ACCA_FRATT
ID ACCA_FRATT Reviewed; 315 AA.
AC Q5NEV9;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=FTT_1498c;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG46131.1; -; Genomic_DNA.
DR RefSeq; WP_003022368.1; NZ_CP010290.1.
DR RefSeq; YP_170433.1; NC_006570.2.
DR AlphaFoldDB; Q5NEV9; -.
DR SMR; Q5NEV9; -.
DR STRING; 177416.FTT_1498c; -.
DR DNASU; 3192200; -.
DR EnsemblBacteria; CAG46131; CAG46131; FTT_1498c.
DR KEGG; ftu:FTT_1498c; -.
DR eggNOG; COG0825; Bacteria.
DR OMA; TPWQRVQ; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001174; 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..315
FT /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT subunit alpha"
FT /id="PRO_0000223769"
FT DOMAIN 36..289
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
SQ SEQUENCE 315 AA; 35464 MW; 85C9F6D2B0B81FEA CRC64;
MNYLDFESKI KEIEDKITSL SHVFEDEKTE VEIKKLSKKR LELMESTYSK LTDWQVVQLS
RHPDRPYFKD LLPLIFTDFQ ELHGDRTFGD DLAVIGGLAK LNNKPVMVIG QEKGRDTKSK
IKHNFGMMHP EGYRKALRLM KLAEKFNMPV VTFIDTPGAY PGIKAEERGQ SEAIARNLLE
MSALKVPVVC IVIGEGCSGG ALGIGVGDRL LMLQYSYFAT ISPEGCASIL HKTAEKASEV
TQMMNITSGR LKELKIVDEV IPEPLGGAHR DYETTATNIR KAVAAELKIL SEMTVEQRNS
RRYDKLMSFG RFKEA
