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THS2_VITVI
ID   THS2_VITVI              Reviewed;         392 AA.
AC   P51070; A5BBF1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Stilbene synthase 2;
DE            EC=2.3.1.95;
DE   AltName: Full=PSV21;
DE   AltName: Full=Resveratrol synthase 2;
DE   AltName: Full=Trihydroxystilbene synthase 2;
DE            Short=StSy 2;
GN   ORFNames=GSVIVT00004047001, LOC100246143, VITISV_010833;
GN   and
GN   ORFNames=GSVIVT00008253001, LOC100259169, VITISV_024260;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Optima;
RX   PubMed=1898048; DOI=10.1016/0003-9861(91)90234-a;
RA   Melchior F., Kindl H.;
RT   "Coordinate- and elicitor-dependent expression of stilbene synthase and
RT   phenylalanine ammonia-lyase genes in Vitis cv. Optima.";
RL   Arch. Biochem. Biophys. 288:552-557(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Lambrusco Foglia Frastagliata;
RX   PubMed=8193299; DOI=10.1007/bf00029856;
RA   Sparvoli F., Martin C., Scienza A., Gavazzi G., Tonelli C.;
RT   "Cloning and molecular analysis of structural genes involved in flavonoid
RT   and stilbene biosynthesis in grape (Vitis vinifera L.).";
RL   Plant Mol. Biol. 24:743-755(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024;
RX   PubMed=17721507; DOI=10.1038/nature06148;
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir;
RX   DOI=10.1371/journal.pone.0001326;
RA   Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA   Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA   Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA   Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA   Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA   Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA   Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA   Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA   Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA   Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT   "A high quality draft consensus sequence of the genome of a heterozygous
RT   grapevine variety.";
RL   PLoS ONE 2:E1326-E1326(2007).
CC   -!- FUNCTION: Mediates resistance to pathogens which are sensitive to
CC       stilbenes. {ECO:0000250}.
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   -!- PATHWAY: Phytoalexin biosynthesis; 3,4',5-trihydroxystilbene
CC       biosynthesis; 3,4',5-trihydroxystilbene from trans-4-coumarate: step
CC       2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By stress.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; S63221; AAB19887.2; -; mRNA.
DR   EMBL; X76892; CAA54221.1; -; mRNA.
DR   EMBL; AM453354; CAN69968.1; -; Genomic_DNA.
DR   EMBL; AM463938; CAN68069.1; -; Genomic_DNA.
DR   RefSeq; XP_003634068.1; XM_003634020.3.
DR   RefSeq; XP_019081580.1; XM_019226035.1.
DR   AlphaFoldDB; P51070; -.
DR   SMR; P51070; -.
DR   STRING; 29760.VIT_16s0100g01010.t01; -.
DR   GeneID; 100853406; -.
DR   GeneID; 100855299; -.
DR   KEGG; vvi:100853406; -.
DR   eggNOG; ENOG502QRSY; Eukaryota.
DR   HOGENOM; CLU_034992_2_0_1; -.
DR   UniPathway; UPA00372; UER00548.
DR   ExpressionAtlas; P51070; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050350; F:trihydroxystilbene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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; PTHR11877; 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; SSF53901; 2.
DR   PROSITE; PS00441; CHALCONE_SYNTH; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Cytoplasm; Plant defense; Stress response; Transferase.
FT   CHAIN           1..392
FT                   /note="Stilbene synthase 2"
FT                   /id="PRO_0000216083"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10023"
FT   BINDING         55..58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         305..307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        39
FT                   /note="Y -> F (in Ref. 2; CAA54221)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        160..161
FT                   /note="YH -> DQ (in Ref. 1; AAB19887)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        193
FT                   /note="I -> S (in Ref. 1; AAB19887)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   392 AA;  42758 MW;  30200ABC20660E86 CRC64;
     MASVEEIRNA QRAKGPATIL AIGTATPDHC VYQSDYADYY FRVTKSEHMT ALKKKFNRIC
     DKSMIKKRYI HLTEEMLEEH PNIGAYMAPS LNIRQEIITA EVPKLGKEAA LKALKEWGQP
     KSKITHLVFC TTSGVEMPGA DYKLANLLGL EPSVRRVMLY HQGCYAGGTV LRTAKDLAEN
     NAGARVLVVC SEITVVTFRG PSEDALDSLV GQALFGDGSA AVIVGSDPDI SIERPLFQLV
     SAAQTFIPNS AGAIAGNLRE VGLTFHLWPN VPTLISENIE KCLTQAFDPL GISDWNSLFW
     IAHPGGPAIL DAVEAKLNLD KKKLEATRHV LSEYGNMSSA CVLFILDEMR KKSLKGERAT
     TGEGLDWGVL FGFGPGLTIE TVVLHSIPMV TN
 
 
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