ID   AGLU_ORYSJ              Reviewed;         885 AA.
AC   Q653V7; Q0DA62;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Probable alpha-glucosidase Os06g0675700;
DE            EC=3.2.1.20;
DE   AltName: Full=Maltase;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os06g0675700, LOC_Os06g46284;
GN   ORFNames=B1153E06.2, OsJ_22347 {ECO:0000312|EMBL:EEE66212.1};
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=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   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   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   [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   PROTEIN SEQUENCE OF 34-43.
RX   PubMed=10617595; DOI=10.1074/jbc.275.1.129;
RA   Chang T., Kuo M.-C., Khoo K.-H., Inoue S., Inoue Y.;
RT   "Developmentally regulated expression of a peptide:N-glycanase during
RT   germination of rice seeds (Oryza sativa) and its purification and
RT   characterization.";
RL   J. Biol. Chem. 275:129-134(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC         glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
CC   -!- CAUTION: Was isolated and reported to have peptide:N-glycanase activity
CC       (PubMed:10617595). However, its strong sequence similarity with alpha-
CC       glucosidase proteins suggest that it is not its function in vivo.
CC       {ECO:0000305|PubMed:10617595}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP004989; BAD45910.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF20261.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS99103.1; -; Genomic_DNA.
DR   EMBL; CM000143; EEE66212.1; -; Genomic_DNA.
DR   EMBL; AK119824; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015643120.1; XM_015787634.1.
DR   AlphaFoldDB; Q653V7; -.
DR   SMR; Q653V7; -.
DR   STRING; 39947.Q653V7; -.
DR   BindingDB; Q653V7; -.
DR   ChEMBL; CHEMBL1163102; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   PaxDb; 39947-Q653V7; -.
DR   EnsemblPlants; Os06t0675700-01; Os06t0675700-01; Os06g0675700.
DR   GeneID; 4341824; -.
DR   Gramene; Os06t0675700-01; Os06t0675700-01; Os06g0675700.
DR   KEGG; osa:4341824; -.
DR   eggNOG; KOG1065; Eukaryota.
DR   HOGENOM; CLU_000631_11_1_1; -.
DR   InParanoid; Q653V7; -.
DR   OMA; YKGAVWP; -.
DR   OrthoDB; 5480935at2759; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000007752; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR   CDD; cd06602; GH31_MGAM_SI_GAA; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR030458; Glyco_hydro_31_AS.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR030459; Glyco_hydro_31_CS.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF133; ALPHA-GLUCOSIDASE; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR   PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000269|PubMed:10617595"
FT   CHAIN           34..885
FT                   /note="Probable alpha-glucosidase Os06g0675700"
FT                   /id="PRO_0000249005"
FT   ACT_SITE        443
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        446
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        540
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        467
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        477
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        576
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        844
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        34
FT                   /note="G -> S (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="S -> L (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="A -> P (in Ref. 5; AK119824)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        445
FT                   /note="N -> S (in Ref. 5; AK119824)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   885 AA;  96336 MW;  34ABDF8A194C75A5 CRC64;
     MMGSPPAPPA RRLGALAVFL LALFLAAPWG VDCGYNVASV AGSKNRLRAR LELAGGGGGA
     APELGPDVRR LSLTASLETD SRLHVRITDA DHPRWEVPQD VIPRPSPDSF LAATRPGGGR
     VLSTATSDLT FAIHTSPFRF TVTRRSTGDV LFDTTPNLVF KDRYLELTSS LPPPGRASLY
     GLGEQTKRTF RLQRNDTFTL WNSDIAAGNV DLNLYGSHPF YMDVRSGGGG GGGAAHGVLL
     LNSNGMDVIY GGSYVTYKVI GGVLDFYFFA GPSPLAVVDQ YTQLIGRPAP MPYWSFGFHQ
     CRYGYKNVAD LEGVVAGYAK ARIPLEVMWT DIDYMDAYKD FTLDPVNFPA DRMRPFVDRL
     HRNGQKFVVI IDPGINVNTT YGTFVRGMKQ DIFLKWNGSN YLGVVWPGNV YFPDFLNPRA
     AEFWAREIAA FRRTLPVDGL WVDMNEISNF VDPPPLNAID DPPYRINNSG VRRPINNKTV
     PASAVHYGGV AEYDAHNLFG FLEARATHDA LLRDTGRRPF VLSRSTFVGS GRYTAHWTGD
     NAATWEDLHY SINTMLSFGL FGIPMIGADI CGFGGNTTEE LCSRWIQLGA FYPFSRDHSA
     IGTVRRELYL WESVARSARK ALGLRYRLLP YLYTLMYEAH TTGAPIARPL FFSYPGDVET
     YGIDRQFLLG RGVLVSPVLE PGATTVTAYF PAGRWFSLYD FSLAVATKTG KRVTLPAPAD
     TVNVHVAGGN ILTLQQPALT SSRVRQSVVH LLVALADDGT ATGDLFLDDG ESPEMAGPRS
     RWSQIKFSGA TESGGGVVRV RSHVVHDSYA PSRTMAIGKV VLMGLRSAAP PKGFAVYANG
     VQVNASTAVG GAAGSPEKGA LGVAHVSGLT LVVGQEFDLK VVMTY
//