(data stored in ACNUC7421 zone)

SWISSPROT: ACCA_SALTY

ID   ACCA_SALTY              Reviewed;         319 AA.
AC   P0A1C3; P40674;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   11-DEC-2019, entry version 95.
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=STM0232;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RX   PubMed=2676978; DOI=10.1128/jb.171.10.5581-5586.1989;
RA   Lancy E.D., Lifsics M.R., Munson P., Maurer R.;
RT   "Nucleotide sequences of dnaE, the gene for the polymerase subunit of DNA
RT   polymerase III in Salmonella typhimurium, and a variant that facilitates
RT   growth in the absence of another polymerase subunit.";
RL   J. Bacteriol. 171:5581-5586(1989).
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}.
DR   EMBL; AE006468; AAL19196.1; -; Genomic_DNA.
DR   EMBL; M26046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_459237.1; NC_003197.2.
DR   RefSeq; WP_000055753.1; NC_003197.2.
DR   SMR; P0A1C3; -.
DR   PaxDb; P0A1C3; -.
DR   PRIDE; P0A1C3; -.
DR   EnsemblBacteria; AAL19196; AAL19196; STM0232.
DR   GeneID; 1251750; -.
DR   KEGG; stm:STM0232; -.
DR   PATRIC; fig|99287.12.peg.245; -.
DR   eggNOG; ENOG4107QM9; Bacteria.
DR   eggNOG; COG0825; LUCA.
DR   HOGENOM; HOG000273832; -.
DR   KO; K01962; -.
DR   OMA; HPERPYT; -.
DR   PhylomeDB; P0A1C3; -.
DR   BioCyc; SENT99287:STM0232-MONOMER; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000001014; 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;
DR   PRODOM; P0A1C3.
DR   SWISS-2DPAGE; P0A1C3.
KW   ATP-binding; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..319
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit alpha"
FT                   /id="PRO_0000146777"
FT   DOMAIN          35..296
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT   CONFLICT        17
FT                   /note="A -> R (in Ref. 2; M26046)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   319 AA;  35344 MW;  55B3F98F39281B32 CRC64;
     MSLNFLDFEQ PIAELEAKID SLTAVSRQDE KLDINIDEEV HRLREKSVEL TRKIFADLGA
     WQVAQLARHP QRPYTLDYVR LAFDEFDELA GDRAYADDKA IVGGIARLEG RPVMIIGHQK
     GRETKEKIRR NFGMPAPEGY RKALRLMEMA ERFNMPIITF IDTPGAYPGV GAEERGQSEA
     IARNLREMSR LNVPVICTVI GEGGSGGALA IGVGDKVNML QYSTYSVISP EGCASILWKS
     ADKAPLAAEA MGIIAPRLKE LKLIDSIIPE PLGGAHRNPE AMAASLKAQL LEDLADLDVL
     STDDLKNRRY QRLMSYGYA
//

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