BGL14_ORYSJ
ID BGL14_ORYSJ Reviewed; 516 AA.
AC Q7XPY7; A0A0P0WCL2;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable inactive beta-glucosidase 14 {ECO:0000305};
DE Short=Os4bglu14 {ECO:0000303|PubMed:17196101};
DE Flags: Precursor;
GN Name=BGLU14 {ECO:0000303|PubMed:17196101};
GN OrderedLocusNames=Os04g0513100 {ECO:0000312|EMBL:BAS90056.1},
GN LOC_Os04g43360 {ECO:0000305};
GN ORFNames=OSJNBa0004N05.21 {ECO:0000312|EMBL:CAE03397.2};
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 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 [6]
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).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=25219312; DOI=10.1016/j.plantsci.2014.07.009;
RA Baiya S., Hua Y., Ekkhara W., Ketudat Cairns J.R.;
RT "Expression and enzymatic properties of rice (Oryza sativa L.) monolignol
RT beta-glucosidases.";
RL Plant Sci. 227:101-109(2014).
CC -!- TISSUE SPECIFICITY: Expressed in flowers and endosperm.
CC {ECO:0000269|PubMed:25219312}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Glu residue acting as catalytic proton
CC donor. Its enzyme activity is therefore unsure. {ECO:0000305}.
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DR EMBL; AL606622; CAE03397.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF15216.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS90056.1; -; Genomic_DNA.
DR EMBL; AK067841; BAG90635.1; -; mRNA.
DR RefSeq; XP_015634345.1; XM_015778859.1.
DR AlphaFoldDB; Q7XPY7; -.
DR SMR; Q7XPY7; -.
DR STRING; 4530.OS04T0513100-01; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q7XPY7; -.
DR PRIDE; Q7XPY7; -.
DR EnsemblPlants; Os04t0513100-01; Os04t0513100-01; Os04g0513100.
DR GeneID; 4336388; -.
DR Gramene; Os04t0513100-01; Os04t0513100-01; Os04g0513100.
DR KEGG; osa:4336388; -.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q7XPY7; -.
DR OMA; HFDMPLH; -.
DR OrthoDB; 408001at2759; -.
DR BRENDA; 3.2.1.126; 8948.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q7XPY7; 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: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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..516
FT /note="Probable inactive beta-glucosidase 14"
FT /id="PRO_0000390331"
FT ACT_SITE 405
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 43
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 145
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 190
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 334
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 454
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 461..462
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 210..217
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT DISULFID 342..347
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
SQ SEQUENCE 516 AA; 58823 MW; 19D0C38BABBC7906 CRC64;
MAAAWLVVLL TVHRLLHLSG VSAVDRSQFP PDFLFGTSSS AYQVEGGYLE GNKGLSNWDV
FTHKQGTIED GSNGDTANDH YHRYMEDIEL MHSLGVNSYR FSISWARILP KGRFGDVNPD
GVAFYNALID GLVQKGIQPF VTICHYDIPH ELDERYGGWL SPEIQKDFSY FAEVCFKLFG
DRIKFWTTFN QPNLSIKFSY MDGFYSPGRC SEPFGKCALG NSSIEPYVAG HNIILSHANA
VSVYRNKYQG KQGGQIGIAL SITWYEPFRN TTIDLLAVKR ALSFGASWFL DPILLGDYPT
EMREVLGQSL PKFTSKQKNR LQSTKLDFIG LNHYTTCYVK DCIFSPCEID PVNADARVFS
LYERDGVPIG KATGAPFFHD VPRGMEEAVT YYKQRYNNTP TYITENGYSQ ASNSNMTAKD
FTNDTGRITY IQGYLISLAS AIRKGADVRG YFVWSLLDDF EWNFGYTLRF GLYHVHYKTL
KRTPKLSVDW YRKFLTGSLL RRKFRDESQL HKFNSY
