ID   AMYB_SECCE              Reviewed;         222 AA.
AC   P30271;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Beta-amylase;
DE            EC=3.2.1.2;
DE   AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE   Flags: Fragment;
GN   Name=BMY1;
OS   Secale cereale (Rye).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Secale.
OX   NCBI_TaxID=4550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Endosperm;
RX   AGRICOLA=IND92007634; DOI=10.1007/BF00226260;
RA   Rorat T., Sadowski J., Grellet F., Daussant J., Delseny M.;
RT   "Characterization of cDNA clones for rye endosperm beta-amylase and
RT   analysis of beta-amylase deficiency in rye mutant lines.";
RL   Theor. Appl. Genet. 83:257-263(1991).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X56785; CAA40105.1; -; mRNA.
DR   PIR; S38779; S38779.
DR   AlphaFoldDB; P30271; -.
DR   SMR; P30271; -.
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; 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.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           <1..222
FT                   /note="Beta-amylase"
FT                   /id="PRO_0000153937"
FT   ACT_SITE        74
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         75..76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10538"
FT   NON_TER         1
SQ   SEQUENCE   222 AA;  24349 MW;  29A66E6EA5C0F718 CRC64;
     SHAAEVTAGY YNLHDRDDYR PIARMLTRHH ASLNFTCAEM RDSEQSSQAM SAPEELVQQV
     WSAGWREGLN IACENALPRY DPTAYNTILR NARPHGINHS SPTEHKLFGF TYLRLSNQLL
     EGQNYVNFKT FVDRMHANLP HDPSVDPVAP LQRSGPEIPI EVILQAAQPK LDPFPFEDHT
     DLPVQCLGGI GGGEVECPAG GIGGEVQQDP TGGMGGELPP AV