_1000134490"
FT   DOMAIN          35..296
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ   SEQUENCE   319 AA;  35219 MW;  19FA6BFC4BBBCD84 CRC64;
     MSLNYLDFEQ PIAELEAKID SLKSVGRQDE KLDINLDEEV QRLRDKSVEL TRKIFSDLGA
     WQIAQLARHP LRPYTLDYVR NVFTDFDELA GDRAYADDKA IVGGIARLED RPVMIIGHQK
     GRETKEKIRR NFGMPAPEGY RKALRLMEMA ERFNMPIITF IDTPGAYPGV GAEERGQSEA
     IARNLREMSG LKVPVICTVI GEGGSGGALA IGVGDKVNML QYSTYSVISP EGCASILWKS
     ADKAPLAAEA MGIIAPRLKE LKLIDSVIPE PLGGAHRDPL AIGASLKAQL LADLADLDTL
     TKAELLDRRY QRLMSYGYA