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P29964 (CDAS_THEP3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cyclomaltodextrinase
Short name=CDase
EC=3.2.1.54
Alternative name(s):
Cyclomaltodextrin hydrolase, decycling
Gene names
Ordered Locus Names:Teth39_0676
OrganismThermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum) [Complete proteome] [HAMAP]
Taxonomic identifier340099 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Thermoanaerobacter

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes cyclodextrins. Can also act on linear maltodextrins, with the exception of maltose.

Catalytic activity

Cyclomaltodextrin + H2O = linear maltodextrin.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functioncyclomaltodextrinase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574Cyclomaltodextrinase
PRO_0000054309

Sites

Active site3251 Ref.3
Active site3541 Ref.3
Metal binding1441Calcium By similarity
Metal binding1461Calcium; via carbonyl oxygen By similarity
Metal binding1491Calcium By similarity
Metal binding1501Calcium By similarity
Metal binding1681Calcium; via carbonyl oxygen By similarity
Metal binding1701Calcium By similarity
Site4211Transition state stabilizer By similarity

Experimental info

Mutagenesis3251D → N: Loss of activity.
Mutagenesis3541E → Q: Loss of activity.
Mutagenesis4211D → N: Loss of activity.
Sequence conflict41E → G AA sequence Ref.1
Sequence conflict2781P → G in AAA23219. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29964 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 94CBCDA1383251F3

FASTA57468,066
        10         20         30         40         50         60 
MIKEAIFHKS DVPYAYPLNE NQLKIVLRTA VFDVDRVYVL YKDRYDWLGK FKIKPMVLTH 

        70         80         90        100        110        120 
TNELFDYYET TLELNKKFVY FFYLVSDGGE KLYYTEAGFY KKRPENHFWG FFHYPYIGEK 

       130        140        150        160        170        180 
DVFFAPEWTS DCMVYQIFPE RFNNGDKSND PENVKPWGEK PTADSFFGGD LQGIIDKIDY 

       190        200        210        220        230        240 
LKDLGINAIY LTPIFLSHST HKYDTTDYYT IDPHFGDTQK ARELVQKCHD NGIKVIFDAV 

       250        260        270        280        290        300 
FNHCGYDFFA FQDVIKNGKK SKYWDWFNIY EWPIKTHPKP SYEAFADTVW RMPKLMTKNP 

       310        320        330        340        350        360 
EVQKYLLEVA EYWIKEVDID GWRLDVANEI DHHFWRKFRE VVKAAKPEAI IVGEVWHDAS 

       370        380        390        400        410        420 
PWLRGDQFDS VMNYPFRNAV VDFFAKRKIS ASRFNTMITE QLMRHMDSVN RVMFNLIGSH 

       430        440        450        460        470        480 
DTERFLTLAN GMVARMKLAL VFQFTFVGIP YIYYGDEVGM VGDYDPDCRR CMIWEEEKQN 

       490        500        510        520        530        540 
KSIFNFYKKL ISIRRENEEL KYGSFCTLYA IGRVFAFKRE YKGKSIIVVL NNSSKQEVIF 

       550        560        570 
LNEVEGKEDI LKMKELKRSG NLLYLQPNSA YILK

« Hide

References

« Hide 'large scale' references
[1]"Structure of the gene encoding cyclomaltodextrinase from Clostridium thermohydrosulfuricum 39E and characterization of the enzyme purified from Escherichia coli."
Podkovyrov S.M., Zeikus J.G.
J. Bacteriol. 174:5400-5405(1992) [PubMed: 1644767] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5.
[2]"Complete sequence of Thermoanaerobacter pseudethanolicus 39E."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33223 / 39E.
[3]"Analysis of the catalytic center of cyclomaltodextrinase from Thermoanaerobacter ethanolicus 39E."
Podkovyrov S.M., Burdette D., Zeikus J.G.
FEBS Lett. 317:259-262(1993) [PubMed: 8425614] [Abstract]
Cited for: ACTIVE SITES, MUTANTS ASP-325-ASN; GLU-354-GLN AND ASP-421-ASN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M88602 Genomic DNA. Translation: AAA23219.1.
CP000924 Genomic DNA. Translation: ABY94339.1.
RefSeqYP_001664675.1. NC_010321.1.

3D structure databases

ProteinModelPortalP29964.
ModBaseSearch...

Protein-protein interaction databases

STRINGP29964.

Protein family/group databases

CAZyCBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5873880.
GenomeReviewsGene locus Teth39_0676 in contig CP000924_GR.
KEGGtpd:Teth39_0676.
PATRIC23885970. VBIThePse6203_0709.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG726713.
OMAETVWYQI.
ProtClustDBCLSK901433.

Enzyme and pathway databases

BioCycTPSE340099:TETH39_0676-MONOMER.

Family and domain databases

InterProIPR015902. Alpha_amylase.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004185. Glyco_hydro_13_lg-like_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCDAS_THEP3
AccessionPrimary (citable) accession number: P29964
Secondary accession number(s): B0K7U0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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