CDAS_THEP3
ID CDAS_THEP3 Reviewed; 574 AA.
AC P29964; B0K7U0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cyclomaltodextrinase;
DE Short=CDase;
DE EC=3.2.1.54;
DE AltName: Full=Cyclomaltodextrin hydrolase, decycling;
GN OrderedLocusNames=Teth39_0676;
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-5.
RX PubMed=1644767; DOI=10.1128/jb.174.16.5400-5405.1992;
RA Podkovyrov S.M., Zeikus J.G.;
RT "Structure of the gene encoding cyclomaltodextrinase from Clostridium
RT thermohydrosulfuricum 39E and characterization of the enzyme purified from
RT Escherichia coli.";
RL J. Bacteriol. 174:5400-5405(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP ACTIVE SITES, AND MUTANTS ASP-325-ASN; GLU-354-GLN AND ASP-421-ASN.
RX PubMed=8425614; DOI=10.1016/0014-5793(93)81288-b;
RA Podkovyrov S.M., Burdette D., Zeikus J.G.;
RT "Analysis of the catalytic center of cyclomaltodextrinase from
RT Thermoanaerobacter ethanolicus 39E.";
RL FEBS Lett. 317:259-262(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 -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; M88602; AAA23219.1; -; Genomic_DNA.
DR EMBL; CP000924; ABY94339.1; -; Genomic_DNA.
DR RefSeq; WP_012269128.1; NC_010321.1.
DR AlphaFoldDB; P29964; -.
DR SMR; P29964; -.
DR STRING; 340099.Teth39_0676; -.
DR CAZy; CBM34; Carbohydrate-Binding Module Family 34.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; P29964; -.
DR EnsemblBacteria; ABY94339; ABY94339; Teth39_0676.
DR KEGG; tpd:Teth39_0676; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_6_2_9; -.
DR OMA; RSENFLM; -.
DR Proteomes; UP000002156; Chromosome.
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; IPR014756; Ig_E-set.
DR InterPro; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02903; Alpha-amylase_N; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..574
FT /note="Cyclomaltodextrinase"
FT /id="PRO_0000054309"
FT ACT_SITE 325
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:8425614"
FT ACT_SITE 354
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:8425614"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q60053"
FT BINDING 168
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 243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 420..421
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT SITE 421
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MUTAGEN 325
FT /note="D->N: Loss of activity."
FT MUTAGEN 354
FT /note="E->Q: Loss of activity."
FT MUTAGEN 421
FT /note="D->N: Loss of activity."
FT CONFLICT 4
FT /note="E -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="P -> G (in Ref. 1; AAA23219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 68066 MW; 94CBCDA1383251F3 CRC64;
MIKEAIFHKS DVPYAYPLNE NQLKIVLRTA VFDVDRVYVL YKDRYDWLGK FKIKPMVLTH
TNELFDYYET TLELNKKFVY FFYLVSDGGE KLYYTEAGFY KKRPENHFWG FFHYPYIGEK
DVFFAPEWTS DCMVYQIFPE RFNNGDKSND PENVKPWGEK PTADSFFGGD LQGIIDKIDY
LKDLGINAIY LTPIFLSHST HKYDTTDYYT IDPHFGDTQK ARELVQKCHD NGIKVIFDAV
FNHCGYDFFA FQDVIKNGKK SKYWDWFNIY EWPIKTHPKP SYEAFADTVW RMPKLMTKNP
EVQKYLLEVA EYWIKEVDID GWRLDVANEI DHHFWRKFRE VVKAAKPEAI IVGEVWHDAS
PWLRGDQFDS VMNYPFRNAV VDFFAKRKIS ASRFNTMITE QLMRHMDSVN RVMFNLIGSH
DTERFLTLAN GMVARMKLAL VFQFTFVGIP YIYYGDEVGM VGDYDPDCRR CMIWEEEKQN
KSIFNFYKKL ISIRRENEEL KYGSFCTLYA IGRVFAFKRE YKGKSIIVVL NNSSKQEVIF
LNEVEGKEDI LKMKELKRSG NLLYLQPNSA YILK
