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Database: UniProt/TrEMBL
Entry: E1UR23_BACAS
LinkDB: E1UR23_BACAS
Original site: E1UR23_BACAS 
ID   E1UR23_BACAS            Unreviewed;       412 AA.
AC   E1UR23;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   26-NOV-2014, entry version 24.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2 {ECO:0000256|PIRNR:PIRNR000447};
DE            EC=2.3.1.179 {ECO:0000256|PIRNR:PIRNR000447};
GN   Name=fabF {ECO:0000313|EMBL:CBI42333.1};
GN   OrderedLocusNames=BAMF_1207 {ECO:0000313|EMBL:CBI42333.1};
OS   Bacillus amyloliquefaciens (strain ATCC 23350 / DSM 7 / BCRC 11601 /
OS   NBRC 15535 / NRRL B-14393).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=692420 {ECO:0000313|EMBL:CBI42333.1, ECO:0000313|Proteomes:UP000006562};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM7;
RX   DOI=10.1099/ijs.0.023267-0 ;
RA   Borriss R., Chen X., Rueckert C., Blom J., Becker A., Baumgarth B.,
RA   Fan B., Pukall R., Schumann P., Sproer C., Junge H., Vater J.,
RA   Puhler A., Klenk H.P.;
RT   "Relationship of Bacillus amyloliquefaciens clades associated with
RT   strains DSM7T and FZB42: a proposal for Bacillus amyloliquefaciens
RT   subsp. amyloliquefaciens subsp. nov. and Bacillus amyloliquefaciens
RT   subsp. plantarum subsp. nov. based on their discriminating complete
RT   genome sequences.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2010).
RN   [2] {ECO:0000313|Proteomes:UP000006562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23350 / DSM 7 / BCRC 11601 / NBRC 15535 / NRRL B-14393
RC   {ECO:0000313|Proteomes:UP000006562};
RX   PubMed=21262282; DOI=10.1016/j.jbiotec.2011.01.006;
RA   Ruckert C., Blom J., Chen X., Reva O., Borriss R.;
RT   "Genome sequence of B. amyloliquefaciens type strain DSM7(T) reveals
RT   differences to plant-associated B. amyloliquefaciens FZB42.";
RL   J. Biotechnol. 155:78-85(2011).
CC   -!- FUNCTION: Catalyzes the condensation reaction of fatty acid
CC       synthesis by the addition to an acyl acceptor of two carbons from
CC       malonyl-ACP. {ECO:0000256|PIRNR:PIRNR000447}.
CC   -!- CATALYTIC ACTIVITY: (Z)-hexadec-11-enoyl-[acyl-carrier-protein] +
CC       malonyl-[acyl-carrier-protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-
CC       carrier-protein] + CO(2) + [acyl-carrier-protein].
CC       {ECO:0000256|PIRNR:PIRNR000447}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|PIRNR:PIRNR000447}.
CC   -!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family.
CC       {ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
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DR   EMBL; FN597644; CBI42333.1; -; Genomic_DNA.
DR   RefSeq; YP_003919803.1; NC_014551.1.
DR   EnsemblBacteria; CBI42333; CBI42333; BAMF_1207.
DR   GeneID; 9778758; -.
DR   KEGG; bao:BAMF_1207; -.
DR   PATRIC; 42471438; VBIBacAmy172706_1297.
DR   HOGENOM; HOG000060166; -.
DR   KO; K09458; -.
DR   BioCyc; BAMY692420:GHU2-1294-MONOMER; -.
DR   UniPathway; UPA00094; -.
DR   GO; GO:0033817; F:beta-ketoacyl-acyl-carrier-protein synthase II activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR016038; Thiolase-like_subgr.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   PIRSF; PIRSF000447; KAS_II; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   TIGRFAMs; TIGR03150; fabF; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|PIRNR:PIRNR000447,
KW   ECO:0000313|EMBL:CBI42333.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006562};
KW   Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR000447};
KW   Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000447};
KW   Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000447};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR000447};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000447,
KW   ECO:0000256|RuleBase:RU003694}.
FT   ACT_SITE    164    164       {ECO:0000256|PIRSR:PIRSR000447-1}.
SQ   SEQUENCE   412 AA;  43771 MW;  024D2ACCE7438D03 CRC64;
     MSKKRVVVTG LGALSPLGND AETSWKNAIS GVSGIGPITR VESDEYPAKV AAELKDFNVE
     NYMDKKEARK MDRFTQYAVV AAKMAVEDAG LNITEEIAPR VGVWVGSGIG GLETLESQFE
     IFLTKGPRRV SPFFVPMMIP DMATGQISIA LGAKGVNSCT VTACATGTNS IGDAFKVIQR
     GDADAMISGG TEAPLTRMSF AGFSANKALS TNPDPKTASR PFDKNRDGFV MGEGAGIVVL
     EELEHALARG AKIYGEIVGY GSTGDAYHIT APAQDGEGGA RAMQEAIKDA GIKPEEIDYI
     NAHGTSTYYN DKYETKAIKT VFGDHAYKLA VSSTKSMTGH LLGAAGGIEA IFSVMAIKDG
     IIPPTINIET PDEECDLDYV PDKAREQDVN IVLSNSLGFG GHNATLIFKK YQ
//
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