ID   CDAS_LYSSH              Reviewed;         591 AA.
AC   Q08341;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Cyclomaltodextrinase;
DE            Short=CDase;
DE            EC=3.2.1.54;
DE   AltName: Full=Cyclomaltodextrin hydrolase, decycling;
OS   Lysinibacillus sphaericus (Bacillus sphaericus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=E-244;
RX   PubMed=7763728; DOI=10.1007/bf00228606;
RA   Oguma T., Matsuyama A., Kikuchi M., Nakano E.;
RT   "Cloning and sequence analysis of the cyclomaltodextrinase gene from
RT   Bacillus sphaericus and expression in Escherichia coli cells.";
RL   Appl. Microbiol. Biotechnol. 39:197-203(1993).
CC   -!- FUNCTION: Hydrolyzes cyclodextrins. Can also act on linear
CC       maltodextrins, with the exception of maltose.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclomaltodextrin + H2O = linear maltodextrin;
CC         Xref=Rhea:RHEA:23980, Rhea:RHEA-COMP:14584, Rhea:RHEA-COMP:14707,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17623, ChEBI:CHEBI:18398; EC=3.2.1.54;
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0.;
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.;
CC   -!- SUBUNIT: Monomer.
CC   -!- INDUCTION: By cyclodextrins.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; X62576; CAA44454.1; -; Genomic_DNA.
DR   PIR; S48130; S48130.
DR   AlphaFoldDB; Q08341; -.
DR   SMR; Q08341; -.
DR   CAZy; CBM34; Carbohydrate-Binding Module Family 34.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; Q08341; -.
DR   GO; GO:0047798; F:cyclomaltodextrinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding.
FT   CHAIN           1..591
FT                   /note="Cyclomaltodextrinase"
FT                   /id="PRO_0000054308"
FT   ACT_SITE        327
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   ACT_SITE        356
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   BINDING         146
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q60053"
FT   BINDING         148
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q60053"
FT   BINDING         151
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         170
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         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   BINDING         325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   BINDING         422..423
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   BINDING         467
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   BINDING         471
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P38940"
FT   SITE            423
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   591 AA;  67899 MW;  702FD7BA99A23E3F CRC64;
     MIMLEAVYHR MGQNWSYAYN DSTLHIRIRT KRDNVPRIDL HCGEKYDPEK YKETIPMERM
     ASDGLFDYWQ AAVQPRYRRL VYYFALHSDN GDAVYFMEKG FFDQPPKVMY EGLFDFPYLN
     RQDVHTPPAW VKEAIFYQIF PERFANGDPS NDPEGVQEWG GTPSAGNFFG GDLQGVIDHL
     DYLSDLGVNA LYFNPLFAAT TNHKYDTADY MKIDPQFGTN EKLKELVDAC HARGMRVLLD
     AVFNHCGHTF PPFVDVLNNG LNSRYADWFH VREWPLRVVD GIPTYDTFAF EPIMPKLNTG
     NEEVKAYLLN VGRYWLEEMG LDGWRLDVAN EVDHQFWREF RSEIKRINPS AYILGEIMHD
     SMPWLQGDQF DAVMNYPFTN ILLNFFARRL TNAAEFAQAI GTQLAGYPQQ VTEVSFNLLG
     SHDTTRLLTL CSGNVERMKL ATLFQLTYQG TPCIYYGDEI GMDGEYDPLN RKCMEWDKSK
     QNTELLAFFR SMISLRKAHP ALRGSGLRFL PVLEHPQLLV YERWDDNERF LIMLNNEDAP
     VNVVIPAAQP GASWRTVNGE PCAVVEESSI QAALPPYGYA ILHAPIAGTA E