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Database: UniProt
Entry: F6HP35_VITVI
LinkDB: F6HP35_VITVI
Original site: F6HP35_VITVI 
ID   F6HP35_VITVI            Unreviewed;       392 AA.
AC   F6HP35;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=trihydroxystilbene synthase {ECO:0000256|ARBA:ARBA00044056};
DE            EC=2.3.1.95 {ECO:0000256|ARBA:ARBA00044056};
GN   OrderedLocusNames=VIT_16s0100g00940 {ECO:0000313|EMBL:CCB56441.1};
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:CCB56441.1, 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; CCB56441.1; -; Genomic_DNA.
DR   RefSeq; XP_003634070.1; XM_003634022.3.
DR   AlphaFoldDB; F6HP35; -.
DR   STRING; 29760.F6HP35; -.
DR   PaxDb; 29760-VIT_16s0100g00940-t01; -.
DR   GeneID; 100853526; -.
DR   KEGG; vvi:100853526; -.
DR   eggNOG; ENOG502QRSY; Eukaryota.
DR   HOGENOM; CLU_034992_2_0_1; -.
DR   InParanoid; F6HP35; -.
DR   OrthoDB; 911439at2759; -.
DR   Proteomes; UP000009183; Chromosome 16.
DR   ExpressionAtlas; F6HP35; 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..387
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;  42812 MW;  B5BC1532988B4EC8 CRC64;
     MASVEEIRNA QRAKGPATVL AIGTATPDNC LYQSDFADYY FRVTKSEHMT ELKKKFNRIC
     DKSMIKKRYI HLTEEMLEEH PNIGAYMAPS LNIRQEIITA EVPKLGKEAA LKALKEWGQP
     KSKITHLVFC TTSGVEMPGA DYKLANLLGL EPSVRRVMLY HQGCYAGGTV LRIAKDLAEN
     NAGARVLVVC SEITVVTFRG PSETALDSLV GQALFGDGSA AVIIGSDPDI SIERPLFQLV
     SAAQTFIPNS AGAIAGNLRE VGLTFQLWPN VPSLISENIE KCLTKAFDPI GISDWNSLFW
     IAHPGGPAIL DAVEAKLNLD KQKLKATRHI LSEYGNMSSA CVLFILDEMR KKSLKEGKIT
     TGEGLDWGVL FGFGPGLTIE TVVLHSVQMD SN
//
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