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Reviewed, UniProtKB/Swiss-Prot P31797 (CDGT_BACST)

Last modified November 25, 2008. Version 80. 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
Gene names
Name: cgt
OrganismBacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length711 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131
Chain32 – 711680Cyclomaltodextrin glucanotransferase
PRO_0000001442

Regions

Domain526 – 60479IPT/TIG
Domain605 – 711107CBM20
Region32 – 165134A1
Region166 – 22964B
Region230 – 433204A2
Region434 – 52289C
Region523 – 60684D
Region607 – 711105E

Sites

Active site2561Nucleophile
Active site2841Proton donor
Active site3551
Metal binding551Calcium 2
Metal binding571Calcium 2; via carbonyl oxygen
Metal binding601Calcium 2
Metal binding611Calcium 2
Metal binding791Calcium 2; via carbonyl oxygen
Metal binding811Calcium 2
Metal binding1661Calcium 1
Metal binding2171Calcium 1; via carbonyl oxygen
Metal binding2261Calcium 1
Metal binding2601Calcium 1; via carbonyl oxygen

Amino acid modifications

Disulfide bond71 ↔ 78

Experimental info

Sequence conflict4601A → R AA sequence Ref.2

Secondary structure

................................................................................................................................... 711
Helix Strand Turn

Details...