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Database: UniProt
Entry: A3BMZ5
LinkDB: A3BMZ5
Original site: A3BMZ5 
ID   BGL26_ORYSJ             Reviewed;         510 AA.
AC   A3BMZ5; Q0D407;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   16-APR-2014, entry version 43.
DE   RecName: Full=Beta-glucosidase 26;
DE            Short=Os7bglu26;
DE            EC=3.2.1.21;
DE   Flags: Precursor;
GN   Name=BGLU26; OrderedLocusNames=Os07g0656200, LOC_Os07g46280;
GN   ORFNames=OsJ_25416;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
OX   NCBI_TaxID=39947;
RN   [1]
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   [2]
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   [3]
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.,
RA   Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
RA   Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
RA   Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
RA   Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
RA   Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
RA   Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
RA   Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
RA   Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
RA   Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
RA   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   [4]
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
RT   Os4bglu12 beta-glucosidase.";
RL   BMC Plant Biol. 6:33-33(2006).
RN   [5]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19766588; DOI=10.1016/j.abb.2009.09.004;
RA   Kuntothom T., Luang S., Harvey A.J., Fincher G.B., Opassiri R.,
RA   Hrmova M., Ketudat Cairns J.R.;
RT   "Rice family GH1 glycoside hydrolases with beta-D-glucosidase and
RT   beta-D-mannosidase activities.";
RL   Arch. Biochem. Biophys. 491:85-95(2009).
CC   -!- FUNCTION: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl
CC       beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl
CC       beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl
CC       beta-L-arabinoside, cello-oligosaccharides, laminari-
CC       oligosaccharides and sophorose.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D-
CC       glucosyl residues with release of beta-D-glucose.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.27 mM for p-nitrophenyl beta-D-glucoside (at pH 5.0);
CC         KM=0.52 mM for p-nitrophenyl beta-D-mannoside (at pH 5.0);
CC         KM=19.6 mM for cellobiose (at pH 5.0);
CC         KM=0.52 mM for cellotriose (at pH 5.0);
CC         KM=0.09 mM for cellotetraose (at pH 5.0);
CC         KM=0.06 mM for cellopentaose (at pH 5.0);
CC         KM=0.05 mM for cellohexaose (at pH 5.0);
CC         KM=0.86 mM for laminaribiose (at pH 5.0);
CC         KM=8.7 mM for laminaritriose (at pH 5.0);
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF22416.1; Type=Erroneous gene model prediction;
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DR   EMBL; AP008213; BAF22416.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM000144; EAZ40934.1; -; Genomic_DNA.
DR   RefSeq; NP_001060502.1; NM_001067037.1.
DR   UniGene; Os.20617; -.
DR   ProteinModelPortal; A3BMZ5; -.
DR   PRIDE; A3BMZ5; -.
DR   GeneID; 4344146; -.
DR   KEGG; osa:4344146; -.
DR   Gramene; A3BMZ5; -.
DR   eggNOG; COG2723; -.
DR   SABIO-RK; A3BMZ5; -.
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:0047701; F:beta-L-arabinosidase activity; IDA:UniProtKB.
DR   GO; GO:0004567; F:beta-mannosidase activity; IDA:UniProtKB.
DR   GO; GO:0080079; F:cellobiose glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; -; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR013781; Glyco_hydro_catalytic_dom.
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   1: Evidence at protein level;
KW   Complete proteome; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Reference proteome; Signal.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28    510       Beta-glucosidase 26.
FT                                /FTId=PRO_0000390343.
FT   REGION      470    471       Substrate binding (By similarity).
FT   ACT_SITE    206    206       Proton donor (By similarity).
FT   ACT_SITE    416    416       Nucleophile (By similarity).
FT   BINDING      59     59       Substrate (By similarity).
FT   BINDING     160    160       Substrate (By similarity).
FT   BINDING     205    205       Substrate (By similarity).
FT   BINDING     345    345       Substrate (By similarity).
FT   BINDING     463    463       Substrate (By similarity).
FT   CARBOHYD     87     87       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    127    127       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    233    233       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    424    424       N-linked (GlcNAc...) (Potential).
FT   DISULFID    225    228       By similarity.
SQ   SEQUENCE   510 AA;  58498 MW;  9EBEAE24EE62833E CRC64;
     MRKFIAALRL ALAAAAHLLL TLPPAQCYWL NPEIYDAGGL SRRAFPEGFV FGTAASAYQV
     EGMAKQGGRG PSIWDAFIEK PGTIPNNATA DVTVDEYHRY KEDVNIMKNM GFDAYRFSIS
     WSRIFPNGTG MVNQEGVDYY NRLIDYMVKK GIKPYANLYH YDLPLALHEQ YLGWLSPNIV
     EAFADYADFC FQTFGDRVKD WFTFNEPRCV AALGYDNGFH APGRCSGCDA GGNSTTEPYL
     AAHHLILSHA AAVKRYREKY QLYQKGRIGI LLDFVWYEPF SDSNADRAAA QRARDFHLGW
     FLDPIIHGRY PYSMLEIVKD RMPTFSDEES RMVKDSIDYV GINHYTSFYM KDPGPWNLTP
     TSYQDDWHVG FAYERNGVPI GAQANSYWLY IVPWGINKAV TYVKETYGNP TMILSENGMD
     QPGNVSITQG VHDTVRIRYY RNYITELKKA IDDGAKVIGY FAWSLLDNFE WRLGYTSRFG
     IVYVDYKTLK RYPKDSAFWF KNMLSSKKRN
//
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