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Database: UniProt
Entry: X0QCU2_9LACO
LinkDB: X0QCU2_9LACO
Original site: X0QCU2_9LACO 
ID   X0QCU2_9LACO            Unreviewed;       256 AA.
AC   X0QCU2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=acetyl-CoA carboxytransferase {ECO:0000256|ARBA:ARBA00011883};
DE            EC=2.1.3.15 {ECO:0000256|ARBA:ARBA00011883};
GN   ORFNames=FD41_GL002559 {ECO:0000313|EMBL:KRM09500.1}, JCM14108_1397
GN   {ECO:0000313|EMBL:GAF36430.1};
OS   Lentilactobacillus farraginis DSM 18382 = JCM 14108.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=1423743 {ECO:0000313|EMBL:GAF36430.1, ECO:0000313|Proteomes:UP000019488};
RN   [1] {ECO:0000313|EMBL:GAF36430.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14108 {ECO:0000313|EMBL:GAF36430.1};
RA   Yuki M., Oshima K., Suda W., Kitahara M., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Two Lactobacillus Strains, L. farraginis JCM
RT   14108T and L. composti JCM 14202T, Isolated from Compost of Distilled
RT   Shochu Residue.";
RL   Genome Announc. 2:e00257-14(2014).
RN   [2] {ECO:0000313|EMBL:KRM09500.1, ECO:0000313|Proteomes:UP000051966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18382 {ECO:0000313|EMBL:KRM09500.1,
RC   ECO:0000313|Proteomes:UP000051966};
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:GAF36430.1}.
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DR   EMBL; BAKI01000011; GAF36430.1; -; Genomic_DNA.
DR   EMBL; AZFY01000045; KRM09500.1; -; Genomic_DNA.
DR   RefSeq; WP_035179157.1; NZ_BAKI01000011.1.
DR   AlphaFoldDB; X0QCU2; -.
DR   STRING; 1423743.FD41_GL002559; -.
DR   PATRIC; fig|1423743.5.peg.2626; -.
DR   OrthoDB; 9808023at2; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000019488; Unassembled WGS sequence.
DR   Proteomes; UP000051966; 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:GAF36430.1}.
FT   DOMAIN          1..236
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   256 AA;  28540 MW;  4710CFAA8A77ED03 CRC64;
     MVKKTAYERV QAARSTKKIS TDELIHGLID NFFELHGDRS DGDDQAIIGG VGLLNDEPVT
     VVGIRKGANT DENIKRHFGS PEPEGYRKAL RLMKQAEKFH RPILALVNTP GAWPDVEAEY
     HGIGSAIAQC LQVGMQLKVP YISVIVGEGG SGGAIALACG DKVFMFEDSI YSVLSPEGYA
     SIMWKDSSKV AQAAEDLKLT PDHLLKSGII DQIIHEYRPG DDLKPLRDFL YNQFNELKNL
     PVDELLRQRK ERYRKF
//
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