ID   VICHY_VICSN             Reviewed;         509 AA.
AC   A2SY66;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Vicianin hydrolase {ECO:0000312|EMBL:ABD03937.1};
DE            Short=VH {ECO:0000303|PubMed:17548373};
DE            EC=3.2.1.119;
DE   Flags: Precursor; Fragment;
OS   Vicia sativa subsp. nigra (Common vetch) (Vicia angustifolia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3909;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ABD03937.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-34, FUNCTION, CATALYTIC
RP   ACTIVITY, AND TISSUE SPECIFICITY.
RC   TISSUE=Seed {ECO:0000269|PubMed:17548373};
RX   PubMed=17548373; DOI=10.1093/pcp/pcm065;
RA   Ahn Y.O., Saino H., Mizutani M., Shimizu B., Sakata K.;
RT   "Vicianin hydrolase is a novel cyanogenic beta-glycosidase specific to
RT   beta-vicianoside (6-O-alpha-L-arabinopyranosyl-beta-D-glucopyranoside) in
RT   seeds of Vicia angustifolia.";
RL   Plant Cell Physiol. 48:938-947(2007).
CC   -!- FUNCTION: Hydrolyzes the disaccharide glycosides vicianin, pNP beta-
CC       primeveroside, 2-phenylethyl beta-primeveroside and furcatin.
CC       {ECO:0000269|PubMed:17548373}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-vicianin + H2O = mandelonitrile + vicianose;
CC         Xref=Rhea:RHEA:14041, ChEBI:CHEBI:15377, ChEBI:CHEBI:16177,
CC         ChEBI:CHEBI:16358, ChEBI:CHEBI:16910; EC=3.2.1.119;
CC         Evidence={ECO:0000269|PubMed:17548373};
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in seeds, at moderate
CC       levels in flowers and at low levels in roots, stems and leaves.
CC       {ECO:0000269|PubMed:17548373}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000255}.
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DR   EMBL; DQ371927; ABD03937.1; -; mRNA.
DR   AlphaFoldDB; A2SY66; -.
DR   SMR; A2SY66; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   PRIDE; A2SY66; -.
DR   BioCyc; MetaCyc:MON-17579; -.
DR   BRENDA; 3.2.1.119; 6644.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IDA:UniProtKB.
DR   GO; GO:0050392; F:vicianin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IDA:UniProtKB.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Signal.
FT   SIGNAL          <1..19
FT                   /evidence="ECO:0000269|PubMed:17548373"
FT   CHAIN           20..509
FT                   /note="Vicianin hydrolase"
FT                   /evidence="ECO:0000269|PubMed:17548373"
FT                   /id="PRO_0000398809"
FT   ACT_SITE        204
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P26205"
FT   ACT_SITE        416
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P26205,
FT                   ECO:0000255|PROSITE-ProRule:PRU10055"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         465
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         472..473
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        424
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        223..230
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:ABD03937.1"
SQ   SEQUENCE   509 AA;  57620 MW;  A51A79F959F4B7C5 CRC64;
     ISPSLLYLFS LATLLAVVTG TGTPSQEVHP SHYATTFNKS LFPKDFLFGI GSSAYQVEGA
     SNIDGRGPSI WDTFTKQHPE KIWDHSSGNI GADFYHRYKS DIKIVKEIGL DSYRFSISWS
     RIFPKGKGEV NPLGVKFYNN VINEILANGL IPFVTLFHWD LPQSLEDEYK GFLSSKVVKD
     FENYADFVFK TYGDRVKHWV TLNEPFSYAL YGYNGGTFAP GRCSKYAGNC EYGDSSTEPY
     IVAHNLILSH AAAAKLYKTK YQAHQKGNIG ATLVTHYFEP HSNSAADRVA ASRALDFFFG
     WFAHPLTYGH YPQSMISSLG NRLPKFSKEE VELTKGSYDF LGVNYYSTYY AQSAPLTTVN
     RTFYTDIQAN VSPLKNGAPI GPATDLNWLY VYPKGIHSLV THMKDVYKNP IVYITENGVA
     QSRNDSIPIS EARKDGIRIS YHDNHLKFLL QGIKDGANVK GYYAWSFSDS YEWDAGYTLR
     FGIIYVDFKD NLRRYPKYSA LWLQKFLLK