ID A0A0D9Z1W3_9ORYZ Unreviewed; 557 AA.
AC A0A0D9Z1W3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Beta-amylase {ECO:0000256|ARBA:ARBA00012594, ECO:0000256|RuleBase:RU000509};
DE EC=3.2.1.2 {ECO:0000256|ARBA:ARBA00012594, ECO:0000256|RuleBase:RU000509};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM03G03160.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM03G03160.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM03G03160.1}
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|ARBA:ARBA00000546,
CC 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; A0A0D9Z1W3; -.
DR SMR; A0A0D9Z1W3; -.
DR STRING; 40148.A0A0D9Z1W3; -.
DR EnsemblPlants; OGLUM03G03160.1; OGLUM03G03160.1; OGLUM03G03160.
DR EnsemblPlants; OGLUM03G03160.2; OGLUM03G03160.2; OGLUM03G03160.
DR Gramene; OGLUM03G03160.1; OGLUM03G03160.1; OGLUM03G03160.
DR Gramene; OGLUM03G03160.2; OGLUM03G03160.2; OGLUM03G03160.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR HOGENOM; CLU_016754_5_1_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
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; IPR018238; Glyco_hydro_14_CS.
DR InterPro; IPR001371; Glyco_hydro_14B_pln.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR31352:SF54; BETA-AMYLASE 2, CHLOROPLASTIC; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR PRINTS; PR00842; GLHYDLASE14B.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000509};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000509};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000509};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU000509};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961}.
FT ACT_SITE 267
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 465
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 466..467
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 499
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ SEQUENCE 557 AA; 60757 MW; 8DF437F3327B5C45 CRC64;
MMSLNLAHQT GAAAAVAPAA PRTAVVAAAA GTVSAPAVAP AAAPSLQLQT QTVDPAAPAQ
GPDLPMAFQA LVESLPEEQH PDVGGEERRK VGVPVYVMMP LDTVRKDGNG LNRRKAVEAS
LKALKSAGAE GIMVDVWWGI AECEGPGRYN FTGYMELMEM AKKNGLKVQA VMSFHQCGGN
VGDSVTIPLP KWVLEEMDKD QDLAYTDRSG RRNYEYLSLG ADAMPVLKGR TPVQCYGDFM
RAFRDHFAAF MGNTIVEIQV GMGPAGELRY PSYPESNGTW RFPGIGEFQC YDRYMLSSLK
AAAEAVGKPE WGNAGPGDSG GYNDWPEDSP FFRREGGWNT PYGEFFMSWY SQMLLEHGER
ILSAASGVYT GTPGVKISVK VAGIHWHYGT RSHAAELTAG YYNTRHHDGY QPIARMLARH
GAVLNFTCVE MRNHEQPQDA QCRPEELVQQ VAAAARESGV GLAGENALPR YDETAHDQIV
TTAAEKAEEE RMVAFTYLRM GPDLFQPDNW RRFAAFVKRM TESGVRDVCR EQVEREAQGV
AHATGSLVHE AAVALSN
//
