ID   AMYB_MEDSA              Reviewed;         496 AA.
AC   O22585;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Beta-amylase;
DE            EC=3.2.1.2;
DE   AltName: Full=1,4-alpha-D-glucan maltohydrolase;
GN   Name=BMY1; Synonyms=BA1;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root;
RX   PubMed=9847126; DOI=10.1104/pp.118.4.1495;
RA   Gana J.A., Kalengamaliro N.E., Cunningham S.M., Volenec J.J.;
RT   "Expression of beta-amylase from alfalfa taproots.";
RL   Plant Physiol. 118:1495-1506(1998).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
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DR   EMBL; AF026217; AAD04188.1; -; mRNA.
DR   PIR; T09300; T09300.
DR   AlphaFoldDB; O22585; -.
DR   SMR; O22585; -.
DR   CAZy; GH14; Glycoside Hydrolase Family 14.
DR   PRIDE; O22585; -.
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   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; PTHR31352; 1.
DR   Pfam; PF01373; Glyco_hydro_14; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   PRINTS; PR00842; GLHYDLASE14B.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR   PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           1..496
FT                   /note="Beta-amylase"
FT                   /id="PRO_0000153936"
FT   REGION          455..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10050"
FT   ACT_SITE        381
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         382..383
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         421
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
SQ   SEQUENCE   496 AA;  56140 MW;  80F444482AB15E84 CRC64;
     MATSNKNMLL NYVPVYVMLP LGVINVNNVF EDPDGLKEQL VQLRAAGVDG VMIDVWWGII
     EQKGPKEYDW SAYKSLFQLV QKCGLKLQAI MSFHQCGGNV GDVVNIPLPK WVLDIGESDP
     DIFYTNRSGI RNQEYLSIGV DNKPIFHGRT AIEIYSDYMK SFRENMSDLL KSEVIIDIEV
     GLGPAGELRY PSYPQNQGWQ FPGIGEFQCY DKYLRESFKA AAAKAGHSEW ELPDDAGTYN
     DVPESTEFFK TNGTYLTEKG KFFLTWYSNQ LLNHGDQILD EANKAFLGCK VKLAIKVSGI
     HWWYKAPNHA AELTAGYYNL DDRDGYRPIA KIVSRHHAIL NFTCLEMRDS EQSSDAHSSP
     QKLVQQVLSG GWRENIEVAG ENALSRYDAT AYNQIILNAR PQGVNKDGPP KLRMYGVTYL
     RLSDDLMQQS NFDIFKKFVV KMHADQDYCS DPEKYNHGIP PLKRSGPKIP DDVLNEATKP
     IPPFPWDSET DMKVDG