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Reviewed, UniProtKB/Swiss-Prot P43379 (CDGT2_BACCI)

Last modified June 16, 2009. Version 81. 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 circulans
Taxonomic identifier1397 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length713 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 – 2727 Ref.1
Chain28 – 713686Cyclomaltodextrin glucanotransferase
PRO_0000001431

Regions

Domain526 – 60782IPT/TIG
Domain608 – 713106CBM20
Region28 – 165138A1
Region166 – 22964B
Region230 – 433204A2
Region434 – 52289C
Region523 – 60987D
Region610 – 713104E

Sites

Active site2561Nucleophile
Active site2841Proton donor
Active site3551
Metal binding541Calcium 1
Metal binding561Calcium 1; via carbonyl oxygen
Metal binding591Calcium 1
Metal binding601Calcium 1
Metal binding801Calcium 1
Metal binding1661Calcium 2
Metal binding2171Calcium 2; via carbonyl oxygen
Metal binding2261Calcium 2
Metal binding2601Calcium 2; via carbonyl oxygen

Amino acid modifications

Disulfide bond70 ↔ 77

Secondary structure

1 ......................................................................................................................................... 713
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P43379-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 8ABBFB2C633A004B

FASTA71377,309
        10         20         30         40         50         60 
MKKFLKSTAA LALGLSLTFG LFSPAQAAPD TSVSNKQNFS TDVIYQIFTD RFSDGNPANN 

        70         80         90        100        110        120 
PTGAAFDGTC TNLRLYCGGD WQGIINKIND GYLTGMGVTA IWISQPVENI YSIINYSGVN 

       130        140        150        160        170        180 
NTAYHGYWAR DFKKTNPAYG TIADFQNLIA AAHAKNIKVI IDFAPNHTSP ASSDQPSFAE 

       190        200        210        220        230        240 
NGRLYDNGTL LGGYTNDTQN LFHHNGGTDF STTENGIYKN LYDLADLNHN NSTVDVYLKD 

       250        260        270        280        290        300 
AIKMWLDLGI DGIRMDAVKH MPFGWQKSFM AAVNNYKPVF TFGEWFLGVN EVSPENHKFA 

       310        320        330        340        350        360 
NESGMSLLDF RFAQKVRQVF RDNTDNMYGL KAMLEGSAAD YAQVDDQVTF IDNHDMERFH 

       370        380        390        400        410        420 
ASNANRRKLE QALAFTLTSR GVPAIYYGTE QYMSGGTDPD NRARIPSFST STTAYQVIQK 

       430        440        450        460        470        480 
LAPLRKCNPA IAYGSTQERW INNDVLIYER KFGSNVAVVA VNRNLNAPAS ISGLVTSLPQ 

       490        500        510        520        530        540 
GSYNDVLGGL LNGNTLSVGS GGAASNFTLA AGGTAVWQYT AATATPTIGH VGPMMAKPGV 

       550        560        570        580        590        600 
TITIDGRGFG SSKGTVYFGT TAVSGADITS WEDTQIKVKI PAVAGGNYNI KVANAAGTAS 

       610        620        630        640        650        660 
NVYDNFEVLS GDQVSVRFVV NNATTALGQN VYLTGSVSEL GNWDPAKAIG PMYNQVVYQY 

       670        680        690        700        710 
PNWYYDVSVP AGKTIEFKFL KKQGSTVTWE GGSNHTFTAP SSGTATINVN WQP

« Hide

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References

[1]"Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form."
Lawson C.L., van Montfort R., Strokopytov B., Rozeboom H.J., Kalk K.H., de Vries G.E., Penninga D., Dijkhuizen L., Dijkstra B.W.
J. Mol. Biol. 236:590-600(1994) [PubMed: 8107143] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-37, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Strain: 251.
[2]"Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products."
Knegtel R.M.A., Strokopytov B., Penninga D., Faber O.G., Rozeboom H.J., Kalk K.H., Dijkhuizen L., Dijkstra B.W.
J. Biol. Chem. 270:29256-29264(1995) [PubMed: 7493956] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Strain: 251.
[3]"The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251."
Penninga D., van der Veen B.A., Knegtel R.M.A., van Hijum S.A.F.T., Rozeboom H.J., Kalk K.H., Dijkstra B.W., Dijkhuizen L.
J. Biol. Chem. 271:32777-32784(1996) [PubMed: 8955113] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[4]"Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6-A resolution. Implications for product specificity."
Strokopytov B., Knegtel R.M.A., Penninga D., Rozeboom H.J., Kalk K.H., Dijkhuizen L., Dijkstra B.W.
Biochemistry 35:4241-4249(1996) [PubMed: 8672460] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
Strain: 251.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X78145 Genomic DNA. Translation: CAA55023.1.
PIRA58800.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CDGX-ray2.00A28-713[»]
1CGVX-ray2.50A28-713[»]
1CGWX-ray2.50A28-713[»]
1CGXX-ray2.50A28-713[»]
1CGYX-ray2.50A28-713[»]
1CXEX-ray2.10A28-713[»]
1CXFX-ray2.10A28-713[»]
1CXHX-ray2.41A28-713[»]
1CXIX-ray2.20A28-713[»]
1CXKX-ray2.09A28-713[»]
1CXLX-ray1.81A28-713[»]
1D3CX-ray1.78A28-713[»]
1DTUX-ray2.40A28-713[»]
1EO5X-ray2.00A28-713[»]
1EO7X-ray2.48A28-713[»]
1KCKX-ray2.43A28-713[»]
1KCLX-ray1.94A28-713[»]
1OT1X-ray2.00A28-713[»]
1OT2X-ray2.10A28-713[»]
1PEZX-ray2.32A28-713[»]
1PJ9X-ray2.00A28-713[»]
1TCMX-ray2.20A/B28-713[»]
2CXGX-ray2.50A28-713[»]
2DIJX-ray2.60A28-713[»]
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.
[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.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCDGT2_BACCI
AccessionPrimary (citable) accession number: P43379
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 81 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