ID   BGL16_ORYSJ             Reviewed;         516 AA.
AC   Q7XSK2; A0A0P0WC95; A0A0P0WCR8; Q0JBS0;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   24-JAN-2024, entry version 107.
DE   RecName: Full=Beta-glucosidase 16 {ECO:0000303|PubMed:17196101};
DE            Short=Os4bglu16 {ECO:0000303|PubMed:17196101};
DE            EC=3.2.1.21 {ECO:0000269|PubMed:25219312};
DE   Flags: Precursor;
GN   Name=BGLU16 {ECO:0000303|PubMed:17196101};
GN   OrderedLocusNames=Os04g0513400 {ECO:0000312|EMBL:BAF15217.1},
GN   LOC_Os04g43390 {ECO:0000305};
GN   ORFNames=OSJNBa0004N05.24 {ECO:0000312|EMBL:CAE54544.1},
GN   OSJNBb0070J16.1 {ECO:0000312|EMBL:CAE01908.2};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17196101; DOI=10.1186/1471-2229-6-33;
RA   Opassiri R., Pomthong B., Onkoksoong T., Akiyama T., Esen A.,
RA   Ketudat Cairns J.R.;
RT   "Analysis of rice glycosyl hydrolase family 1 and expression of Os4bglu12
RT   beta-glucosidase.";
RL   BMC Plant Biol. 6:33-33(2006).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=25219312; DOI=10.1016/j.plantsci.2014.07.009;
RA   Baiya S., Hua Y., Ekkhara W., Ketudat Cairns J.R.;
RT   "Expression and enzymatic properties of rice (Oryza sativa L.) monolignol
RT   beta-glucosidases.";
RL   Plant Sci. 227:101-109(2014).
CC   -!- FUNCTION: Hydrolyzes glycosides and monolignol glucosides
CC       (PubMed:25219312). Can hydrolyze para-nitrophenyl beta-D-
CC       glucopyranoside (pNPGlc) in vitro (PubMed:25219312). Hydrolyzes para-
CC       nitrophenyl beta-D-fucopyranoside, para-nitrophenyl beta-D-
CC       galactopyranoside and para-nitrophenyl beta-D-xylopyranoside in vitro
CC       (PubMed:25219312). Hydrolyzes the monolignol glucosides coniferin and
CC       syringin with high catalytic efficiencies (PubMed:25219312).
CC       {ECO:0000269|PubMed:25219312}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000269|PubMed:25219312};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.88 mM for para-nitrophenyl beta-D-glucopyranoside
CC         {ECO:0000269|PubMed:25219312};
CC         KM=7.72 mM for para-nitrophenyl beta-D-fucopyranoside
CC         {ECO:0000269|PubMed:25219312};
CC         KM=2.99 mM for para-nitrophenyl beta-D-xylopyranoside
CC         {ECO:0000269|PubMed:25219312};
CC         KM=19.9 mM for coniferin {ECO:0000269|PubMed:25219312};
CC         KM=4.66 mM for syringin {ECO:0000269|PubMed:25219312};
CC         Note=kcat is 3.05 sec(-1) with para-nitrophenyl
CC         beta-D-glucopyranoside as substrate. kcat is 6.92 sec(-1) with
CC         para-nitrophenyl beta-D-fucopyranoside as substrate. kcat is 0.788
CC         sec(-1) with para-nitrophenyl beta-D-xylopyranoside as substrate.
CC         kcat is 429 sec(-1) with coniferin as substrate. kcat is 106.3
CC         sec(-1) with syringin as substrate. {ECO:0000269|PubMed:25219312};
CC       pH dependence:
CC         Optimum pH is 6.5 with para-nitrophenyl beta-D-glucopyranoside
CC         (pNPGlc) as substrate. {ECO:0000269|PubMed:25219312};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius with para-nitrophenyl
CC         beta-D-glucopyranoside (pNPGlc) as substrate.
CC         {ECO:0000269|PubMed:25219312};
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, stems and endosperm.
CC       {ECO:0000269|PubMed:25219312}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF15217.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAS90059.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAS90060.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL606622; CAE54544.1; -; Genomic_DNA.
DR   EMBL; AL606659; CAE01908.2; -; Genomic_DNA.
DR   EMBL; AP008210; BAF15217.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014960; BAS90059.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014960; BAS90060.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_015636696.1; XM_015781210.1.
DR   AlphaFoldDB; Q7XSK2; -.
DR   SMR; Q7XSK2; -.
DR   STRING; 39947.Q7XSK2; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q7XSK2; 4 sites, No reported glycans.
DR   PaxDb; 39947-Q7XSK2; -.
DR   GeneID; 4336389; -.
DR   KEGG; osa:4336389; -.
DR   eggNOG; KOG0626; Eukaryota.
DR   InParanoid; Q7XSK2; -.
DR   OrthoDB; 3373839at2759; -.
DR   BRENDA; 3.2.1.126; 8948.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   GO; GO:0033907; F:beta-D-fucosidase activity; IDA:UniProtKB.
DR   GO; GO:0004565; F:beta-galactosidase activity; IDA:UniProtKB.
DR   GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0047782; F:coniferin beta-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0033491; P:coniferin metabolic process; IDA:UniProtKB.
DR   GO; GO:0016137; P:glycoside metabolic process; IDA:UniProtKB.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF159; BETA-GLUCOSIDASE 16; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..516
FT                   /note="Beta-glucosidase 16"
FT                   /id="PRO_0000390333"
FT   ACT_SITE        196
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   ACT_SITE        410
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         47
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         150
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         195..196
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         339
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         410
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         457
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         464..465
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         473
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        215..222
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   DISULFID        347..352
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
SQ   SEQUENCE   516 AA;  58556 MW;  8F828ECAEDF55FC0 CRC64;
     MAVAAATRIA VVVVVLALAV LAPAARGLRR DDFPPGFLFG AATSAYQIEG AYLDDNKGLN
     NWDVFTHTQA GRISDGRNGD VADDHYHRYT EDVDILHNLG VNSYRFSISW ARILPRGRLG
     GVNSAGIAFY NRLINALLQK GIQPFVTLNH FDIPHELETR YGGWLGAAIR EEFEYYSDVC
     FNAFGDRVRF WTTFNEPNLS TRHQYILGEF PPNHCSPPFG NCSSGDSRRE PYAAAHNILL
     SHAAAVHNYK TNYQAKQGGS IGIVIAVKWY EPLTNSTEDV RAARRALAFE VDWFLDPIFF
     GDYPREMREI LSSNLPKFTP EEKKLLQNNK VDFIGINHYT AIYAKDCIYS PCTLDTYEGN
     ALVYAIGRRN GKIIGKPTAL HGYFVVPEAM EKVVMYVNDR YRNTTIYITE NGYSQHSDTS
     MEDLINDVER VNYMHDYLKY LSSAIRKGAN VGGYFAWSIV DNFEWVYGYT VKFGLYQVDF
     DTQERIPRMS AKWYRDFLTS SSLTDGLQVR SRRADS
//