ID   FENF_BACIU              Reviewed;         400 AA.
AC   Q9R9J2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Malonyl CoA-acyl carrier protein transacylase;
DE            Short=MCT;
DE            EC=2.3.1.39;
GN   Name=fenF;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6633 / DSM 347 / IFO 3134 / PCI 219 / NRS 231;
RX   PubMed=10557314; DOI=10.1073/pnas.96.23.13294;
RA   Duitman E.H., Hamoen L.W., Rembold M., Venema G., Seitz H., Saenger W.,
RA   Bernhard F., Reinhardt R., Schmidt M., Ullrich C., Stein T., Leenders F.,
RA   Vater J.;
RT   "The mycosubtilin synthetase of Bacillus subtilis ATCC6633: a
RT   multifunctional hybrid between a peptide synthetase, an amino transferase,
RT   and a fatty acid synthase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:13294-13299(1999).
RN   [2]
RP   CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 6633 / DSM 347 / IFO 3134 / PCI 219 / NRS 231;
RX   PubMed=17330903; DOI=10.1002/cbic.200600575;
RA   Aron Z.D., Fortin P.D., Calderone C.T., Walsh C.T.;
RT   "FenF: servicing the mycosubtilin synthetase assembly line in trans.";
RL   ChemBioChem 8:613-616(2007).
CC   -!- FUNCTION: Is involved in the mycosubtilin synthetase assembly, by
CC       catalyzing the transfer of malonyl groups to a specific acyl-carrier-
CC       protein domain on MycA. {ECO:0000269|PubMed:17330903}.
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         Evidence={ECO:0000269|PubMed:17330903};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=45 uM for malonyl-CoA {ECO:0000269|PubMed:17330903};
CC         KM=950 uM for acyl-carrier-protein domain of MycA
CC         {ECO:0000269|PubMed:17330903};
CC   -!- SIMILARITY: Belongs to the FabD family. {ECO:0000305}.
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DR   EMBL; AF184956; AAF08794.1; -; Genomic_DNA.
DR   PIR; T44805; T44805.
DR   AlphaFoldDB; Q9R9J2; -.
DR   SMR; Q9R9J2; -.
DR   PATRIC; fig|1423.172.peg.141; -.
DR   SABIO-RK; Q9R9J2; -.
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-KW.
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; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   TIGRFAMs; TIGR00128; fabD; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Transferase.
FT   CHAIN           1..400
FT                   /note="Malonyl CoA-acyl carrier protein transacylase"
FT                   /id="PRO_0000385454"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        201
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   400 AA;  45222 MW;  2A4430664C90C578 CRC64;
     MNNLAFLFPG QGSQFVGMGK SFWNDFVLAK RLFEEASDAI SMDVKKLCFD GDMTELTRTM
     NAQPAILTVS VIAYQVYMQE IGIKPHFLAG HSLGEYSALV CAGVLSFQEA VKLIRQRGIL
     MQNADPEQLG TMAAITQVYI QPLQDLCTEI STEDFPVGVA CMNSDQQHVI SGHRQAVEFV
     IKKAERMGAN HTYLNVSAPF HSSMMRSASE QFQTALNQYS FRDAEWPIIS NVTAIPYNNG
     HSVREHLQTH MTMPVRWAES MHYLLLHGVT EVIEMGPKNV LVGLLKKITN HIAAYPLGQT
     SDLHLLSDSA ERNENIVNLR KKQLNKMMIQ SIIARNYNKD AKTYSNLTTP LFPQIQLLKE
     RVERKEVELS AEELEHSIHL CQLICEAKQL PTWEQLRILK