ID   ACCA_SYNP2              Reviewed;         325 AA.
AC   B1XK66;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, 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};
GN   OrderedLocusNames=SYNPCC7002_A2443;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) 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: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; CP000951; ACB00421.1; -; Genomic_DNA.
DR   RefSeq; WP_012308039.1; NC_010475.1.
DR   AlphaFoldDB; B1XK66; -.
DR   SMR; B1XK66; -.
DR   STRING; 32049.SYNPCC7002_A2443; -.
DR   EnsemblBacteria; ACB00421; ACB00421; SYNPCC7002_A2443.
DR   KEGG; syp:SYNPCC7002_A2443; -.
DR   eggNOG; COG0825; Bacteria.
DR   HOGENOM; CLU_015486_0_2_3; -.
DR   OMA; TPWQRVQ; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001688; 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_1000134531"
FT   DOMAIN          44..298
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ   SEQUENCE   325 AA;  35844 MW;  528135CC91FD9151 CRC64;
     MPKTERRTFL LDFEKPLSEL ESRIHQIRDL AAENNVDVSE QIQQLEARAD QLREEIFSTL
     TPAQRLQLAR HPRRPSTLDY VQMMADEWFE LHGDRGGSDD PALIGGVARF DGQPVMMLGH
     QKGRDTKDNV ARNFGMPAPG GYRKAMRLMD HANRFGMPIL TFIDTPGAWA GLEAEKLGQG
     EAIAFNLREM FSLDVPIICT VIGEGGSGGA LGIGVGDRVL MLKNSVYTVA TPEACAAILW
     KDAGKSEQAA AALKITAEDL KSLEIIDEIV PEPASCAHAD PIGAAQLLKA AIQDNLQALL
     KLTPERRREL RYQRFRKIGV FLESS