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Reviewed, UniProtKB/Swiss-Prot P30920 (CDGT1_BACCI)

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
OrganismBacillus circulans
Taxonomic identifier1397 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length718 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
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 – 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

1 .................................................................................................................................... 718
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P30920-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: E08CF0FE9C98BDA1

FASTA71878,047
        10         20         30         40         50         60 
MFQMAKRAFL STTLTLGLLA GSALPFLPAS AVYADPDTAV TNKQSFSTDV IYQVFTDRFL 

        70         80         90        100        110        120 
DGNPSNNPTG AAYDATCSNL KLYCGGDWQG LINKINDNYF SDLGVTALWI SQPVENIFAT 

       130        140        150        160        170        180 
INYSGVTNTA YHGYWARDFK KTNPYFGTMA DFQNLITTAH AKGIKIVIDF APNHTSPAME 

       190        200        210        220        230        240 
TDTSFAENGR LYDNGTLVGG YTNDTNGYFH HNGGSDFSSL ENGIYKNLYD LADFNHNNAT 

       250        260        270        280        290        300 
IDKYFKDAIK LWLDMGVDGI RVDAVKHMPL GWQKSWMSSI YAHKPVFTFG EWFLGSAASD 

       310        320        330        340        350        360 
ADNTDFANKS GMSLLDFRFN SAVRNVFRDN TSNMYALDSM INSTATDYNQ VNDQVTFIDN 

       370        380        390        400        410        420 
HDMDRFKTSA VNNRRLEQAL AFTLTSRGVP AIYYGTEQYL TGNGDPDNRA KMPSFSKSTT 

       430        440        450        460        470        480 
AFNVISKLAP LRKSNPAIAY GSTQQRWINN DVYVYERKFG KSVAVVAVNR NLSTSASITG 

       490        500        510        520        530        540 
LSTSLPTGSY TDVLGGVLNG NNITSTNGSI NNFTLAAGAT AVWQYTTAET TPTIGHVGPV 

       550        560        570        580        590        600 
MGKPGNVVTI DGRGFGSTKG TVYFGTTAVT GAAITSWEDT QIKVTIPSVA AGNYAVKVAA 

       610        620        630        640        650        660 
SGVNSNAYNN FTILTGDQVT VRFVVNNAST TLGQNLYLTG NVAELGNWST GSTAIGPAFN 

       670        680        690        700        710 
QVIHQYPTWY YDVSVPAGKQ LEFKFFKKNG STITWESGSN HTFTTPASGT ATVTVNWQ

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References

[1]"Molecular cloning, nucleotide sequence and expression in Escherichia coli of the beta-cyclodextrin glycosyltransferase gene from Bacillus circulans strain no. 8."
Nitschke L., Heeger K., Bender H., Schulz G.E.
Appl. Microbiol. Biotechnol. 33:542-546(1990) [PubMed: 1368573] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 8.
[2]"Structure of cyclodextrin glycosyltransferase refined at 2.0-A resolution."
Klein C., Schulz G.E.
J. Mol. Biol. 217:737-750(1991) [PubMed: 1826034] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Strain: 8.
[3]"Three-dimensional structure of cyclodextrin glycosyltransferase from Bacillus circulans at 3.4-A resolution."
Hofmann B.E., Bender H., Schulz G.E.
J. Mol. Biol. 209:793-800(1989) [PubMed: 2531228] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
Strain: 8.
[4]"Structure of cyclodextrin glycosyltransferase complexed with a derivative of its main product beta-cyclodextrin."
Schmidt A.K., Cottaz S., Driguez H., Schulz G.E.
Biochemistry 37:5909-5915(1998) [PubMed: 9558324] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Strain: 8.
[5]"Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the gamma-cyclodextrin production."
Parsiegla G., Schmidt A.K., Schulz G.E.
Eur. J. Biochem. 255:710-717(1998) [PubMed: 9738912] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Strain: 8.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X68326 Genomic DNA. Translation: CAA48401.1.
PIRALBSGC. S23674.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CGTX-ray2.00A35-718[»]
1CGUX-ray2.50A35-718[»]
3CGTX-ray2.40A35-718[»]
4CGTX-ray2.60A35-718[»]
5CGTX-ray2.50A35-718[»]
6CGTX-ray2.60A35-718[»]
7CGTX-ray3.00A35-718[»]
8CGTX-ray2.40A35-718[»]
9CGTX-ray2.50A35-718[»]
ModBaseSearch...

Protein family/group databases

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

Enzyme and pathway databases

BRENDA2.4.1.19. 1207.

Family and domain databases

InterProIPR006048. A-amylase_b_C.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
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.
IPR017909. Twin_arg_translocation_Tat.
[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. 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.
PS51318. TAT. 1 hit. Uncertain.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCDGT1_BACCI
AccessionPrimary (citable) accession number: P30920
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