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Database: UniProt
Entry: F6HP18_VITVI
LinkDB: F6HP18_VITVI
Original site: F6HP18_VITVI 
ID   F6HP18_VITVI            Unreviewed;       392 AA.
AC   F6HP18;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=trihydroxystilbene synthase {ECO:0000256|ARBA:ARBA00044056};
DE            EC=2.3.1.95 {ECO:0000256|ARBA:ARBA00044056};
GN   OrderedLocusNames=VIT_16s0100g01160 {ECO:0000313|EMBL:CCB56424.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB56424.1, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-coumaroyl-CoA + 3 H(+) + 3 malonyl-CoA = 4 CO2 + 4 CoA +
CC         trans-resveratrol; Xref=Rhea:RHEA:11936, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:45713, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57355, ChEBI:CHEBI:57384; EC=2.3.1.95;
CC         Evidence={ECO:0000256|ARBA:ARBA00001104};
CC   -!- PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene
CC       biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step
CC       2/2. {ECO:0000256|ARBA:ARBA00043953}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000256|ARBA:ARBA00005531,
CC       ECO:0000256|RuleBase:RU003633}.
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DR   EMBL; FN596000; CCB56424.1; -; Genomic_DNA.
DR   RefSeq; XP_003634063.1; XM_003634015.3.
DR   AlphaFoldDB; F6HP18; -.
DR   STRING; 29760.F6HP18; -.
DR   PaxDb; 29760-VIT_16s0100g01160-t01; -.
DR   EnsemblPlants; Vitvi16g04353_t001; Vitvi16g04353_P001; Vitvi16g04353.
DR   GeneID; 100852886; -.
DR   Gramene; Vitvi16g04353_t001; Vitvi16g04353_P001; Vitvi16g04353.
DR   KEGG; vvi:100852886; -.
DR   HOGENOM; CLU_034992_2_0_1; -.
DR   InParanoid; F6HP18; -.
DR   OrthoDB; 1015444at2759; -.
DR   Proteomes; UP000009183; Chromosome 16.
DR   ExpressionAtlas; F6HP18; baseline and differential.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR   GO; GO:0050350; F:trihydroxystilbene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030639; P:polyketide biosynthetic process; IBA:GO_Central.
DR   CDD; cd00831; CHS_like; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR012328; Chalcone/stilbene_synt_C.
DR   InterPro; IPR001099; Chalcone/stilbene_synt_N.
DR   InterPro; IPR018088; Chalcone/stilbene_synthase_AS.
DR   InterPro; IPR011141; Polyketide_synthase_type-III.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR11877:SF14; CHALCONE SYNTHASE; 1.
DR   PANTHER; PTHR11877; HYDROXYMETHYLGLUTARYL-COA SYNTHASE; 1.
DR   Pfam; PF02797; Chal_sti_synt_C; 1.
DR   Pfam; PF00195; Chal_sti_synt_N; 1.
DR   PIRSF; PIRSF000451; PKS_III; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00441; CHALCONE_SYNTH; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003633};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Plant defense {ECO:0000256|ARBA:ARBA00022821};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016};
KW   Transferase {ECO:0000256|RuleBase:RU003633}.
FT   DOMAIN          5..228
FT                   /note="Chalcone/stilbene synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00195"
FT   DOMAIN          238..388
FT                   /note="Chalcone/stilbene synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02797"
FT   ACT_SITE        164
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000451-1"
SQ   SEQUENCE   392 AA;  42870 MW;  0C2E8C3263792431 CRC64;
     MASVEEFRNA QRAKGPATIL AIGTATPDHC VYQSDYADYY FRVTKSEHMT ELKKKFNRIC
     DKSMIKKRYI HLTEEMLEEH PNIGAYMAPS LNIRQEIITA EVPRLGRDAA LKALKEWGQP
     KSKITHLVFC TTSGVEMPGA DYKLANLLGL ETSVRRVMLY HQGCYAGGTV LRTAKDLAEN
     NAGARVLVVC SEITVVTFRG PSEDALDSLV GQALFGDGSS AVIVGSDPDV SIERPLFQLV
     SAAQTFIPNS AGAIAGNLRE VGLTFHLWPN VPTLISENIE KCLTQAFDPL GISDWNSLFW
     IAHPGGPAIL DAVEAKLNLE KKKLEATRHV LSEYGNMSSA CVLFILDEMR KKSLKGEKAT
     TGEGLDWGVL FGFGPGLTIE TVVLHSVPMV TN
//
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