ID G0RCX7_HYPJQ Unreviewed; 431 AA.
AC G0RCX7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase {ECO:0000256|PIRNR:PIRNR000447};
GN ORFNames=TRIREDRAFT_120712 {ECO:0000313|EMBL:EGR50879.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR50879.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR50879.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] +
CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460;
CC Evidence={ECO:0000256|ARBA:ARBA00023361};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837;
CC Evidence={ECO:0000256|ARBA:ARBA00023361};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] +
CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464;
CC Evidence={ECO:0000256|ARBA:ARBA00023414};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853;
CC Evidence={ECO:0000256|ARBA:ARBA00023414};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-
CC oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649,
CC Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477,
CC ChEBI:CHEBI:78478; Evidence={ECO:0000256|ARBA:ARBA00023341};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901;
CC Evidence={ECO:0000256|ARBA:ARBA00023341};
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 EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00023389};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC Evidence={ECO:0000256|ARBA:ARBA00023389};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] +
CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456;
CC Evidence={ECO:0000256|ARBA:ARBA00023403};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821;
CC Evidence={ECO:0000256|ARBA:ARBA00023403};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469;
CC Evidence={ECO:0000256|ARBA:ARBA00023396};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869;
CC Evidence={ECO:0000256|ARBA:ARBA00023396};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-
CC [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473;
CC Evidence={ECO:0000256|ARBA:ARBA00023348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885;
CC Evidence={ECO:0000256|ARBA:ARBA00023348};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
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; GL985059; EGR50879.1; -; Genomic_DNA.
DR RefSeq; XP_006963413.1; XM_006963351.1.
DR AlphaFoldDB; G0RCX7; -.
DR STRING; 431241.G0RCX7; -.
DR EnsemblFungi; EGR50879; EGR50879; TRIREDRAFT_120712.
DR GeneID; 18482940; -.
DR KEGG; tre:TRIREDRAFT_120712; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_120712; -.
DR eggNOG; KOG1394; Eukaryota.
DR HOGENOM; CLU_000022_69_2_1; -.
DR OrthoDB; 546841at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 2.
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:SF336; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE, MITOCHONDRIAL; 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 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:UP000008984};
KW Transferase {ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 1..429
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT ACT_SITE 176
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000447-1"
SQ SEQUENCE 431 AA; 45666 MW; CAF4A976359053D4 CRC64;
MRRVVVTGLG AITPLGLGIR RTWTRLIAGE SGIVSVAERE PRQRWRELTC TVAGVVPQGA
GGRAHGVWRA DDWLSAAEQR RMSLFTQYAI AASDMALEDA GWNASRLEDQ EATGVCLGSG
IGNLEEMYET SLSHSRDGYR KVSPLFVPKL LINMAAGHIA MRHGFQGPNH AATTACTTGA
HSIGDAARFI AHGDADVMVA GGAESCIHPL TFAGFGRARS LTTAYNDRPQ SACRPFDADR
DGFVIAEGAA VCVLEELEHA KARGARIYAE VRGYGCSGDA HHMTAPREDG HGAYMAMKRA
LKSAGIKPSQ VDYVNAHATS TQVGDSAEAA AIKRIMLGEE GVSSESQVTV SGTKGAIGHL
LGAAGAIEAL FCILAIDQGI VPATLNLERP DVGVDFNYVP QQSQEKDVRV ALSNSFGFGG
TNSTLVFSRL E
//
