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Database: UniProt
Entry: F6HIS1_VITVI
LinkDB: F6HIS1_VITVI
Original site: F6HIS1_VITVI 
ID   F6HIS1_VITVI            Unreviewed;       366 AA.
AC   F6HIS1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=trihydroxystilbene synthase {ECO:0000256|ARBA:ARBA00044056};
DE            EC=2.3.1.95 {ECO:0000256|ARBA:ARBA00044056};
GN   OrderedLocusNames=VIT_10s0042g00910 {ECO:0000313|EMBL:CCB52117.1};
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:CCB52117.1, 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; FN595766; CCB52117.1; -; Genomic_DNA.
DR   RefSeq; XP_010655919.1; XM_010657617.2.
DR   AlphaFoldDB; F6HIS1; -.
DR   STRING; 29760.F6HIS1; -.
DR   PaxDb; 29760-VIT_10s0042g00910-t01; -.
DR   GeneID; 100244220; -.
DR   KEGG; vvi:100244220; -.
DR   eggNOG; ENOG502QRSY; Eukaryota.
DR   HOGENOM; CLU_034992_2_0_1; -.
DR   InParanoid; F6HIS1; -.
DR   OrthoDB; 883077at2759; -.
DR   Proteomes; UP000009183; Chromosome 10.
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..364
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   366 AA;  40691 MW;  5D8C096A8A915630 CRC64;
     MASVEDIRNA QHAKRLATIL VIGTATPDNY AYQSDYADYY FRVTKSEHMT DLKKKFNRIC
     EKSMIKKRYI HLTEEMLEEH PNMGAYMAPS LNIRQEIITT EVPKLGKEAT LKALKEWGQP
     KSKITHLVFC TTSGVEMPGA DYKLANLLGL ETSVRRVMLY HQGCYAGGTV LRTAKDLAEN
     NAGARVLVVC SEITVVTFRG PSETHLHSLV GQALFGDGST TIIVGSDPDT SIERPLFQLI
     SAAQTFIPNT QGAIVGNLRE VGLTFHLWPN VPTLISENIE KCLTQAFAPL GISDWNSLFW
     IAHPGGPAIL DAVEAKLNLE KKKLEATRHI FSEYGNMSSA CVLFILDEMR KKSLKEERTT
     TGKELD
//
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