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 03-AUG-2022, entry version 100.
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; 4530.OS04T0513900-01; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q7XSK0; -.
DR PRIDE; 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; 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 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
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 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 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
