ID   ACCA_GEOKA              Reviewed;         325 AA.
AC   Q5KWB0;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=GK2741;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD77026.1; -; Genomic_DNA.
DR   RefSeq; WP_011232215.1; NC_006510.1.
DR   AlphaFoldDB; Q5KWB0; -.
DR   SMR; Q5KWB0; -.
DR   STRING; 235909.GK2741; -.
DR   EnsemblBacteria; BAD77026; BAD77026; GK2741.
DR   KEGG; gka:GK2741; -.
DR   eggNOG; COG0825; Bacteria.
DR   HOGENOM; CLU_015486_0_2_9; -.
DR   OMA; TPWQRVQ; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001172; 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..325
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit alpha"
FT                   /id="PRO_0000223771"
FT   DOMAIN          35..292
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ   SEQUENCE   325 AA;  36387 MW;  D7F254E639722F78 CRC64;
     MVAELEFEKP LVELRRKIQE LKEFMKTADV DLSAEIEKLE ARLAKLENEI YANLTPWDRV
     QIARHPQRPT TLDYIERLFT NFLECHGDRC FGDDEAIVGG IAKYDGLPVT VIGHQRGKDT
     KENLRRNFGM PHPEGYRKAL RLMKQAEKFS RPIICFIDTK GAYPGKAAEE RGQSEAIARN
     LFEMAGLTVP VVCIVIGEGG SGGALALGVG NHIHMLENST YSVISPEGAA AILWKDASLA
     QRAAETMKIT AHDLKALGVI DEIIPEVKGG AHRNADEQAK EIDRVLRRSL KQLLALDGEE
     LVRQRYEKFK QMGQVSFLPE TIRAR