BGL16_ORYSJ
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 03-AUG-2022, entry version 102.
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 beta-D-
CC glucopyranoside as substrate. kcat is 6.92 sec(-1) with para-
CC nitrophenyl beta-D-fucopyranoside as substrate. kcat is 0.788 sec(-1)
CC with para-nitrophenyl beta-D-xylopyranoside as substrate. kcat is 429
CC sec(-1) with coniferin as substrate. kcat is 106.3 sec(-1) with
CC 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 beta-
CC 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 4530.OS04T0513400-01; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q7XSK2; -.
DR PRIDE; Q7XSK2; -.
DR EnsemblPlants; Os04t0513400-01; Os04t0513400-01; Os04g0513400.
DR EnsemblPlants; Os04t0513400-02; Os04t0513400-02; Os04g0513400.
DR GeneID; 4336389; -.
DR Gramene; Os04t0513400-01; Os04t0513400-01; Os04g0513400.
DR Gramene; Os04t0513400-02; Os04t0513400-02; Os04g0513400.
DR KEGG; osa:4336389; -.
DR eggNOG; KOG0626; Eukaryota.
DR InParanoid; Q7XSK2; -.
DR OrthoDB; 408001at2759; -.
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 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 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
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 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 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
