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P43379 (CDGT2_BACCI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 › Bacilli › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length713 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. Ref.3

Cofactor

Binds 3 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.

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_functioncyclomaltodextrin glucanotransferase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

starch binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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
Region127 – 1282Substrate binding
Region166 – 22964B
Region172 – 1743Substrate binding
Region220 – 2234Substrate binding
Region230 – 433204A2
Region259 – 2602Substrate binding
Region434 – 52289C
Region523 – 60987D
Region610 – 713104E

Sites

Active site2561Nucleophile Ref.3 Ref.6
Active site2841Proton donor Ref.3 Ref.6
Metal binding541Calcium 1
Metal binding561Calcium 1; via carbonyl oxygen
Metal binding591Calcium 1
Metal binding601Calcium 1
Metal binding781Calcium 1; via carbonyl oxygen
Metal binding801Calcium 1
Metal binding1661Calcium 2
Metal binding2171Calcium 2; via carbonyl oxygen
Metal binding2261Calcium 2
Metal binding2601Calcium 2; via carbonyl oxygen
Metal binding3421Calcium 3; via carbonyl oxygen
Metal binding6041Calcium 3
Binding site1671Substrate
Binding site2541Substrate
Binding site3541Substrate
Binding site3981Substrate
Binding site4021Substrate
Site3551Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond70 ↔ 77 Ref.6

Experimental info

Mutagenesis2561D → N: Reduces activity 23000-fold. Reduces activity 520000-fold; when associated with N-355. Ref.3
Mutagenesis2841E → Q: Reduces activity 4100-fold. Ref.3
Mutagenesis3551D → N: Reduces activity 56000-fold. Reduces activity 520000-fold; when associated with N-256. Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P43379 [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

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-37, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Strain: 251.
[2]"X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases."
Strokopytov B., Penninga D., Rozeboom H.J., Kalk K.H., Dijkhuizen L., Dijkstra B.W.
Biochemistry 34:2234-2240(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 28-713 IN COMPLEX WITH ACARBOSE.
[3]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ASN-256/GLN-284, ACTIVE SITE, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-256; GLU-284 AND ASP-355.
Strain: 251.
[4]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
Strain: 251.
[6]"X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family."
Uitdehaag J.C., Mosi R., Kalk K.H., van der Veen B.A., Dijkhuizen L., Withers S.G., Dijkstra B.W.
Nat. Struct. Biol. 6:432-436(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 28-713 OF MUTANT ASN-256/GLN-284 IN COMPLEXES WITH CALCIUM IONS AND MALTOTETRAOSE, ACTIVE SITE, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X78145 Genomic DNA. Translation: CAA55023.1.
PIRA58800.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP43379.
SMRP43379. Positions 28-713.
ModBaseSearch...

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.4.1.19. 649.
SABIO-RKP43379.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT_TIG_rcpt.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMSSF49452. CBD_4. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 1 hit.
PROSITEPS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP43379.

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: April 3, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents