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Reviewed, UniProtKB/Swiss-Prot P30920 (CDGT1_BACCI)

Last modified November 25, 2008. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cyclomaltodextrin glucanotransferase
    EC=2.4.1.19
Alternative name(s):
    Cyclodextrin-glycosyltransferase
      Short name=CGTase
OrganismBacillus circulans
Taxonomic identifier1397 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length718 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond.

Cofactor

Binds 2 calcium ions per subunit.

Subunit structure

Monomer.

Subcellular location

SecretedBy similarity.

Domain

May consist of two protein domains: the one in the N-terminal side cleaves the alpha-1,4-glucosidic bond in starch, and the other in the C-terminal side catalyzes other activities, including the reconstitution of an alpha-1,4-glucosidic linkage for cyclizing the maltooligosaccharide produced.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Contains 1 CBM20 (carbohydrate binding type-20) domain.

Contains 1 IPT/TIG domain.

Ontologies

Keywords

   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   Technical term3D-structure

Gene Ontology (GO)

   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

cyclomaltodextrin glucanotransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434
Chain35 – 718684Cyclomaltodextrin glucanotransferase
PRO_0000001430

Regions

Domain532 – 61281IPT/TIG
Domain613 – 718106CBM20
Region35 – 172138A1
Region173 – 23664B
Region237 – 440204A2
Region441 – 52888C
Region529 – 61486D
Region615 – 718104E

Sites

Active site2631Nucleophile By similarity
Active site2911Proton donor By similarity
Active site3621 By similarity
Metal binding611Calcium 2
Metal binding631Calcium 2; via carbonyl oxygen
Metal binding661Calcium 2
Metal binding671Calcium 2
Metal binding851Calcium 2; via carbonyl oxygen
Metal binding871Calcium 2
Metal binding1731Calcium 1
Metal binding2241Calcium 1; via carbonyl oxygen
Metal binding2331Calcium 1
Metal binding2671Calcium 1; via carbonyl oxygen

Amino acid modifications

Disulfide bond77 ↔ 84

Secondary structure

.................................................................................................................................... 718
Helix Strand Turn

Details...