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Database: UniProt
Entry: A0A0R2CVE5_9LACO
LinkDB: A0A0R2CVE5_9LACO
Original site: A0A0R2CVE5_9LACO 
ID   A0A0R2CVE5_9LACO        Unreviewed;       262 AA.
AC   A0A0R2CVE5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=acetyl-CoA carboxytransferase {ECO:0000256|ARBA:ARBA00011883};
DE            EC=2.1.3.15 {ECO:0000256|ARBA:ARBA00011883};
GN   ORFNames=FC19_GL001263 {ECO:0000313|EMBL:KRM95784.1};
OS   Liquorilactobacillus aquaticus DSM 21051.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1423725 {ECO:0000313|EMBL:KRM95784.1, ECO:0000313|Proteomes:UP000051015};
RN   [1] {ECO:0000313|EMBL:KRM95784.1, ECO:0000313|Proteomes:UP000051015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21051 {ECO:0000313|EMBL:KRM95784.1,
RC   ECO:0000313|Proteomes:UP000051015};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:0000256|ARBA:ARBA00001072};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRM95784.1}.
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DR   EMBL; AYZD01000018; KRM95784.1; -; Genomic_DNA.
DR   RefSeq; WP_057876250.1; NZ_AYZD01000018.1.
DR   AlphaFoldDB; A0A0R2CVE5; -.
DR   STRING; 1423725.FC19_GL001263; -.
DR   PATRIC; fig|1423725.3.peg.1301; -.
DR   OrthoDB; 9808023at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000051015; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001095; Acetyl_CoA_COase_a_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   NCBIfam; NF041504; AccA_sub; 1.
DR   PANTHER; PTHR42853; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR42853:SF3; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA, CHLOROPLASTIC; 1.
DR   Pfam; PF03255; ACCA; 1.
DR   PRINTS; PR01069; ACCCTRFRASEA.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRM95784.1}.
FT   DOMAIN          1..242
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   262 AA;  28944 MW;  92CCD2B1651BF520 CRC64;
     MVSLLDKKKT AAQIVANARS EEKMSAYELI DGIFSEFMEL HGDRLSDDDA AIVGGVAKFN
     DTPVTVIATN KGKSAEERLR THFGCPEPSG YRKSLRLIKQ AEKFRRPVIA FVNTAGAYPG
     KSAEENGQGE AIAHNLLEIS SVKTPVISMI YGEGGSGGAL ALACGDRVWM FENSMYSVLS
     PEGFAAILWK DSSRADEAAD VMQLTPEKLL EQHVIDGIVP ESRSHKRVFK AVKKILQKEL
     TDLEKLTSSE LIEKRHQRFR QF
//
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