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P05618 (CDGT_BACS0) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 sp. (strain 1011)
Taxonomic identifier1410 [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.

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.

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_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
Chain28 – 713686Cyclomaltodextrin glucanotransferase
PRO_0000001437

Regions

Domain526 – 60782IPT/TIG
Domain608 – 713106CBM20
Region28 – 165138A1
Region127 – 1282Substrate binding
Region166 – 22964B
Region220 – 2234Substrate binding
Region230 – 433204A2
Region259 – 2602Substrate binding By similarity
Region434 – 52289C
Region523 – 60987D
Region610 – 713104E

Sites

Active site2561Nucleophile
Active site2841Proton donor
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
Binding site1671Substrate By similarity
Binding site2541Substrate By similarity
Binding site3541Substrate By similarity
Binding site3981Substrate
Binding site4021Substrate
Site3551Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond70 ↔ 77

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P05618 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 524B259526B56C52

FASTA71378,340
        10         20         30         40         50         60 
MKRFMKLTAV WTLWLSLTLG LLSPVHAAPD TSVSNKQNFS TDVIYQIFTD RFSDGNPANN 

        70         80         90        100        110        120 
PTGAAFDGSC TNLRLYCGGD WQGIINKIND GYLTGMGITA IWISQPVENI YSVINYSGVN 

       130        140        150        160        170        180 
NTAYHGYWAR DFKKTNPAYG TMQDFKNLID TAHAHNIKVI IDFAPNHTSP ASSDDPSFAE 

       190        200        210        220        230        240 
NGRLYDNGNL LGGYTNDTQN LFHHYGGTDF STIENGIYKN LYDLADLNHN NSSVDVYLKD 

       250        260        270        280        290        300 
AIKMWLDLGV DGIRVDAVKH MPFGWQKSFM ATINNYKPVF TFGEWFLGVN EISPEYHQFA 

       310        320        330        340        350        360 
NESGMSLLDF RFAQKARQVF RDNTDNMYGL KAMLEGSEVD YAQVNDQVTF IDNHDMERFH 

       370        380        390        400        410        420 
TSNGDRRKLE QALAFTLTSR GVPAIYYGSE QYMSGGNDPD NRARLPSFST TTTAYQVIQK 

       430        440        450        460        470        480 
LAPLRKSNPA IAYGSTHERW INNDVIIYER KFGNNVAVVA INRNMNTPAS ITGLVTSLRR 

       490        500        510        520        530        540 
ASYNDVLGGI LNGNTLTVGA GGAASNFTLA PGGTAVWQYT TDATTPIIGN VGPMMAKPGV 

       550        560        570        580        590        600 
TITIDGRGFG SGKGTVYFGT TAVTGADIVA WEDTQIQVKI PAVPGGIYDI RVANAAGAAS 

       610        620        630        640        650        660 
NIYDNFEVLT GDQVTVRFVI NNATTALGQN VFLTGNVSEL GNWDPNNAIG PMYNQVVYQY 

       670        680        690        700        710 
PTWYYDVSVP AGQTIEFKFL KKQGSTVTWE GGANRTFTTP TSGTATVNVN WQP

« Hide

References

[1]"Nucleotide sequence of the beta-cyclodextrin glucanotransferase gene of alkalophilic Bacillus sp. strain 1011 and similarity of its amino acid sequence to those of alpha-amylases."
Kimura K., Kataoka S., Ishii Y., Takano T., Yamane K.
J. Bacteriol. 169:4399-4402(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"X-ray structure of cyclodextrin glucanotransferase from alkalophilic Bacillus Sp. 1011. Comparison of two independent molecules at 1.8-A resolution."
Harata K., Haga K., Nakamura A., Aoyagi M., Yamane K.
Acta Crystallogr. D 52:1136-1145(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-713.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M17366 Genomic DNA. Translation: AAA22308.1.
PIRALBSG1. A26678.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D7FX-ray1.90A/B28-713[»]
1DEDX-ray2.00A/B28-713[»]
1I75X-ray2.00A/B28-713[»]
1PAMX-ray1.80A/B28-713[»]
1UKQX-ray2.00A/B28-713[»]
1UKSX-ray1.90A/B28-713[»]
1UKTX-ray2.20A/B28-713[»]
1V3JX-ray2.00A/B28-713[»]
1V3KX-ray2.00A/B28-713[»]
1V3LX-ray2.10A/B28-713[»]
1V3MX-ray2.00A/B28-713[»]
ProteinModelPortalP05618.
SMRP05618. 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. 691.

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

EvolutionaryTraceP05618.

Entry information

Entry nameCDGT_BACS0
AccessionPrimary (citable) accession number: P05618
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: April 3, 2013
This is version 109 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

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