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BGL23_ORYSJ
ID   BGL23_ORYSJ             Reviewed;         542 AA.
AC   Q6L597;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Putative beta-glucosidase 23;
DE            Short=Os5bglu23;
DE            EC=3.2.1.21;
DE   Flags: Precursor;
GN   Name=BGLU23; OrderedLocusNames=Os05g0366800, LOC_Os05g30390;
GN   ORFNames=OJ1393_A07.1, OSJNBa0090H02.13;
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(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=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   [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 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}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT38010.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAV31360.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC104279; AAT38010.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC137618; AAV31360.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q6L597; -.
DR   SMR; Q6L597; -.
DR   STRING; 4530.OS05T0366800-00; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   PaxDb; Q6L597; -.
DR   PRIDE; Q6L597; -.
DR   eggNOG; KOG0626; Eukaryota.
DR   InParanoid; Q6L597; -.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
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; 2.
DR   Pfam; PF00232; Glyco_hydro_1; 2.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   5: Uncertain;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..542
FT                   /note="Putative beta-glucosidase 23"
FT                   /id="PRO_0000390340"
FT   ACT_SITE        262
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         405
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         476
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         483..484
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        281..289
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   542 AA;  60955 MW;  011A7FC047901C4B CRC64;
     MAACTSSLVS LLLLLLLLLL LLVAGEATAE AALNFTRQDF PGGLRRRHIC LPGFRDADSI
     TFPRDIESLT CGTHMCLDPR GSHTSVTQCH GECHRRNVIE SQSRFRRTYE GATGEDGRTP
     SIWDTFTHSG RMADNSTGDR AAAGYHKYKE DVKLMSDTGL EAYRFSISWS RLIPRGRGPI
     NPKGLEYYND LIDKLVKRGE ICDCSMGIEI HVTLYHLDFP QALQDEYNGW LSPRIIEDFT
     AYADVCFREF GDLVRHWTTV GEPNVLSIAG YDSGVIPPCR CSPPFGTSCA AGDSTVEPYF
     AAHNSILAHA SAVRLYWDKY QAKQKGVVGT NIYSFWPYPL SRSCADIDAV QRVLDFTIGW
     ILDPLVYGDY PEIMKKQAGS RIPSFTKEQS ELIRGSADFI GINHYKSLYV SDGSNREKAG
     LRDYNADMAA HFRGFGQFDK EDSLNDTERV EYLSSYMGGT LAALRNGANV KGYFVWSFLD
     VFELFAGYHS PFGLHHVDFE DPSLPRQPKL SAQWYSKFLR SEIGINIEKM VSPDEHEHAY
     YQ
 
 
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