ID   AMYM_BACAD              Reviewed;         586 AA.
AC   P32818;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Maltogenic alpha-amylase;
DE            EC=3.2.1.133;
DE   AltName: Full=Glucan 1,4-alpha-maltohydrolase;
OS   Bacillus acidopullulyticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=28030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kelly A.P., Diderichsen B., Jorgensen S.T., McConnell D.J.;
RT   "Molecular genetics analysis of a maltogenic amylase gene of Bacillus
RT   acidopullulyticus.";
RL   Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts starch into maltose.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides so as to remove successive alpha-maltose residues
CC         from the non-reducing ends of the chains.; EC=3.2.1.133;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P38940};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P38940};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; Z22520; CAA80246.1; -; Genomic_DNA.
DR   PIR; S34731; S34731.
DR   AlphaFoldDB; P32818; -.
DR   SMR; P32818; -.
DR   CAZy; CBM34; Carbohydrate-Binding Module Family 34.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0043897; F:glucan 1,4-alpha-maltohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02857; E_set_CDase_PDE_N; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.90.400.10; -; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004185; Glyco_hydro_13_lg-like_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02903; Alpha-amylase_N; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding.
FT   CHAIN           1..586
FT                   /note="Maltogenic alpha-amylase"
FT                   /id="PRO_0000054295"
FT   ACT_SITE        328
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   ACT_SITE        357
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   BINDING         147
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q60053"
FT   BINDING         152
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q60053"
FT   BINDING         153
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q60053"
FT   BINDING         172
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q60053"
FT   BINDING         174
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q60053"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   BINDING         326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   BINDING         423..424
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   BINDING         468
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   BINDING         472
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   SITE            424
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   586 AA;  68520 MW;  EEC050711DCD627A CRC64;
     MFREAIYHRP KDNYAYACAN GELHIRIRTK KDDMKEVTLV YGDTYEFDDN KWTYSTAHMK
     KTGSDQLFDY WLASVTPRYK RLRYGFIVND RKDSTCFTEK GFYPEPPVND ISYYFSFPYV
     NQADIFQAPE WVKDTVWYQI FPERFANGNK DNDPDGTLPW GSREPEIDNF FGGDLEGVIE
     HIDYLKELGI GGIYFTPIFK AHSNHKYDTI DYMEIDPQFG TKETLKKLID VCHKNGIKVM
     LDAVFNHSGV FFPPFQDVVE KGKNSKYQDW FHIREFPLVM EPRPNYDTFG FTSSMPKFKT
     ENPEVKEYLL EVGRYWVREF DIDGWRLDVA NEVSHAFWRE FRREVKAIKP DLYILGEIWH
     DSLPWLRGDQ FDAVMNYPLS TNIVNLFANQ SVSVKEFVEN MSHVIHMYPD TVNEAAFNLV
     GSHDTPRILT QCGEDVERLK QVFVLLLTFI GTPCIYYGDE IGLTGGQDPG CRKCMEWNPD
     QQNRELLQHV RKLIQLRSEN PLLANEGELT FVPPKNEEDP CLAYTKSNEE KTIMIIINKS
     KNSVEYPLSF DAAEQTVKNL WNQEQLILQN GQTLELKAND FKILEF