ID   CBG_PINCO               Reviewed;         513 AA.
AC   Q9ZT64;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Coniferin beta-glucosidase;
DE            EC=3.2.1.126;
DE   Flags: Precursor;
OS   Pinus contorta (Shore pine) (Lodgepole pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RX   PubMed=10412914; DOI=10.1023/a:1006226931512;
RA   Dharmawardhana D.P., Ellis B.E., Carlson J.E.;
RT   "cDNA cloning and heterologous expression of coniferin beta-glucosidase.";
RL   Plant Mol. Biol. 40:365-372(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-40, SUBUNIT, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP   GLYCOSYLATION.
RX   PubMed=7724669; DOI=10.1104/pp.107.2.331;
RA   Dharmawardhana D.P., Ellis B.E., Carlson J.E.;
RT   "A beta-glucosidase from lodgepole pine xylem specific for the lignin
RT   precursor coniferin.";
RL   Plant Physiol. 107:331-339(1995).
CC   -!- FUNCTION: Involved in the release of monolignols for lignin
CC       biosynthesis. Unable to hydrolyze 4-nitrophenyl beta-cellobioside or
CC       alpha-linked methylumbelliferyl glucoside.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-O-(beta-D-glucosyl)-trans-coniferol + H2O = (E)-coniferol +
CC         D-glucose; Xref=Rhea:RHEA:12252, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16220, ChEBI:CHEBI:17745; EC=3.2.1.126;
CC         Evidence={ECO:0000269|PubMed:10412914, ECO:0000269|PubMed:7724669};
CC   -!- ACTIVITY REGULATION: Inhibited by glucono-1,5-lactone, but not by
CC       bromoconduritol or conduritol B epoxide. {ECO:0000269|PubMed:7724669}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.18 mM for coniferin {ECO:0000269|PubMed:7724669};
CC         KM=0.29 mM for syringin {ECO:0000269|PubMed:7724669};
CC         KM=2.3 mM for 4-methylumbelliferyl p-glucoside
CC         {ECO:0000269|PubMed:7724669};
CC         KM=1.9 mM for 4-nitrophenyl P-glucoside {ECO:0000269|PubMed:7724669};
CC       pH dependence:
CC         Optimum pH is 5.4-5.9. {ECO:0000269|PubMed:7724669};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7724669}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:7724669}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; AF072736; AAC69619.1; -; mRNA.
DR   AlphaFoldDB; Q9ZT64; -.
DR   SMR; Q9ZT64; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GO; GO:0047782; F:coniferin beta-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009809; P:lignin biosynthetic process; IDA:UniProtKB.
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   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Lignin biosynthesis; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:7724669"
FT   CHAIN           24..513
FT                   /note="Coniferin beta-glucosidase"
FT                   /id="PRO_0000418448"
FT   ACT_SITE        191
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        408
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         457
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         464..465
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        210..219
FT                   /evidence="ECO:0000250"
FT   CONFLICT        35
FT                   /note="M -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   513 AA;  58300 MW;  6FF2EB790266165C CRC64;
     MEVSVLMWVL LFYSLLGFQV TTARLDRNNF PSDFMFGTAS SAYQYEGAVR EDGKGPSTWD
     ALTHMPGRIK DSSNGDVAVD QYHRYMEDIE LMASLGLDAY RFSISWSRIL PEGRGEINMA
     GIEYYNNLID ALLQNGIQPF VTLFHFDLPK ALEDSYGGWL SPQIINDFEA YAEICFRAFG
     DRVKYWATVN EPNLFVPLGY TVGIFPPTRC AAPHANPLCM TGNCSSAEPY LAAHHVLLAH
     ASAVEKYREK YQKIQGGSIG LVISAPWYEP LENSPEERSA VDRILSFNLR WFLDPIVFGD
     YPQEMRERLG SRLPSISSEL SAKLRGSFDY MGINHYTTLY ATSTPPLSPD HTQYLYPDSR
     VYLTGERHGV SIGERTGMDG LFVVPHGIQK IVEYVKEFYD NPTIIIAENG YPESEESSST
     LQENLNDVRR IRFHGDCLSY LSAAIKNGSD VRGYFVWSLL DNFEWAFGYT IRFGLYHVDF
     ISDQKRYPKL SAQWFRQFLQ HDDQGSIRSS SSI