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 03-AUG-2022, entry version 104.
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).
RN [3]
RP ANTIBIOTIC RESISTANCE, AND MUTAGENESIS OF PRO-164; PRO-168 AND SER-229.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=29914944; DOI=10.1128/aac.00463-18;
RA Wozniak C.E., Lin Z., Schmidt E.W., Hughes K.T., Liou T.G.;
RT "Thailandamide, a Fatty Acid Synthesis Antibiotic That Is Coexpressed with
RT a Resistant Target Gene.";
RL Antimicrob. Agents Chemother. 62:0-0(2018).
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; 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 AlphaFoldDB; P0A1C3; -.
DR SMR; P0A1C3; -.
DR STRING; 99287.STM0232; -.
DR PaxDb; P0A1C3; -.
DR EnsemblBacteria; AAL19196; AAL19196; STM0232.
DR GeneID; 1251750; -.
DR KEGG; stm:STM0232; -.
DR PATRIC; fig|99287.12.peg.245; -.
DR HOGENOM; CLU_015486_0_2_6; -.
DR OMA; TPWQRVQ; -.
DR PhylomeDB; P0A1C3; -.
DR BioCyc; SENT99287:STM0232-MON; -.
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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Antibiotic resistance; ATP-binding; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0ABD5"
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 MUTAGEN 164
FT /note="P->L,Q,S,T: Resistance to polyketide antibiotic
FT thailandamide."
FT /evidence="ECO:0000269|PubMed:29914944"
FT MUTAGEN 168
FT /note="P->H: Resistance to thailandamide."
FT /evidence="ECO:0000269|PubMed:29914944"
FT MUTAGEN 229
FT /note="S->T: Resistance to thailandamide."
FT /evidence="ECO:0000269|PubMed:29914944"
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
