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E13B_VITVI
ID   E13B_VITVI              Reviewed;         344 AA.
AC   A7PQW3; F6GWB5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase {ECO:0000250|UniProtKB:Q03467};
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase {ECO:0000250|UniProtKB:Q03467};
DE            Short=(1->3)-beta-glucanase {ECO:0000250|UniProtKB:Q03467};
DE   AltName: Full=Beta-1,3-endoglucanase {ECO:0000250|UniProtKB:Q03467};
DE   Flags: Precursor;
GN   OrderedLocusNames=VIT_06s0061g00120;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000269|PubMed:17721507};
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   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 143-158.
RA   Belchi-Navarro S., Almagro L., Bru R., Pedreno M.A.;
RL   Submitted (JUL-2008) to UniProtKB.
CC   -!- FUNCTION: Implicated in the defense of plants against pathogens.
CC       {ECO:0000250|UniProtKB:Q03467}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC         beta-D-glucans.; EC=3.2.1.39;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000255}.
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DR   EMBL; FN594957; CCB44250.1; -; Genomic_DNA.
DR   RefSeq; XP_002278123.1; XM_002278087.4.
DR   AlphaFoldDB; A7PQW3; -.
DR   SMR; A7PQW3; -.
DR   STRING; 29760.VIT_06s0061g00120.t01; -.
DR   PRIDE; A7PQW3; -.
DR   EnsemblPlants; Vitvi06g01917_t001; Vitvi06g01917_P001; Vitvi06g01917.
DR   GeneID; 100265368; -.
DR   Gramene; Vitvi06g01917_t001; Vitvi06g01917_P001; Vitvi06g01917.
DR   KEGG; vvi:100265368; -.
DR   eggNOG; ENOG502QQ3M; Eukaryota.
DR   HOGENOM; CLU_024953_0_0_1; -.
DR   InParanoid; A7PQW3; -.
DR   OrthoDB; 966331at2759; -.
DR   BRENDA; 3.2.1.39; 6671.
DR   Proteomes; UP000009183; Chromosome 6.
DR   ExpressionAtlas; A7PQW3; baseline and differential.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR044965; Glyco_hydro_17_plant.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR32227; PTHR32227; 1.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase;
KW   Pathogenesis-related protein; Plant defense; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..344
FT                   /note="Glucan endo-1,3-beta-glucosidase"
FT                   /id="PRO_0000363744"
FT   ACT_SITE        123
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        268
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
SQ   SEQUENCE   344 AA;  37093 MW;  FB0E7417F0EB1A72 CRC64;
     MALTRNRPFV VVLLLGFVIM STITIGAQSI GVCYGRNGNN LPSASQVINL YKSNGIGSMR
     IYDPNSDTLQ ALRGSDIELI LDVPNTDLQS LASDASAAAT WVQNNVVNYA SEVKFRYIAV
     GNEVLPTGSN AQYAQYVLPA MKNVQSAITS AGLQDQIKVS TATFSAVLGK SYPPSEGSFS
     DDVSSFINPI ISFLAENGSP LLANIYPYFS YTGDTQNIRL DYALFTASGV VVQDGSYQYQ
     NLFDALLDAL YAALEKAGGS NLKIVVSESG WPSEGGTAAT VDNARTYYKN LINHVKGGTP
     RKSGAIETYL FAMFDENQKT GLETEKHFGL FTPGQESKYQ ISFS
 
 
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