ID   A0A0D9VU07_9ORYZ        Unreviewed;       449 AA.
AC   A0A0D9VU07;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Beta-amylase {ECO:0000256|RuleBase:RU000509};
DE            EC=3.2.1.2 {ECO:0000256|RuleBase:RU000509};
OS   Leersia perrieri.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX   NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR03G15160.1, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR03G15160.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:LPERR03G15160.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA   Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA   Zhang J., Wing R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:LPERR03G15160.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides so as to remove successive maltose units from the
CC         non-reducing ends of the chains.; EC=3.2.1.2;
CC         Evidence={ECO:0000256|RuleBase:RU000509};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family.
CC       {ECO:0000256|ARBA:ARBA00005652, ECO:0000256|RuleBase:RU000509}.
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DR   AlphaFoldDB; A0A0D9VU07; -.
DR   EnsemblPlants; LPERR03G15160.1; LPERR03G15160.1; LPERR03G15160.
DR   Gramene; LPERR03G15160.1; LPERR03G15160.1; LPERR03G15160.
DR   eggNOG; ENOG502QPTU; Eukaryota.
DR   HOGENOM; CLU_016754_5_0_1; -.
DR   Proteomes; UP000032180; Chromosome 3.
DR   GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016161; F:beta-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001554; Glyco_hydro_14.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31352:SF32; BETA-AMYLASE; 1.
DR   PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF01373; Glyco_hydro_14; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000509};
KW   Glycosidase {ECO:0000256|RuleBase:RU000509};
KW   Hydrolase {ECO:0000256|RuleBase:RU000509};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU000509};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032180}.
SQ   SEQUENCE   449 AA;  47406 MW;  9F81513420532831 CRC64;
     MEAVLMQQAA VAAPAARRRC AAGEDAAVRG RGSPGLVRLG FLPRRRWCSG RAVRVHLAPA
     RAHLAVDRSS EAAAAVEDFN DEAAVRLFVG LPTDVVCSDG VNRAKAVSAG LRALKLLGVD
     GVELLVSWAV AQPNSGDGFE WAGYLAVAGM VRDAGLCLRV SLDTHALPAW AAADPEILLA
     DRSGNRRDGC LSFAVDELPV LAGKSPLQAY EAFYRGFADA FRDFFGSTIT DVTVSLGPNG
     ELRYPSYPPG SDGGDYGGAG EFQCYDKHML ARLKQHAAAA GQPMWGLSGP HDAPRYGESP
     ETSAFFRSPG GSSETAYGRF FLSWYSGELL AHGDRVLAVA SKVFDGMPVE LSAKAPLMGR
     RSRAAEATAG LHGGYGPVAE TFARHGCTRM GADFFSPDHW PLFVQMVRAM ECPEEAHEDD
     LAPAGDGARL AVPRAGAAAD ATAKEAQTV
//