ID   AMYB_MAIZE              Reviewed;         488 AA.
AC   P55005;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Beta-amylase;
DE            EC=3.2.1.2;
DE   AltName: Full=1,4-alpha-D-glucan maltohydrolase;
GN   Name=BMY1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. TN351; TISSUE=Aleurone;
RX   PubMed=9046591; DOI=10.1104/pp.113.2.403;
RA   Wang S.M., Lue W.L., Wu S.Y., Huang H.W., Chen J.;
RT   "Characterization of a maize beta-amylase cDNA clone and its expression
RT   during seed germination.";
RL   Plant Physiol. 113:403-409(1997).
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; Z25871; CAA81091.1; -; mRNA.
DR   PIR; S37075; S37075.
DR   RefSeq; NP_001105496.1; NM_001112026.1.
DR   AlphaFoldDB; P55005; -.
DR   SMR; P55005; -.
DR   STRING; 4577.GRMZM2G058310_P01; -.
DR   CAZy; GH14; Glycoside Hydrolase Family 14.
DR   PaxDb; P55005; -.
DR   PRIDE; P55005; -.
DR   GeneID; 542472; -.
DR   KEGG; zma:542472; -.
DR   MaizeGDB; 30053; -.
DR   eggNOG; ENOG502QUU5; Eukaryota.
DR   OrthoDB; 533202at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P55005; baseline and differential.
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; Reference proteome.
FT   CHAIN           1..488
FT                   /note="Beta-amylase"
FT                   /id="PRO_0000153935"
FT   ACT_SITE        184
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10050"
FT   ACT_SITE        378
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         340
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         379..380
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         418
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
SQ   SEQUENCE   488 AA;  55180 MW;  A04D57F1C73C064E CRC64;
     MAGNALANYV QVYVMLPLDV ITVDNTFEKE DETRAQLKKL TEAGADGVMI DVWWGLVEGK
     EPGVYDWSAY RQVFKLVQEA GLKLQAIMSC HQCGGNVGDV VNIPIPQWVR DVGKSNPDIF
     YTNRSGLTNI EYLTLGVDDQ PLFHGRTAIQ LYADYMKSFR ENMADFLDAG VVVDIEVGLG
     PAGEMRYPSY PQSQGWVFPG VGEFICYDKY LQADFKAAAE EAGHPEWDLL DDAGTYNDTP
     EKTQFFADNG TYQTDKGKFF LTWYSNKLIK HGDKILDEAN KVFLGCKVQL AIKVSGIHWW
     YNVPNHAAEL TAGYYNLDDR DGYRTIAHML TRHRASMNFT CAEMRDSEQS SEAKSAPEEL
     VQQVLSAGWR EGLNLACENA LNRYDATAYN TILRNARPQG INKNGPPEHK LHGFTYLRVS
     DELFQEQNYT TFKTFVRRMH ANLDYNPNVD PVAPLERSKA EIPIEEILEV AQPKLEPFPF
     DKDTDLPV