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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//