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Database: UniProt
Entry: F6HP23_VITVI
LinkDB: F6HP23_VITVI
Original site: F6HP23_VITVI 
ID   F6HP23_VITVI            Unreviewed;       392 AA.
AC   F6HP23;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=trihydroxystilbene synthase {ECO:0000256|ARBA:ARBA00044056};
DE            EC=2.3.1.95 {ECO:0000256|ARBA:ARBA00044056};
GN   OrderedLocusNames=VIT_16s0100g01100 {ECO:0000313|EMBL:CCB56429.1};
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:CCB56429.1, 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   -!- 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; CCB56429.1; -; Genomic_DNA.
DR   RefSeq; XP_002264455.1; XM_002264419.4.
DR   AlphaFoldDB; F6HP23; -.
DR   SMR; F6HP23; -.
DR   STRING; 29760.F6HP23; -.
DR   PaxDb; 29760-VIT_16s0100g01100-t01; -.
DR   GeneID; 100263437; -.
DR   KEGG; vvi:100263437; -.
DR   eggNOG; ENOG502QRSY; Eukaryota.
DR   HOGENOM; CLU_034992_2_0_1; -.
DR   InParanoid; F6HP23; -.
DR   OrthoDB; 1015444at2759; -.
DR   Proteomes; UP000009183; Chromosome 16.
DR   ExpressionAtlas; F6HP23; 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; 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.
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;  42994 MW;  4B02FD7139396277 CRC64;
     MASVEEIRNA QRAKGPATIL AIGTATPDNC IYQSDYADYY FRVTKSEHMT ELKKKFNRIC
     EKSMIKKRYI HLTEKMLEEH PNIGAYMAPS LNIRQEIITA EIPKLGKEAA LKALKEWGQP
     KSKITHLVFC TTSGVEMPGA DYKLANLLGL DNSVRRVMLY HQGCHAGGTV LRTAKDLAEN
     NAGARVLVVC SEITVVTFRG PSEEALDSLV GQVLFGDGSA AVIVGSDPDL SIERPHFQLI
     SAAQTFIPNS QGAIAGNLRE VGLTFHLWPS VPTLISENIE KCLTQAFDPL GISDWNSLFW
     IAHPGGPAIL DAVEAKLNLE KKKLEATRHV LSEYGNMSSA CVLFILDEMR KKSLKREKAT
     TGDGLDWGVL FGFGPGLTIE TVVLRSIPTV IN
//
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