ID H3H6B1_PHYRM Unreviewed; 2209 AA.
AC H3H6B1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra86209, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra86209}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra86209};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC Evidence={ECO:0000256|ARBA:ARBA00001572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
CC Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83139; EC=2.3.1.86;
CC Evidence={ECO:0000256|ARBA:ARBA00000343};
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DR EMBL; DS566529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 164328.H3H6B1; -.
DR EnsemblProtists; Phyra86209; Phyra86209; Phyra86209.
DR VEuPathDB; FungiDB:PSURA_86209; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_2_1_1; -.
DR InParanoid; H3H6B1; -.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00828; elong_cond_enzymes; 1.
DR Gene3D; 2.40.128.700; -; 1.
DR Gene3D; 3.30.70.3330; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.25.70; -; 1.
DR Gene3D; 6.10.140.1400; -; 1.
DR Gene3D; 6.10.140.1410; -; 1.
DR Gene3D; 6.10.250.1930; -; 1.
DR Gene3D; 6.10.60.10; -; 1.
DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00101; AcpS; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR002582; ACPS.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR040899; Fas_alpha_ACP.
DR InterPro; IPR047224; FAS_alpha_su_C.
DR InterPro; IPR041550; FASI_helical.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR00556; pantethn_trn; 1.
DR PANTHER; PTHR10982:SF21; FATTY ACID SYNTHASE SUBUNIT BETA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR Pfam; PF01648; ACPS; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 2.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005238};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1424..1937
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1402..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2023..2055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2024..2042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2209 AA; 239764 MW; 4A70A1D528E65651 CRC64;
EVLEPLVELH SEFLIRGSFD DFESTFSIDK STEEFVPSRQ EDVEILKAKG WLEVAAEASV
NVGDHLAFQL TTKKQYASIG SLSSVEVSGT LLREEAGSKV EIGTVEFKSH DVNESPVVAF
LRQVQPEDAK SGGMFANGGS HMLEKPLEIS VPTNALAYAV ASRDLNPIHR SKYAAILGHL
PKGKPIMHGL WTATKVRDLV IQSFGLGVDS NVVDYDVNFD GMVYPGDKLF MQARHIGLDN
GKKVLSVEVV NGSGERVVSA RAVVKQAPMA FVFTGQGSAA VGMGMDRYQE SSVAREIWNR
GDTHLRKTFG FSILDMVRKN PNSITVHFGG KKGRKIREKY MSLTCEDPVT GEIAPLLPEI
NARTQSFSFS APEGLLFATQ FSQPALVLLE KAMFSEIEAA QLIPDDAHFA GHSLGEYAGL
SSFAGALAVE DVVEVVFLRG LIMQKAVKRD AEGRSDYGMV ATNPTRVGPH FTEEVMYKIV
DGVEAASGKL LQVVNFNIQQ RQYVVAGENV NLETLSLALS AFKTMKSTAA EDVEKVIAES
LEQARSRKEK CEQSGRPFTL ARGLATIPLV GIDVPFHSRE LLGGVPSFRA LLRTKFDPQV
LERQLPLLVN RYIPNLVATP FSLERSYFEE VYEATKSPYL AEVLDPMQWK LTTKAQLAHL
LVVELLAYQF ASPVQWIKTQ ALLFSEGGVR RFVEIGPAAT LTNMALRTLQ VGDFPDVPRE
ILWYQRDREV VHFEEETSNI SASEYARGLA AEAAAETAAA AAKAVAESAP TEEAVTPATP
APVVAAPVQQ VPAPAPVAAA PAAADAPVAA LHVLRVLLAV RLNKELGEIK EDTDVKTLCA
GKSAVQNEIL GDLEKEFGGG VPEGAGEVPL KELASKFSGY NALGKVTNGL INKVVASKMP
GGFTMSSIKE YLGTEKGLGA GRMESVLAQS LLLAPQTRFK SDADARKWLD DSVSGYESFA
GVSLARPTMS ATPGAVGMSF NPAPVSIPTV SDKSVEPKHA LLVMLAAKFG KDFSEIPETA
TIKELSAGKS AVQNEIVGDL EKEFGSGPDD AAEMKLAELA GKFPDYASPG KVTSALIAKM
LASKMPGGFG LSAIKEYLSS ERCLPSGRIE SVLLHGLTQN PKQRLTDDGT AKKWLDGVVD
DYAKYTGIDI PYLSKLGGMM AGPAMGQQAM QSSSLPSDFE KRLKSMIADQ IDALSSYLGD
DQLDWHRKIE TEVDMREDLE SSVSHWVAEH GEFYGSGIAG KFDAKKERQY DSYWNWAVQD
AMELYYRTAA AAKAVNPKLN VNESLSLHLC NRATPELVRC MEFVMSRAEV ESDELAQTLK
VLVAQIEACL ITKPVSVQKF NPTVPRLYIL ESGEVEYVEV PREGVVDPIS YVEEVARGLE
YSCTFEMGKG VLGVTSNMTK PIGFEATPTD NGSTTSEDLD SDELENSEDD GATVRIADIQ
SAGTNKAPHT ECTHINVLCA IPQNHNEKES EWPRVRNSSM HCCVNENLKK IVLPHVHVRK
PSDVDPTIRL YDVESTCVLL SCMREMASTG ISFAGKVALL TGCGKNSIGA EIVKALLEGG
ATVFVTTSSF SMKTTTLFRE IYEQHGSRGS RLIVLPFNQA SKMDVEKXAE TIKSGKARIC
IVGGYDDFGE EGAFEFAQMK ATSDSVKETG MGREPKEMCR PCTTTRGGFM ESHGAGIQLL
MDAQLALEMG LPIYGIVALT NTATDKNGRS VPAPGQGILT TAREASSDNS KPSPLLDVEY
RRRQFDDELE SIEKWYAREI ALINGDESRV AFLDEMKVRK VQSAQSMWGD NFFHGRTDIA
PIRGALSVWN LDIDDLGAAS FHGTGTKAND KNESEVTHKQ MAHLGRSPGN PLPVICQKNL
TGHPKGAAAA WMLNGLLQVL NSGLIPGNRQ LDNTCETLRK YDHLVYPNRS FQTVGIKAVV
MKSFGFGQAG GEVLLVHPDC LLSTLPAGEF QHYSARREQR LIKMNTHTQS VITGKQSHIQ
VKNEAPYSSA QESNVYLDPT ARAEYDATSK TWRFGGADSL TANENRRLRA EKRAKKAKAA
ADAASTKKTS ETHSADSSST LLTAINQAAT DLGLSKNMGM GVDVEPVATF ENLNGREDFI
RRNFTDQEMA YCYSAPHPAA SFAGRWAAKE AVIKAISSSS PSEPNLWKGA GAPLREIEIF
MTASGAPSVL LSGYPLQVFN RLGLSKLSVS ISHSGDFAVS QAVANFQQE
//
