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Beta-glucosidase 12 (Os4bglu12) (EC 3.2.1.21)

 BGL12_ORYSJ             Reviewed;         510 AA.
Q7XKV4; B7EQY4; Q0JCF3;
15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
23-MAY-2018, entry version 91.
RecName: Full=Beta-glucosidase 12 {ECO:0000305};
Short=Os4bglu12 {ECO:0000303|PubMed:17196101};
EC=3.2.1.21 {ECO:0000269|PubMed:17196101};
Flags: Precursor;
Name=BGLU12 {ECO:0000305};
OrderedLocusNames=Os04g0474800 {ECO:0000312|EMBL:BAF14984.1},
LOC_Os04g39880 {ECO:0000305};
ORFNames=OsJ_15166 {ECO:0000312|EMBL:EEE61179.1},
OSJNBa0022H21.3 {ECO:0000312|EMBL:CAE05483.2};
Oryza sativa subsp. japonica (Rice).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
NCBI_TaxID=39947;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=12447439; DOI=10.1038/nature01183;
Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J.,
Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y.,
Weng Q., Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D.,
Liu X., Lu T., Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J.,
Wu M., Zhang R., Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H.,
Cai Z., Ren S., Lv G., Gu W., Zhu G., Tu Y., Jia J., Zhang Y.,
Chen J., Kang H., Chen X., Shao C., Sun Y., Hu Q., Zhang X., Zhang W.,
Wang L., Ding C., Sheng H., Gu J., Chen S., Ni L., Zhu F., Chen W.,
Lan L., Lai Y., Cheng Z., Gu M., Jiang J., Li J., Hong G., Xue Y.,
Han B.;
"Sequence and analysis of rice chromosome 4.";
Nature 420:316-320(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=16100779; DOI=10.1038/nature03895;
International rice genome sequencing project (IRGSP);
"The map-based sequence of the rice genome.";
Nature 436:793-800(2005).
[3]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=18089549; DOI=10.1093/nar/gkm978;
The rice annotation project (RAP);
"The rice annotation project database (RAP-DB): 2008 update.";
Nucleic Acids Res. 36:D1028-D1033(2008).
[4]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=24280374; DOI=10.1186/1939-8433-6-4;
Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H.,
McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
Buell C.R., Matsumoto T.;
"Improvement of the Oryza sativa Nipponbare reference genome using
next generation sequence and optical map data.";
Rice 6:4-4(2013).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H.,
Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
Samudrala R., Wang J., Wong G.K.-S., Yang H.;
"The genomes of Oryza sativa: a history of duplications.";
PLoS Biol. 3:266-281(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Nipponbare;
PubMed=12869764; DOI=10.1126/science.1081288;
The rice full-length cDNA consortium;
"Collection, mapping, and annotation of over 28,000 cDNA clones from
japonica rice.";
Science 301:376-379(2003).
[7]
FUNCTION, CATALYTIC ACTIVITY, GENE FAMILY, AND NOMENCLATURE.
PubMed=17196101; DOI=10.1186/1471-2229-6-33;
Opassiri R., Pomthong B., Onkoksoong T., Akiyama T., Esen A.,
Ketudat Cairns J.R.;
"Analysis of rice glycosyl hydrolase family 1 and expression of
Os4bglu12 beta-glucosidase.";
BMC Plant Biol. 6:33-33(2006).
[8]
MUTAGENESIS OF HIS-276.
PubMed=22341501; DOI=10.1016/j.carres.2012.01.010;
Sansenya S., Maneesan J., Cairns J.R.;
"Exchanging a single amino acid residue generates or weakens a +2
cellooligosaccharide binding subsite in rice beta-glucosidases.";
Carbohydr. Res. 351:130-133(2012).
[9]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 25-510 IN COMPLEX WITH
SUBSTRATE ANALOG, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, AND
DISULFIDE BONDS.
PubMed=21521631; DOI=10.1016/j.abb.2011.04.005;
Sansenya S., Opassiri R., Kuaprasert B., Chen C.J., Cairns J.R.;
"The crystal structure of rice (Oryza sativa L.) Os4BGlu12, an
oligosaccharide and tuberonic acid glucoside-hydrolyzing beta-
glucosidase with significant thioglucohydrolase activity.";
Arch. Biochem. Biophys. 510:62-72(2011).
-!- FUNCTION: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl
beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl
beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, cello-
oligosaccharides and laminaribiose. {ECO:0000269|PubMed:17196101}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D-
glucosyl residues with release of beta-D-glucose.
{ECO:0000269|PubMed:17196101}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.56 mM for p-nitrophenyl beta-D-glucopyranoside
{ECO:0000269|PubMed:21521631};
KM=1.64 mM for p-nitrophenyl beta-D-thioglucoside
{ECO:0000269|PubMed:21521631};
KM=0.91 mM for n-heptyl-beta-D-glucoside
{ECO:0000269|PubMed:21521631};
KM=0.44 mM for n-octyl-beta-D-glucoside
{ECO:0000269|PubMed:21521631};
KM=1.61 mM for n-octyl-beta-D-thioglucopyranoside
{ECO:0000269|PubMed:21521631};
Vmax=20.1 umol/min/mg enzyme with p-nitrophenyl beta-D-
glucopyranoside as substrate {ECO:0000269|PubMed:21521631};
Vmax=0.29 umol/min/mg enzyme with p-nitrophenyl beta-D-
thioglucoside as substrate {ECO:0000269|PubMed:21521631};
Vmax=13.2 umol/min/mg enzyme with n-heptyl-beta-D-glucoside as
substrate {ECO:0000269|PubMed:21521631};
Vmax=10.7 umol/min/mg enzyme with n-octyl-beta-D-glucoside as
substrate {ECO:0000269|PubMed:21521631};
Vmax=4 umol/min/mg enzyme with n-octyl-beta-D-
thioglucopyranoside as substrate {ECO:0000269|PubMed:21521631};
Note=kcat is 18.5 (sec-1) with p-nitrophenyl beta-D-
glucopyranoside as substrate. kcat is 0.27 (sec-1) with p-
nitrophenyl beta-D-thioglucoside as substrate. kcat is 12.1
(sec-1) with n-heptyl-beta-D-glucoside as substrate. kcat is 9.8
(src-1) with n-octyl-beta-D-glucoside as substrate. kcat is
0.038 (sec-1) n-octyl-beta-D-thioglucopyranoside as substrate.
{ECO:0000269|PubMed:21521631};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q7XKV4-1; Sequence=Displayed;
Note=Derived from EST data. No experimental confirmation
available.;
Name=2;
IsoId=Q7XKV4-2; Sequence=VSP_038503, VSP_038504;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAF14984.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AL731582; CAE05483.2; -; Genomic_DNA.
EMBL; AP008210; BAF14984.1; ALT_SEQ; Genomic_DNA.
EMBL; AP014960; BAS89674.1; -; Genomic_DNA.
EMBL; CM000141; EEE61179.1; -; Genomic_DNA.
EMBL; AK100820; BAG94781.1; -; mRNA.
RefSeq; XP_015636597.1; XM_015781111.1. [Q7XKV4-1]
UniGene; Os.59390; -.
PDB; 3PTK; X-ray; 2.49 A; A/B=25-510.
PDB; 3PTM; X-ray; 2.40 A; A/B=25-510.
PDB; 3PTQ; X-ray; 2.45 A; A/B=25-510.
PDBsum; 3PTK; -.
PDBsum; 3PTM; -.
PDBsum; 3PTQ; -.
ProteinModelPortal; Q7XKV4; -.
SMR; Q7XKV4; -.
STRING; 39947.LOC_Os04g39880.1; -.
CAZy; GH1; Glycoside Hydrolase Family 1.
PaxDb; Q7XKV4; -.
EnsemblPlants; Os04t0474800-02; Os04t0474800-02; Os04g0474800. [Q7XKV4-2]
GeneID; 4336145; -.
Gramene; Os04t0474800-02; Os04t0474800-02; Os04g0474800. [Q7XKV4-2]
KEGG; osa:4336145; -.
eggNOG; KOG0626; Eukaryota.
eggNOG; COG2723; LUCA.
HOGENOM; HOG000088630; -.
InParanoid; Q7XKV4; -.
KO; K01188; -.
OMA; NRWWLDP; -.
Reactome; R-OSA-189085; Digestion of dietary carbohydrate.
Proteomes; UP000059680; Chromosome 4.
ExpressionAtlas; Q7XKV4; differential.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0033907; F:beta-D-fucosidase activity; IDA:UniProtKB.
GO; GO:0004565; F:beta-galactosidase activity; IDA:UniProtKB.
GO; GO:0080083; F:beta-gentiobiose beta-glucosidase activity; IDA:UniProtKB.
GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
GO; GO:0047701; F:beta-L-arabinosidase activity; IDA:UniProtKB.
GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IDA:UniProtKB.
GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:1901657; P:glycosyl compound metabolic process; IBA:GO_Central.
InterPro; IPR001360; Glyco_hydro_1.
InterPro; IPR033132; Glyco_hydro_1_N_CS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR10353; PTHR10353; 1.
Pfam; PF00232; Glyco_hydro_1; 1.
PRINTS; PR00131; GLHYDRLASE1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted;
Signal.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 510 Beta-glucosidase 12. {ECO:0000255}.
/FTId=PRO_0000390329.
REGION 473 474 Substrate binding. {ECO:0000244|PDB:3PTQ,
ECO:0000269|PubMed:21521631}.
ACT_SITE 203 203 Proton donor.
{ECO:0000269|PubMed:21521631}.
ACT_SITE 417 417 Nucleophile.
{ECO:0000269|PubMed:21521631}.
BINDING 53 53 Substrate. {ECO:0000244|PDB:3PTQ,
ECO:0000269|PubMed:21521631}.
BINDING 157 157 Substrate. {ECO:0000244|PDB:3PTQ,
ECO:0000269|PubMed:21521631}.
BINDING 202 202 Substrate. {ECO:0000244|PDB:3PTM,
ECO:0000269|PubMed:21521631}.
BINDING 346 346 Substrate. {ECO:0000244|PDB:3PTQ,
ECO:0000269|PubMed:21521631}.
BINDING 466 466 Substrate.
{ECO:0000250|UniProtKB:Q75I93}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 361 361 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 425 425 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 208 243 {ECO:0000244|PDB:3PTK,
ECO:0000244|PDB:3PTM,
ECO:0000244|PDB:3PTQ,
ECO:0000269|PubMed:21521631}.
DISULFID 222 230 {ECO:0000244|PDB:3PTK,
ECO:0000244|PDB:3PTM,
ECO:0000244|PDB:3PTQ,
ECO:0000269|PubMed:21521631}.
VAR_SEQ 1 119 Missing (in isoform 2).
{ECO:0000303|PubMed:12869764}.
/FTId=VSP_038503.
VAR_SEQ 120 122 LPN -> MAD (in isoform 2).
{ECO:0000303|PubMed:12869764}.
/FTId=VSP_038504.
MUTAGEN 276 276 H->M: Decreases the kcat/Km values 2 to
6-fold depending on the substrate.
{ECO:0000269|PubMed:21521631}.
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


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