ID   BEKAS_PSEAE             Reviewed;         350 AA.
AC   Q9HYV7;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Beta-ketodecanoyl-[acyl-carrier-protein] synthase {ECO:0000305};
DE            EC=2.3.1.207 {ECO:0000269|PubMed:22753057};
GN   OrderedLocusNames=PA3286 {ECO:0000312|EMBL:AAG06674.1};
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=22753057; DOI=10.1128/jb.00860-12;
RA   Yuan Y., Leeds J.A., Meredith T.C.;
RT   "Pseudomonas aeruginosa directly shunts beta-oxidation degradation
RT   intermediates into de novo fatty acid biosynthesis.";
RL   J. Bacteriol. 194:5185-5196(2012).
CC   -!- FUNCTION: Catalyzes the condensation of octanoyl-CoA, obtained from
CC       exogenously supplied fatty acids via beta-oxidation, with malonyl-
CC       [acyl-carrier protein], forming 3-oxodecanoyl-[acyl-carrier protein],
CC       an intermediate of the fatty acid elongation cycle that can then be
CC       extended to supply all of the cellular fatty acid needs. The enzyme
CC       thereby shunts fatty acid degradation intermediates from the beta-
CC       oxidation pathway into de novo fatty acid biosynthesis.
CC       {ECO:0000269|PubMed:22753057}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + malonyl-[ACP] + octanoyl-CoA = 3-oxodecanoyl-[ACP] +
CC         CO2 + CoA; Xref=Rhea:RHEA:42264, Rhea:RHEA-COMP:9623, Rhea:RHEA-
CC         COMP:9637, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57386, ChEBI:CHEBI:78449, ChEBI:CHEBI:78464;
CC         EC=2.3.1.207; Evidence={ECO:0000269|PubMed:22753057};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000269|PubMed:22753057}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000305}.
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DR   EMBL; AE004091; AAG06674.1; -; Genomic_DNA.
DR   PIR; E83236; E83236.
DR   RefSeq; NP_251976.1; NC_002516.2.
DR   RefSeq; WP_003119670.1; NC_002516.2.
DR   AlphaFoldDB; Q9HYV7; -.
DR   SMR; Q9HYV7; -.
DR   STRING; 287.DR97_4643; -.
DR   PaxDb; Q9HYV7; -.
DR   PRIDE; Q9HYV7; -.
DR   EnsemblBacteria; AAG06674; AAG06674; PA3286.
DR   GeneID; 882449; -.
DR   KEGG; pae:PA3286; -.
DR   PATRIC; fig|208964.12.peg.3437; -.
DR   PseudoCAP; PA3286; -.
DR   HOGENOM; CLU_039592_4_2_6; -.
DR   InParanoid; Q9HYV7; -.
DR   OMA; LFGCPGW; -.
DR   PhylomeDB; Q9HYV7; -.
DR   BioCyc; MetaCyc:MON-17586; -.
DR   BioCyc; PAER208964:G1FZ6-3347-MON; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0061990; F:beta-ketodecanoyl-[acyl-carrier-protein] synthase activity; IMP:CACAO.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042758; P:long-chain fatty acid catabolic process; IMP:CACAO.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR013751; ACP_syn_III.
DR   InterPro; IPR013747; ACP_syn_III_C.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF08545; ACP_syn_III; 1.
DR   Pfam; PF08541; ACP_syn_III_C; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..350
FT                   /note="Beta-ketodecanoyl-[acyl-carrier-protein] synthase"
FT                   /id="PRO_0000430809"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000250|UniProtKB:P0AAI5"
SQ   SEQUENCE   350 AA;  38171 MW;  2482AB4C8700A66A CRC64;
     MESFNTFVRQ YNDQHAEAIA KGELEALAES SSAFIEKASG IKSRFVMNKE GILDPQRMVP
     YLPERSNDEW SILCEMAVAA AREALQRAGR SAADIDGVIV ACSNLQRAYP AIAVEVQAAL
     GIQGYGYDMN VACSSATFGI QAATTAIQTG QARAILMVNP EICTGHLNFR DRDSHFIFGD
     ACTAVIVERA DLAVSKHQFD IVSTRLLTQF SNNIRNNFGF LNRADESGIG KRDKLFVQEG
     RKVFKDVCPM VAELIGEHLA ANEIQVAEVK RFWLHQANLN MNLLITRKLL GRDAEAHEAP
     VILDSYANTS SAGSVIALHK HQDDLPSGAI GVLSSFGAGY SIGSVILRKH