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Database: UniProt/SWISS-PROT
Entry: BGL18_ORYSJ
LinkDB: BGL18_ORYSJ
Original site: BGL18_ORYSJ 
ID   BGL18_ORYSJ             Reviewed;         505 AA.
AC   Q7XSK0; A0A0P0WCH1; Q0JBR8;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=Beta-glucosidase 18 {ECO:0000303|PubMed:17196101};
DE            Short=Os4bglu18 {ECO:0000303|PubMed:17196101};
DE            EC=3.2.1.21 {ECO:0000269|PubMed:23811195, ECO:0000269|PubMed:25219312};
DE   Flags: Precursor;
GN   Name=BGLU18 {ECO:0000303|PubMed:17196101};
GN   OrderedLocusNames=Os04g0513900 {ECO:0000312|EMBL:BAS90064.1},
GN   LOC_Os04g43410 {ECO:0000305};
GN   ORFNames=OSJNBa0004N05.26 {ECO:0000312|EMBL:CAE54546.1},
GN   OSJNBb0070J16.3 {ECO:0000312|EMBL:CAE01910.2};
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, AND CATALYTIC ACTIVITY.
RX   PubMed=23811195; DOI=10.1016/j.abb.2013.06.005;
RA   Hua Y., Sansenya S., Saetang C., Wakuta S., Ketudat Cairns J.R.;
RT   "Enzymatic and structural characterization of hydrolysis of gibberellin A4
RT   glucosyl ester by a rice beta-D-glucosidase.";
RL   Arch. Biochem. Biophys. 537:39-48(2013).
RN   [7]
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).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 26-505 IN COMPLEX WITH A
RP   BETA-D-GLUCOSIDE, ACTIVE SITE, AND DISULFIDE BONDS.
RX   PubMed=33471829; DOI=10.1371/journal.pone.0241325;
RA   Baiya S., Pengthaisong S., Kitjaruwankul S., Ketudat Cairns J.R.;
RT   "Structural analysis of rice Os4BGlu18 monolignol beta-glucosidase.";
RL   PLoS ONE 16:E0241325-E0241325(2021).
CC   -!- FUNCTION: Hydrolyzes glycosides and monolignol glucosides
CC       (PubMed:25219312). Can hydrolyze para-nitrophenyl beta-D-
CC       glucopyranoside (pNPGlc) in vitro (PubMed:23811195, PubMed:25219312).
CC       Hydrolyzes para-nitrophenyl beta-D-fucopyranoside, para-nitrophenyl
CC       beta-D-galactopyranoside and para-nitrophenyl beta-D-xylopyranoside in
CC       vitro (PubMed:25219312). Hydrolyzes the monolignol glucosides coniferin
CC       and syringin with high catalytic efficiencies (PubMed:25219312).
CC       {ECO:0000269|PubMed:23811195, 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:23811195, ECO:0000269|PubMed:25219312};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.84 mM for para-nitrophenyl beta-D-glucopyranoside
CC         {ECO:0000269|PubMed:25219312};
CC         KM=5.86 mM for para-nitrophenyl beta-D-fucopyranoside
CC         {ECO:0000269|PubMed:25219312};
CC         KM=1.26 mM for para-nitrophenyl beta-D-xylopyranoside
CC         {ECO:0000269|PubMed:25219312};
CC         KM=8.02 mM for coniferin {ECO:0000269|PubMed:25219312};
CC         KM=5.34 mM for syringin {ECO:0000269|PubMed:25219312};
CC         Note=kcat is 3.82 sec(-1) with para-nitrophenyl beta-D-
CC         glucopyranoside as substrate. kcat is 23.8 sec(-1) with para-
CC         nitrophenyl beta-D-fucopyranoside as substrate. kcat is 0.381 sec(-1)
CC         with para-nitrophenyl beta-D-xylopyranoside as substrate. kcat is
CC         255.8 sec(-1) with coniferin as substrate. kcat is 127.9 sec(-1) with
CC         syringin as substrate. {ECO:0000269|PubMed:25219312};
CC       pH dependence:
CC         Optimum pH is 5.0 with para-nitrophenyl beta-D-glucopyranoside
CC         (pNPGlc) as substrate. {ECO:0000269|PubMed:25219312};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius with para-nitrophenyl beta-
CC         D-glucopyranoside (pNPGlc) as substrate.
CC         {ECO:0000269|PubMed:25219312};
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and pollen.
CC       {ECO:0000269|PubMed:25219312}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF15219.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAS90064.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL606622; CAE54546.1; -; Genomic_DNA.
DR   EMBL; AL606659; CAE01910.2; -; Genomic_DNA.
DR   EMBL; AP008210; BAF15219.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014960; BAS90064.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_015636697.1; XM_015781211.1.
DR   PDB; 7D6A; X-ray; 1.70 A; A/B=26-505.
DR   PDB; 7D6B; X-ray; 2.10 A; A/B=26-505.
DR   PDBsum; 7D6A; -.
DR   PDBsum; 7D6B; -.
DR   AlphaFoldDB; Q7XSK0; -.
DR   SMR; Q7XSK0; -.
DR   STRING; 39947.Q7XSK0; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q7XSK0; 1 site, No reported glycans.
DR   PaxDb; 39947-Q7XSK0; -.
DR   EnsemblPlants; Os04t0513900-01; Os04t0513900-01; Os04g0513900.
DR   GeneID; 4336391; -.
DR   Gramene; Os04t0513900-01; Os04t0513900-01; Os04g0513900.
DR   KEGG; osa:4336391; -.
DR   eggNOG; KOG0626; Eukaryota.
DR   InParanoid; Q7XSK0; -.
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:SF236; BETA-GLUCOSIDASE 18; 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   3D-structure; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..505
FT                   /note="Beta-glucosidase 18"
FT                   /id="PRO_0000390335"
FT   ACT_SITE        194
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000269|PubMed:33471829,
FT                   ECO:0007744|PDB:7D6B"
FT   ACT_SITE        408
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:33471829,
FT                   ECO:0007744|PDB:7D6B"
FT   BINDING         46
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000269|PubMed:33471829,
FT                   ECO:0007744|PDB:7D6B"
FT   BINDING         148
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000269|PubMed:33471829,
FT                   ECO:0007744|PDB:7D6B"
FT   BINDING         193..194
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000269|PubMed:33471829,
FT                   ECO:0007744|PDB:7D6B"
FT   BINDING         337
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000269|PubMed:33471829,
FT                   ECO:0007744|PDB:7D6B"
FT   BINDING         408
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:0000269|PubMed:33471829,
FT                   ECO:0007744|PDB:7D6B"
FT   BINDING         464..465
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000269|PubMed:33471829,
FT                   ECO:0007744|PDB:7D6B"
FT   BINDING         473
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        213..220
FT                   /evidence="ECO:0000269|PubMed:33471829,
FT                   ECO:0007744|PDB:7D6B"
FT   DISULFID        345..350
FT                   /evidence="ECO:0000269|PubMed:33471829,
FT                   ECO:0007744|PDB:7D6B"
FT   HELIX           29..31
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           44..47
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           60..65
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          77..79
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           83..97
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           108..111
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           122..137
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          141..149
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           153..159
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           166..182
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   TURN            183..185
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          188..193
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           195..203
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   TURN            226..228
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           229..251
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           253..256
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          259..265
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          268..275
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           276..287
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           290..299
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           304..310
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           311..313
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           319..325
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          330..335
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          339..344
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          346..348
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          352..354
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   TURN            355..360
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          361..367
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          370..375
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           386..399
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          404..409
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           421..425
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           428..446
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          451..457
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           465..470
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          475..479
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   TURN            480..483
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   STRAND          484..487
FT                   /evidence="ECO:0007829|PDB:7D6A"
FT   HELIX           489..499
FT                   /evidence="ECO:0007829|PDB:7D6A"
SQ   SEQUENCE   505 AA;  57602 MW;  C60EAA99754C2512 CRC64;
     MAGGSKTRIH ASLVSTLLLL LPLASAIHRS DFPASFLFGT ATSSYQIEGA YLEGNKSLSN
     WDVFTHLPGN IKDGSNGDIA DDHYHRYEED VELMNSLGVN AYRFSISWSR ILPKGRFGGV
     NPAGIDFYNK LIDSILLKGI QPFVTLTHYD IPQELEDRYG AWLNAEIQSD FGHFADVCFG
     AFGDRVKYWT TFNEPNVAVR HGYMLGTYPP SRCSPPFGHC ARGGDSHAEP YVAAHNVILS
     HATAIEIYKR KYQSKQRGMI GMVLYSTWYE PLRDVPEDRL ATERALAFET PWFLDPLVYG
     DYPPEMRQIL GGRLPSFSPE DRRKLRYKLD FIGVNHYTTL YARDCMFSDC PQGQETQHAL
     AAVTGESNGL PIGTPTAMPT FYVVPDGIEK MVKYFMRRYN NLPMFITENG YAQGGDSYTD
     AEDWIDDEDR IEYLEGYLTK LAKVIRDGAD VRGYFAWSVV DNFEWLFGYT LRFGLYYIDY
     RTQERSPKLS ALWYKEFLQN LHENQ
//
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