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Entry: A0A089YSS1_9PSED
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ID   A0A089YSS1_9PSED        Unreviewed;       429 AA.
AC   A0A089YSS1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2 {ECO:0000256|ARBA:ARBA00014657, ECO:0000256|PIRNR:PIRNR000447};
DE            EC=2.3.1.179 {ECO:0000256|ARBA:ARBA00012356, ECO:0000256|PIRNR:PIRNR000447};
GN   ORFNames=LT40_08375 {ECO:0000313|EMBL:AIS17412.1};
OS   Pseudomonas rhizosphaerae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS17412.1, ECO:0000313|Proteomes:UP000029499};
RN   [1] {ECO:0000313|EMBL:AIS17412.1, ECO:0000313|Proteomes:UP000029499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS17412.1};
RX   PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA   Kwak Y., Jung B.K., Shin J.H.;
RT   "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM 16299T),
RT   a phosphate-solubilizing rhizobacterium for bacterial biofertilizer.";
RL   J. Biotechnol. 193:137-138(2015).
CC   -!- FUNCTION: Involved in the type II fatty acid elongation cycle.
CC       Catalyzes the elongation of a wide range of acyl-ACP by the addition of
CC       two carbons from malonyl-ACP to an acyl acceptor. Can efficiently
CC       catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP)
CC       to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in
CC       the thermal regulation of fatty acid composition.
CC       {ECO:0000256|PIRNR:PIRNR000447}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(11Z)-
CC         octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:55040,
CC         Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:10800,
CC         Rhea:RHEA-COMP:14074, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:83989,
CC         ChEBI:CHEBI:138538; EC=2.3.1.179;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000447};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC         + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000447};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|PIRNR:PIRNR000447}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC       ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
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DR   EMBL; CP009533; AIS17412.1; -; Genomic_DNA.
DR   RefSeq; WP_043188728.1; NZ_CP009533.1.
DR   AlphaFoldDB; A0A089YSS1; -.
DR   STRING; 216142.LT40_08375; -.
DR   KEGG; prh:LT40_08375; -.
DR   eggNOG; COG0304; Bacteria.
DR   HOGENOM; CLU_000022_69_2_6; -.
DR   OrthoDB; 9808669at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000029499; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00834; KAS_I_II; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR03150; fabF; 1.
DR   PANTHER; PTHR11712:SF321; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 2; 1.
DR   PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   PIRSF; PIRSF000447; KAS_II; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|PIRNR:PIRNR000447};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW   ECO:0000256|PIRNR:PIRNR000447};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|PIRNR:PIRNR000447};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029499};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
FT   DOMAIN          7..425
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   ACT_SITE        177
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000447-1"
SQ   SEQUENCE   429 AA;  44309 MW;  4EC8A55A6BC0028D CRC64;
     MNTQDGQKRI VVTGAGLVTP LGCGVYEVWR RLLAGMSGIR ALPEHIGEGT GVAVAGQVPT
     LEMDPVAGYN ADALIPAKER KKMDRFIEFA LVAAHEALTQ AQWHPTDEAQ QQRTATVIGS
     GVGGFGALAG AVRTTDERGP RRLSPFTAPS FLANMAAGHV SISNGFKGPL GAPVTACAAG
     VQAIGDAARL IRSGEADIAL CGGTEAAIDR VTLGCFAAAR ALSTEFNDRP AEASRPFDRD
     RDGFVMSEGA GLLVIESLEH ALARGATPLA ELIGYGTSAD AYHLTAGPED GSGARRAMEQ
     ALRQGGIGPE DVQHINAHAT STPVGDKGEL AAIRALFGTR AGLAITSTKS ATGHLLGAAG
     GIEAIFTVLA LRDQTVPPTL NLQTPDEAAH GLDLVALTAR KTPMTHALSN GFGFGGVNAS
     ALFRRWEGQ
//
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