ID   FABD_BUCBP              Reviewed;         311 AA.
AC   Q89AH0;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Malonyl CoA-acyl carrier protein transacylase;
DE            Short=MCT;
DE            EC=2.3.1.39;
GN   Name=fabD; OrderedLocusNames=bbp_320;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27042.1; -; Genomic_DNA.
DR   RefSeq; WP_011091443.1; NC_004545.1.
DR   AlphaFoldDB; Q89AH0; -.
DR   SMR; Q89AH0; -.
DR   STRING; 224915.bbp_320; -.
DR   KEGG; bab:bbp_320; -.
DR   eggNOG; COG0331; Bacteria.
DR   HOGENOM; CLU_030558_0_0_6; -.
DR   OrthoDB; 9808564at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000601; 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; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 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; IPR016036; Malonyl_transacylase_ACP-bd.
DR   PANTHER; PTHR42681; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42681:SF1; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   PIRSF; PIRSF000446; Mct; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..311
FT                   /note="Malonyl CoA-acyl carrier protein transacylase"
FT                   /id="PRO_0000194211"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   311 AA;  35797 MW;  9E9CD2AEA0C6BC03 CRC64;
     MFKYTLLFPG QNDINRKKIL SPFFSKNKIV QSIFRESSEY IGYDIWKLIQ DDPKKKLKNN
     KYSQLVTLVS SIAIYELWKN KQCTHPNLVI GHSLGEYTAL VCSQSLKLSD AIQLIITRYK
     FMMEAMSKKI GLMTAIIGLN ERTIRKLLKK YDYSHEVSIA CINTDNQIVL SGERNSVKHI
     NLHCKKAGAK NIINLYIHPP SHCTLMKKAS KKLLYVLKHT TFKIPIYPVI SSTSLKFQNS
     EQAIRISLAK QIYSTVRWNS IIKYIKKDIF IFLEVSTKSI LTNLNKNIIK KSLSISLNCQ
     ANFLKALKII L
//