ID   AMYB_NIACI              Reviewed;         575 AA.
AC   P06547;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Beta-amylase;
DE            EC=3.2.1.2;
DE   AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE   Flags: Precursor;
OS   Niallia circulans (Bacillus circulans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=1397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BCRC 12254 / NCIMB 11033;
RX   PubMed=2455212; DOI=10.1111/j.1365-2958.1987.tb00531.x;
RA   Siggens K.W.;
RT   "Molecular cloning and characterization of the beta-amylase gene from
RT   Bacillus circulans.";
RL   Mol. Microbiol. 1:86-91(1987).
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P36924};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P36924};
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
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DR   EMBL; Y00523; CAA68578.1; -; Genomic_DNA.
DR   PIR; S03745; S03745.
DR   AlphaFoldDB; P06547; -.
DR   SMR; P06547; -.
DR   CAZy; CBM25; Carbohydrate-Binding Module Family 25.
DR   CAZy; GH14; Glycoside Hydrolase Family 14.
DR   BRENDA; 3.2.1.2; 649.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR005085; CBM25.
DR   InterPro; IPR001554; Glyco_hydro_14.
DR   InterPro; IPR018238; Glyco_hydro_14_CS.
DR   InterPro; IPR000125; Glyco_hydro_14A_bac.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR31352; PTHR31352; 1.
DR   Pfam; PF03423; CBM_25; 1.
DR   Pfam; PF01373; Glyco_hydro_14; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   PRINTS; PR00841; GLHYDLASE14A.
DR   SMART; SM01066; CBM_25; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR   PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Disulfide bond; Glycosidase; Hydrolase;
KW   Metal-binding; Polysaccharide degradation; Signal.
FT   SIGNAL          1..36
FT   CHAIN           37..575
FT                   /note="Beta-amylase"
FT                   /id="PRO_0000001454"
FT   ACT_SITE        199
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10050"
FT   ACT_SITE        395
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P36924"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P36924"
FT   BINDING         84
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P36924"
FT   BINDING         88
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P36924"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P36924"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P36924"
FT   BINDING         171
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P36924"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P36924"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P36924"
FT   BINDING         358
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P36924"
FT   BINDING         396..397
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P36924"
FT   BINDING         424
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P36924"
FT   DISULFID        119..127
FT                   /evidence="ECO:0000250|UniProtKB:P36924"
SQ   SEQUENCE   575 AA;  62899 MW;  724E8C0D66B4A258 CRC64;
     MLHSQKRIWK KIGLCLLSFI LGITVFTGSF GSKAEAAVAG DFQVSVMGPL AKVTDWNSFK
     NQLTTLKNNG VYAITTDVWW GYVESAGDNQ FDWSYYKTYA DTVKQAGLKW VPIISTHRCG
     GNVGDDCNIP LPSWLWSKGS ADEMQFKDES GYVNNESLSP FWSGVGKQYD ELYASFAQNF
     SAYKDMIPKI YLSGGPSGEL RYPSYYPAAG WSYPARGKFQ VYTETAKSAF RTAMTTKYGS
     LDKINAAWGT NLTSMSQISP PTDSDGFYTG GGYNITYGKD FLSWYQSVLE NHLGVIGAAA
     HKNFDPVFGV RIGAKISGIH WQMNNPSMPH SAEHAGGYYD YNRLIQKFKD TDLDLTFTAL
     EMYDSGTAPN YSLPSTLVDT VSSIANSKGV RLNGENALPT GGSGFQKIEE KITRFGYNGF
     TLLRINNIVN SDGSPTAEMS SFKNYVIKHA KPAGDGGGNP VNSVTIYYKK GFNSPYIHYR
     PAGGTWTDVP GVKMPDSEIS GYAKITLDIG SASQLEAAFN DGNNQWDSNN MRNYFFSPGT
     STYIPGTNGT AGSIQAGPPI TSSDFQALPA YEMSI