ID   FABD_STAAC              Reviewed;         308 AA.
AC   Q5HGK3;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Malonyl CoA-acyl carrier protein transacylase;
DE            Short=MCT;
DE            EC=2.3.1.39;
GN   Name=fabD; OrderedLocusNames=SACOL1244;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SIMILARITY: Belongs to the FabD family. {ECO:0000305}.
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DR   EMBL; CP000046; AAW38078.1; -; Genomic_DNA.
DR   RefSeq; WP_000047348.1; NC_002951.2.
DR   AlphaFoldDB; Q5HGK3; -.
DR   SMR; Q5HGK3; -.
DR   EnsemblBacteria; AAW38078; AAW38078; SACOL1244.
DR   KEGG; sac:SACOL1244; -.
DR   HOGENOM; CLU_030558_0_1_9; -.
DR   OMA; AANYNCP; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000530; Chromosome.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.366.10; -; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR024925; Malonyl_CoA-ACP_transAc.
DR   InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   PIRSF; PIRSF000446; Mct; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   TIGRFAMs; TIGR00128; fabD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Transferase.
FT   CHAIN           1..308
FT                   /note="Malonyl CoA-acyl carrier protein transacylase"
FT                   /id="PRO_0000194221"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        199
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  33635 MW;  C28AEC6CC50805C2 CRC64;
     MSKTAIIFPG QGAQKVGMAQ DLFNNNDQAT EILTSAANTL DFDILETMFT DEEGKLGETE
     NTQPALLTHS SALLAALKNL NPDFTMGHSL GEYSSLVAAD VLSFEDAVKI VRKRGQLMAQ
     AFPTGVGSMA AVLGLDFDKV DEICKSLSSD DKIIEPANIN CPGQIVVSGH KALIDELVEK
     GKSLGAKRVM PLAVSGPFHS SLMKVIEEDF SSYINQFEWR DAKFPVVQNV NAQGETDKEV
     IKSNMVKQLY SPVQFINSTE WLIDQGVDHF IEIGPGKVLS GLIKKINRDV KLTSIQTLED
     VKGWNEND