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Database: UniProt/TrEMBL
Entry: Q65JQ8_BACLD
LinkDB: Q65JQ8_BACLD
Original site: Q65JQ8_BACLD 
ID   Q65JQ8_BACLD            Unreviewed;       319 AA.
AC   Q65JQ8; Q62V63;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   19-FEB-2014, entry version 70.
DE   RecName: Full=Malonyl CoA-acyl carrier protein transacylase;
DE            EC=2.3.1.39;
GN   Name=fabD; OrderedLocusNames=BL02314, BLi01811;
OS   Bacillus licheniformis (strain DSM 13 / ATCC 14580).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13 / ATCC 14580 [Novozymes];
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G.,
RA   Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L.,
RA   Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N.,
RA   Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13, and DSM 13 / ATCC 14580 [Goettingen];
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H.,
RA   Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R.,
RA   Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an
RT   organism with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 13;
RA   Wiegand S., Hertel R., Dietrich S., Volland S., Liesegang H.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Malonyl-CoA + [acyl-carrier-protein] = CoA +
CC       malonyl-[acyl-carrier-protein].
CC   -!- SIMILARITY: Belongs to the fabD family.
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DR   EMBL; CP000002; AAU23346.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU40706.1; -; Genomic_DNA.
DR   RefSeq; YP_006713187.1; NC_006322.1.
DR   RefSeq; YP_078984.1; NC_006270.3.
DR   ProteinModelPortal; Q65JQ8; -.
DR   STRING; 279010.BL02314; -.
DR   EnsemblBacteria; AAU23346; AAU23346; BL02314.
DR   EnsemblBacteria; AAU40706; AAU40706; BLi01811.
DR   GeneID; 3030977; -.
DR   GeneID; 3101534; -.
DR   KEGG; bld:BLi01811; -.
DR   KEGG; bli:BL02314; -.
DR   PATRIC; 18949221; VBIBacLic203714_1814.
DR   eggNOG; COG0331; -.
DR   HOGENOM; HOG000036504; -.
DR   KO; K00645; -.
DR   OMA; PVVTNVE; -.
DR   OrthoDB; EOG6W19KW; -.
DR   ProtClustDB; CLSK2460921; -.
DR   BioCyc; BLIC279010:GJ2P-1796-MONOMER; -.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.366.10; -; 2.
DR   InterPro; IPR001227; Ac_transferase_dom.
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   SUPFAM; SSF52151; SSF52151; 2.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   TIGRFAMs; TIGR00128; fabD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Complete proteome; Transferase.
SQ   SEQUENCE   319 AA;  34282 MW;  0400C5434B3687C7 CRC64;
     MGKIAFLFPG QGSQHIGMGH ELYEKEPNAK KIFEEADQTL ETKLSTLMFE GDAKELTLTY
     NAQPSLLTAS IAALEKLKEY GIKADYAAGH SLGEYSALVA AGALSFKDAV YAVRKRGEFM
     NEAVPAGEGA MAAILGMDSQ ALKEVTDKIS EEGNLVQLAN LNCPGQIVIS GTAKGVELAS
     ELAKEKGAKR AIPLEVSGPF HSELMKPAAD KLREVLDACT INDAAIPVVS NVTADFVTDK
     DDIKNKLIEQ LYSPVRFEET ISRLIDEGVT TFIEIGPGKV LSGLVKKVNR RVKTIAVSDP
     NTIELAVQTL KEENENAGK
//
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