ID   FURH_VIBFR              Reviewed;         538 AA.
AC   Q75W17;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Furcatin hydrolase {ECO:0000303|PubMed:14976214, ECO:0000312|EMBL:BAD14925.1};
DE            Short=FH {ECO:0000303|PubMed:14976214};
DE            EC=3.2.1.161;
DE   Flags: Precursor;
OS   Viburnum furcatum (Scarlet leaved viburnum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Dipsacales; Adoxaceae; Viburnum.
OX   NCBI_TaxID=237940;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAD14925.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Leaf {ECO:0000269|PubMed:14976214};
RX   PubMed=14976214; DOI=10.1074/jbc.m311379200;
RA   Ahn Y.O., Mizutani M., Saino H., Sakata K.;
RT   "Furcatin hydrolase from Viburnum furcatum Blume is a novel disaccharide-
RT   specific acuminosidase in glycosyl hydrolase family 1.";
RL   J. Biol. Chem. 279:23405-23414(2004).
CC   -!- FUNCTION: Disaccharide-specific acuminosidase, hydrolyzes the beta-
CC       glycosidic bond between p-allylphenol and acuminose with retention of
CC       anomeric configuration. Has highest activity towards furcatin, and
CC       lower activity towards beta-primeverosides and beta-vicianoside. Has
CC       very low activity towards beta-gentobiosides.
CC       {ECO:0000269|PubMed:14976214}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-[beta-D-apiofuranosyl-(1->6)-beta-D-
CC         glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid +
CC         beta-D-apiofuranosyl-(1->6)-D-glucose.; EC=3.2.1.161;
CC         Evidence={ECO:0000269|PubMed:14976214};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.2 mM for furcatin {ECO:0000269|PubMed:14976214};
CC         KM=5.1 mM for pNP beta-primeveroside {ECO:0000269|PubMed:14976214};
CC       pH dependence:
CC         Optimum pH is 5.0. Active between pH 4.0 and 10.0.
CC         {ECO:0000269|PubMed:14976214};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Stable below 50 degrees
CC         Celsius. {ECO:0000269|PubMed:14976214};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:14976214}.
CC   -!- TISSUE SPECIFICITY: Expressed in young and mature leaves, but not in
CC       fruit and stem. {ECO:0000269|PubMed:14976214}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000255}.
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DR   EMBL; AB122081; BAD14925.1; -; mRNA.
DR   AlphaFoldDB; Q75W17; -.
DR   SMR; Q75W17; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; ag:BAD14925; -.
DR   BioCyc; MetaCyc:MON-17662; -.
DR   BRENDA; 3.2.1.161; 8017.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0033956; F:beta-apiosyl-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR001360; Glyco_hydro_1.
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; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Disulfide bond; Glycosidase; Hydrolase; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..66
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           67..538
FT                   /note="Furcatin hydrolase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000398616"
FT   REGION          18..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        238
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   ACT_SITE        447
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         494
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         501..502
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   DISULFID        257..260
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
SQ   SEQUENCE   538 AA;  60626 MW;  2C91837555097E20 CRC64;
     MATITTLASS VPLFRPYSFP GGSSRKPKKD NLSIKPPATS SLKVNAKLAS ADDTSSNFNK
     DNWLASADEL SRSFPPGFLF GGGSASYQYE GAVKEGGRTP SIWDTFAHEF PDKIADGSNG
     DVAVDFYHRY KDDVKLMKKI GVNGFRFSIS WTRILPSGKL CGGVNKEGVA FYNSLINELL
     ANGIEPFVTI FHWDLPQGLE NEYDGFLSGQ IVNDYRDYAE VCFQEFGDRV KFWTTLNEPW
     TFCYNGYVNG SFAPGRCSTC TAGNSGTEPY LVAHNLLLSH AAVAQLYKNK YQASQKGQIG
     IVLVCFWMVP YSDCPYDCEA AQRALDFMLG WFLHPLTYGD YPESMRHLVG ERLPQFTEMQ
     AMMMKGSIDF LGLNYYTSIY AANNESPNPH DISYTTDSRV NLFQKRDGIL IGPATGTPAF
     CFCPEGIRDL LVYTKEKYNN PIIYITECGL AEANINTVDQ GVKDVERVEF YYEHLKFLRS
     AIKKGVNVKG FFTWSLLDDW EWNSGFNVRF GIVYIDHEDG LKRYLKYSAL WFKKLFGK