BGL12_ORYSI
ID BGL12_ORYSI Reviewed; 510 AA.
AC B8AVF0; Q01KB2;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Beta-glucosidase 12 {ECO:0000305};
DE EC=3.2.1.21 {ECO:0000305};
DE Flags: Precursor;
GN Name=BGLU12 {ECO:0000305};
GN ORFNames=OsI_16288 {ECO:0000312|EMBL:EEC77466.1},
GN OSIGBa0135C13.7 {ECO:0000312|EMBL:CAH66812.1};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Guang-Lu-Ai No.4;
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. 93-11;
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).
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:0000250|UniProtKB:Q7XKV4}.
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; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {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; CR855145; CAH66812.1; -; Genomic_DNA.
DR EMBL; CM000129; EEC77466.1; -; Genomic_DNA.
DR AlphaFoldDB; B8AVF0; -.
DR SMR; B8AVF0; -.
DR STRING; 39946.B8AVF0; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR EnsemblPlants; BGIOSGA014893-TA; BGIOSGA014893-PA; BGIOSGA014893.
DR Gramene; BGIOSGA014893-TA; BGIOSGA014893-PA; BGIOSGA014893.
DR HOGENOM; CLU_001859_1_0_1; -.
DR OMA; EINAMDM; -.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033907; F:beta-D-fucosidase activity; IEA:UniProt.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProt.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW 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_0000434411"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q7XKV4"
FT ACT_SITE 417
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q7XKV4"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7XKV4"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7XKV4"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7XKV4"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7XKV4"
FT BINDING 466
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT BINDING 473..474
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7XKV4"
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:0000250|UniProtKB:Q7XKV4"
FT DISULFID 222..230
FT /evidence="ECO:0000250|UniProtKB:Q7XKV4"
SQ SEQUENCE 510 AA; 57493 MW; FD73408B5C3FE0AD CRC64;
MAAAGAMPGG LLLTFLLLAV VASGAYNSAG 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 FSRSKSNNDA AKRAIDFMFG
WFMDPLIRGD YPLSMRGLVG NRLPQFTKEQ SKLVKGAFDF IGLNYYTANY ADNLPPSNGL
NNSYTTDSRA NLTGVRNGIP IGPQAASPWL YVYPQGFRDL LLYVKENYGN PTVYITENGV
DEFNNKTLPL QEALKDDARI EYYHKHLLSL LSAIRDGANV KGYFAWSLLD NFEWSNGYTV
RFGINFVDYN DGRKRYPKNS AHWFKKFLLK
