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Reviewed, UniProtKB/Swiss-Prot P31797 (CDGT_BACST)

Last modified June 16, 2009. Version 83. 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

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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 lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

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Protein attributes

Sequence length711 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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

Secreted By 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.

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Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.2
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

1 ................................................................................................................................... 711
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P31797-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 5F9F71FF01C2CC60

FASTA71178,923
        10         20         30         40         50         60 
MRRWLSLVLS MSFVFSAIFI VSDTQKVTVE AAGNLNKVNF TSDVVYQIVV DRFVDGNTSN 

        70         80         90        100        110        120 
NPSGALFSSG CTNLRKYCGG DWQGIINKIN DGYLTDMGVT AIWISQPVEN VFSVMNDASG 

       130        140        150        160        170        180 
SASYHGYWAR DFKKPNPFFG TLSDFQRLVD AAHAKGIKVI IDFAPNHTSP ASETNPSYME 

       190        200        210        220        230        240 
NGRLYDNGTL LGGYTNDANM YFHHNGGTTF SSLEDGIYRN LFDLADLNHQ NPVIDRYLKD 

       250        260        270        280        290        300 
AVKMWIDMGI DGIRMDAVKH MPFGWQKSLM DEIDNYRPVF TFGEWFLSEN EVDANNHYFA 

       310        320        330        340        350        360 
NESGMSLLDF RFGQKLRQVL RNNSDNWYGF NQMIQDTASA YDEVLDQVTF IDNHDMDRFM 

       370        380        390        400        410        420 
IDGGDPRKVD MALAVLLTSR GVPNIYYGTE QYMTGNGDPN NRKMMSSFNK NTRAYQVIQK 

       430        440        450        460        470        480 
LSSLRRNNPA LAYGDTEQRW INGDVYVYER QFGKDVVLVA VNRSSSSNYS ITGLFTALPA 

       490        500        510        520        530        540 
GTYTDQLGGL LDGNTIQVGS NGSVNAFDLG PGEVGVWAYS ATESTPIIGH VGPMMGQVGH 

       550        560        570        580        590        600 
QVTIDGEGFG TNTGTVKFGT TAANVVSWSN NQIVVAVPNV SPGKYNITVQ SSSGQTSAAY 

       610        620        630        640        650        660 
DNFEVLTNDQ VSVRFVVNNA TTNLGQNIYI VGNVYELGNW DTSKAIGPMF NQVVYSYPTW 

       670        680        690        700        710 
YIDVSVPEGK TIEFKFIKKD SQGNVTWESG SNHVYTTPTN TTGKIIVDWQ N

« Hide

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References

[1]"Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme."
Fujiwara S., Kakihara H., Woo K.B., Lejeune A., Kanemoto M., Sakaguchi K., Imanaka T.
Appl. Environ. Microbiol. 58:4016-4025(1992) [PubMed: 1476442] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NO. 2.
[2]"Polypeptide possessing cyclomaltodextrin glucanotransferase activity."
Sugimoto T., Kubota M., Sakai S.
Patent number GB2169902, 23-JUL-1986
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-41.
[3]Kubota M., Matsuura Y., Sakai S., Katsube Y.
Submitted (FEB-1993) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

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Cross-references

Sequence databases

X59042 Genomic DNA. Translation: CAA41770.1.
X59043 Genomic DNA. Translation: CAA41771.1.
X59044 Genomic DNA. Translation: CAA41772.1.
PIRALBSXF. S26588.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CYGX-ray2.50A32-711[»]
ModBaseSearch...

Protein family/group databases

CAZyCBM20. Carbohydrate-Binding Module Family 20.
GH13. Glycoside Hydrolase Family 13.

Family and domain databases

InterProIPR006048. A-amylase_b_C.
IPR006046. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat.
IPR006589. Glyco_hydro_13_sub_cat.
IPR002044. Glyco_hydro_carb-bd.
IPR013781. Glyco_hydro_sg_catalytic.
IPR013783. Ig-like_fold.
IPR002909. IPT_TIG_rcpt.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 2 hits.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
ProDomPD001568. Glyco_hydro_CBD. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
PROSITEPS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCDGT_BACST
AccessionPrimary (citable) accession number: P31797
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 16, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents