ACCA_SYNE7
ID ACCA_SYNE7 Reviewed; 327 AA.
AC Q54766; Q31MU4; Q79PG1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=Synpcc7942_1595; ORFNames=sec0029;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Phung L.T., Haselkorn R.;
RT "Genes encoding the alpha subunit of carboxyltransferase of the acetyl-CoA
RT carboxylase complex and GTP cyclohydrolase I from cyanobacterium
RT Synechococcus sp. PCC 7942.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., Gonzalez A.,
RA Salinas I., McMurtry S., Golden S.S., Youderian P.;
RT "Synechococcus elongatus PCC7942 cosmid 6C3.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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; U59236; AAB82040.1; -; Genomic_DNA.
DR EMBL; AY120852; AAM82646.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57625.1; -; Genomic_DNA.
DR RefSeq; WP_011242365.1; NC_007604.1.
DR AlphaFoldDB; Q54766; -.
DR SMR; Q54766; -.
DR STRING; 1140.Synpcc7942_1595; -.
DR PRIDE; Q54766; -.
DR EnsemblBacteria; ABB57625; ABB57625; Synpcc7942_1595.
DR KEGG; syf:Synpcc7942_1595; -.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_0_2_3; -.
DR OMA; TPWQRVQ; -.
DR OrthoDB; 886663at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1595-MON; -.
DR UniPathway; UPA00655; UER00711.
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..327
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha"
FT /id="PRO_0000146782"
FT DOMAIN 46..299
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ SEQUENCE 327 AA; 35733 MW; 6C4EFCD304CA8132 CRC64;
MAAPVTKKPI LLEFEKPLVE LEERITQIRT LAADNQVDVS GQIQQLEARA IQLRREIFSN
LSPAQRIQVA RHPRRPSTLD YIQAISDEWI ELHGDRNGSD DLALVGGVGA LDGQPVVFLG
HQKGRDTKDN VLRNFGMASP GGYRKALRLM EHADRFGMPI LTFIDTPGAY AGVSAEELGQ
GEAIAVNLRE MFRFSVPILC TVIGEGGSGG ALGIGVGDRL LMFEHSVYTV ASPEACASIL
WRDAGKAAQA AEALKITARD LKQLGILDEI ITEPLGGAHS APLETAQSLR QVLLRHLKDL
QALSPAQLRE QRYQKFRQLG VFLESSD
