BGL12_ORYSJ
ID BGL12_ORYSJ Reviewed; 510 AA.
AC Q7XKV4; B7EQY4; Q0JCF3;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Beta-glucosidase 12 {ECO:0000305};
DE Short=Os4bglu12 {ECO:0000303|PubMed:17196101};
DE EC=3.2.1.21 {ECO:0000269|PubMed:17196101};
DE Flags: Precursor;
GN Name=BGLU12 {ECO:0000305};
GN OrderedLocusNames=Os04g0474800 {ECO:0000312|EMBL:BAF14984.1},
GN LOC_Os04g39880 {ECO:0000305};
GN ORFNames=OsJ_15166 {ECO:0000312|EMBL:EEE61179.1},
GN OSJNBa0022H21.3 {ECO:0000312|EMBL:CAE05483.2};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, 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 [8]
RP MUTAGENESIS OF HIS-276.
RX PubMed=22341501; DOI=10.1016/j.carres.2012.01.010;
RA Sansenya S., Maneesan J., Cairns J.R.;
RT "Exchanging a single amino acid residue generates or weakens a +2
RT cellooligosaccharide binding subsite in rice beta-glucosidases.";
RL Carbohydr. Res. 351:130-133(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 25-510 IN COMPLEX WITH SUBSTRATE
RP ANALOG, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, AND DISULFIDE BONDS.
RX PubMed=21521631; DOI=10.1016/j.abb.2011.04.005;
RA Sansenya S., Opassiri R., Kuaprasert B., Chen C.J., Cairns J.R.;
RT "The crystal structure of rice (Oryza sativa L.) Os4BGlu12, an
RT oligosaccharide and tuberonic acid glucoside-hydrolyzing beta-glucosidase
RT with significant thioglucohydrolase activity.";
RL Arch. Biochem. Biophys. 510:62-72(2011).
CC -!- FUNCTION: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl
CC beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-
CC D-fucoside, p-nitrophenyl beta-L-arabinoside, cello-oligosaccharides
CC and laminaribiose. {ECO:0000269|PubMed:17196101}.
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:17196101};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.56 mM for p-nitrophenyl beta-D-glucopyranoside
CC {ECO:0000269|PubMed:21521631};
CC KM=1.64 mM for p-nitrophenyl beta-D-thioglucoside
CC {ECO:0000269|PubMed:21521631};
CC KM=0.91 mM for n-heptyl-beta-D-glucoside
CC {ECO:0000269|PubMed:21521631};
CC KM=0.44 mM for n-octyl-beta-D-glucoside
CC {ECO:0000269|PubMed:21521631};
CC KM=1.61 mM for n-octyl-beta-D-thioglucopyranoside
CC {ECO:0000269|PubMed:21521631};
CC Vmax=20.1 umol/min/mg enzyme with p-nitrophenyl beta-D-
CC glucopyranoside as substrate {ECO:0000269|PubMed:21521631};
CC Vmax=0.29 umol/min/mg enzyme with p-nitrophenyl beta-D-thioglucoside
CC as substrate {ECO:0000269|PubMed:21521631};
CC Vmax=13.2 umol/min/mg enzyme with n-heptyl-beta-D-glucoside as
CC substrate {ECO:0000269|PubMed:21521631};
CC Vmax=10.7 umol/min/mg enzyme with n-octyl-beta-D-glucoside as
CC substrate {ECO:0000269|PubMed:21521631};
CC Vmax=4 umol/min/mg enzyme with n-octyl-beta-D-thioglucopyranoside as
CC substrate {ECO:0000269|PubMed:21521631};
CC Note=kcat is 18.5 (sec-1) with p-nitrophenyl beta-D-glucopyranoside
CC as substrate. kcat is 0.27 (sec-1) with p-nitrophenyl beta-D-
CC thioglucoside as substrate. kcat is 12.1 (sec-1) with n-heptyl-beta-
CC D-glucoside as substrate. kcat is 9.8 (src-1) with n-octyl-beta-D-
CC glucoside as substrate. kcat is 0.038 (sec-1) n-octyl-beta-D-
CC thioglucopyranoside as substrate. {ECO:0000269|PubMed:21521631};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7XKV4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7XKV4-2; Sequence=VSP_038503, VSP_038504;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF14984.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL731582; CAE05483.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF14984.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; BAS89674.1; -; Genomic_DNA.
DR EMBL; CM000141; EEE61179.1; -; Genomic_DNA.
DR EMBL; AK100820; BAG94781.1; -; mRNA.
DR RefSeq; XP_015636597.1; XM_015781111.1. [Q7XKV4-1]
DR PDB; 3PTK; X-ray; 2.49 A; A/B=25-510.
DR PDB; 3PTM; X-ray; 2.40 A; A/B=25-510.
DR PDB; 3PTQ; X-ray; 2.45 A; A/B=25-510.
DR PDBsum; 3PTK; -.
DR PDBsum; 3PTM; -.
DR PDBsum; 3PTQ; -.
DR AlphaFoldDB; Q7XKV4; -.
DR SMR; Q7XKV4; -.
DR STRING; 4530.OS04T0474800-02; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q7XKV4; -.
DR PRIDE; Q7XKV4; -.
DR EnsemblPlants; Os04t0474800-02; Os04t0474800-02; Os04g0474800. [Q7XKV4-2]
DR GeneID; 4336145; -.
DR Gramene; Os04t0474800-02; Os04t0474800-02; Os04g0474800. [Q7XKV4-2]
DR KEGG; osa:4336145; -.
DR eggNOG; KOG0626; Eukaryota.
DR InParanoid; Q7XKV4; -.
DR OMA; EINAMDM; -.
DR OrthoDB; 408001at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033907; F:beta-D-fucosidase activity; IDA:UniProtKB.
DR GO; GO:0004565; F:beta-galactosidase activity; IDA:UniProtKB.
DR GO; GO:0080083; F:beta-gentiobiose beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0047701; F:beta-L-arabinosidase activity; IDA:UniProtKB.
DR GO; GO:0004338; F:glucan exo-1,3-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 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; Alternative splicing; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..510
FT /note="Beta-glucosidase 12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390329"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:21521631"
FT ACT_SITE 417
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:21521631"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21521631,
FT ECO:0007744|PDB:3PTQ"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21521631,
FT ECO:0007744|PDB:3PTQ"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21521631,
FT ECO:0007744|PDB:3PTM"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21521631,
FT ECO:0007744|PDB:3PTQ"
FT BINDING 466
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT BINDING 473..474
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21521631,
FT ECO:0007744|PDB:3PTQ"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 208..243
FT /evidence="ECO:0000269|PubMed:21521631,
FT ECO:0007744|PDB:3PTK, ECO:0007744|PDB:3PTM,
FT ECO:0007744|PDB:3PTQ"
FT DISULFID 222..230
FT /evidence="ECO:0000269|PubMed:21521631,
FT ECO:0007744|PDB:3PTK, ECO:0007744|PDB:3PTM,
FT ECO:0007744|PDB:3PTQ"
FT VAR_SEQ 1..119
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_038503"
FT VAR_SEQ 120..122
FT /note="LPN -> MAD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_038504"
FT MUTAGEN 276
FT /note="H->M: Decreases the kcat/Km values 2 to 6-fold
FT depending on the substrate."
FT /evidence="ECO:0000269|PubMed:21521631"
SQ SEQUENCE 510 AA; 57464 MW; 5828169EA16037DA CRC64;
MAAAGAMPGG LLLTFLLLAV VASGAYNGAG EPPVSRRSFP KGFIFGTASS SYQYEGGAAE
GGRGPSIWDT FTHQHPEKIA DRSNGDVASD SYHLYKEDVR LMKDMGMDAY RFSISWTRIL
PNGSLRGGVN KEGIKYYNNL INELLSKGVQ PFITLFHWDS PQALEDKYNG FLSPNIINDF
KDYAEICFKE FGDRVKNWIT FNEPWTFCSN GYATGLFAPG RCSPWEKGNC SVGDSGREPY
TACHHQLLAH AETVRLYKAK YQALQKGKIG ITLVSHWFVP FSRSKSNDDA AKRAIDFMFG
WFMDPLIRGD YPLSMRGLVG NRLPQFTKEQ SKLVKGAFDF IGLNYYTANY ADNLPPSNGL
NNSYTTDSRA NLTGVRNGIP IGPQAASPWL YVYPQGFRDL LLYVKENYGN PTVYITENGV
DEFNNKTLPL QEALKDDARI EYYHKHLLSL LSAIRDGANV KGYFAWSLLD NFEWSNGYTV
RFGINFVDYN DGRKRYPKNS AHWFKKFLLK
