ID   AMYB_VIGUN              Reviewed;         496 AA.
AC   O64407;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Beta-amylase;
DE            EC=3.2.1.2;
DE   AltName: Full=1,4-alpha-D-glucan maltohydrolase;
GN   Name=BMY1;
OS   Vigna unguiculata (Cowpea).
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3917;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. C-88;
RA   Bhullar S.S., Willmitzer L., Kossmann J.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
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; AJ225087; CAA12395.1; -; mRNA.
DR   PIR; T11575; T11575.
DR   AlphaFoldDB; O64407; -.
DR   SMR; O64407; -.
DR   CAZy; GH14; Glycoside Hydrolase Family 14.
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_0000153940"
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;  56237 MW;  F2EDDBE1E307C1A5 CRC64;
     MASLDKNMLL NYVPVYVMLP LGVVSVNNVF EDPEGLKEQL VQLREAGVDG VMVDVWWGII
     EQKGPKQYDW SAYKSLFQLV QECGLKLQAI MSFHQCGGNV GDVVNIPIPQ WVLDIGESDP
     DIFYTNRSGT RDKEYLTIGV DNKPIFHGRT AIEVYSDYMK SFRENMSDFL KSEVIIDIEV
     GLGPAGELRY PSYPQNQGWV FPGIGEFQCY DKYLKAEFKA AAARAGHSEW ELPDDAGTYN
     DVPESTEFFK TNGTYLTEKG KFFLTWYSNQ LLNHGDEILD EANKAFLGCK VNLAIKVSGI
     HWWYKAQNHA AELTAGYYNL DDRDGYRPIA KMVSRHHASL NFTCLEMRDS EQSSDAQSGP
     QELVQQVLSG GWRENIEVAG ENALSRYDAT AYNQIILNAR PQGVNKDGPP KHRMYGVTYL
     RLSDELLQQS NFDIFKKFVV KMHADQDYCE DPQEYNHGIP PLKRSEPKIP VDVLNEATKP
     IPPFPWDSET DMKVDG