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BGL38_ORYSJ
ID   BGL38_ORYSJ             Reviewed;         492 AA.
AC   Q2QSR8; A0A0P0Y9W2;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Beta-glucosidase 38;
DE            Short=Os12bglu38;
DE            EC=3.2.1.21;
DE   Flags: Precursor;
GN   Name=BGLU38; OrderedLocusNames=Os12g0420100, LOC_Os12g23170;
GN   ORFNames=OsJ_35886;
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=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
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].
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   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).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; DP000011; ABA97621.2; -; Genomic_DNA.
DR   EMBL; AP008218; BAF29675.1; -; Genomic_DNA.
DR   EMBL; AP014968; BAT16894.1; -; Genomic_DNA.
DR   EMBL; CM000149; EEE53109.1; -; Genomic_DNA.
DR   EMBL; AK071058; BAG92285.1; -; mRNA.
DR   RefSeq; XP_015620634.1; XM_015765148.1.
DR   AlphaFoldDB; Q2QSR8; -.
DR   SMR; Q2QSR8; -.
DR   STRING; 4530.OS12T0420100-01; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   PaxDb; Q2QSR8; -.
DR   PRIDE; Q2QSR8; -.
DR   EnsemblPlants; Os12t0420100-01; Os12t0420100-01; Os12g0420100.
DR   GeneID; 4352082; -.
DR   Gramene; Os12t0420100-01; Os12t0420100-01; Os12g0420100.
DR   KEGG; osa:4352082; -.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; Q2QSR8; -.
DR   OMA; YIAINHY; -.
DR   OrthoDB; 408001at2759; -.
DR   Proteomes; UP000000763; Chromosome 12.
DR   Proteomes; UP000007752; Chromosome 12.
DR   Proteomes; UP000059680; Chromosome 12.
DR   Genevisible; Q2QSR8; OS.
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; IBA:GO_Central.
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; 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.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..492
FT                   /note="Beta-glucosidase 38"
FT                   /id="PRO_0000390353"
FT   ACT_SITE        192
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        400
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         447
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         454..455
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        211..214
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   492 AA;  57004 MW;  FD4359BFBD5FDF43 CRC64;
     MNMPLLLLIA IVVVSLSHGN GEQTDLTRET FPAGFVFGTA SSAYQVEGNA LQYGRGPCIW
     DTFLMQPGVT PDNSTANVTV DEYHRYMDDV DNMVRVGFDA YRFSISWSRI FPSGLGKINK
     DGVDYYHRLI DYMLANNIIP YVVLYHYDLP QVLHDQYKGW LHPRIVRDFV RFADFCFKTY
     GHKVKNWFTI NEPRMMANHG YGDGFFPPGR CTGCQPGGNS ATEPYIAAHN LLLSHAAAVR
     TYRDKYQAIQ KGKIGILLDF VWYEPLTDKE EDHAAAHRAR EFTLGWYLHP ITYGHYPETM
     QNAVKERLPN FTREQSEMIK GSADYIAINH YTTYYVSHHV NKTSISYLND WDVKISYERN
     GVPIGKQAYS NWLYVVPWGI YKAVMHVKEK YKDPIIIIGE NGIDQPGNET LPGALYDFFR
     IQYFDQYLHE LKRAIKDGAR VTGYFAWSLL DNFEWRLGFT SKFGIVYVDR STFTRYPKDS
     TRWFRKMIKS EV
 
 
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