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 01-MAY-2013, entry version 66.
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., Baumer 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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 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; EVSGPFH; -.
DR ProtClustDB; CLSK2460921; -.
DR BioCyc; BLIC279010:GJ2P-1796-MONOMER; -.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA: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; Acyl_Trfase/lysoPlipase; 1.
DR SUPFAM; SSF55048; Malonyl_transacylase_ACP-bd; 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
//
