Skip Header

Contribute Send feedback
Read comments (?) or add your own

P30921 (CDGT_BAC11) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 sp. (strain 17-1)
Taxonomic identifier72572 [NCBI]
Taxonomic lineageBacteria › Firmicutes › 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 By similarity.

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 termDirect 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 functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

cyclomaltodextrin glucanotransferase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.1
Chain28 – 713686Cyclomaltodextrin glucanotransferase
PRO_0000001440

Regions

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

Sites

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

Amino acid modifications

Disulfide bond70 ↔ 77 By similarity

Sequences

Sequence LengthMass (Da)Tools
P30921 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: D13AEF6C507FF45E

FASTA71377,390
        10         20         30         40         50         60 
MKKISKLTTA LALSLSLALS LLGPAHAAPD TSVSNKQNFS TDVIYQIFTD RFSDGNPANN 

        70         80         90        100        110        120 
PTGPAFDGTC TNLRLYCGGD WQGIINKIND GYLTGMGVTA IWISQPVENI YSVINYSGVN 

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

       190        200        210        220        230        240 
NGKLYNNGRD EGGYTNDTHN LFHHNGGTDF STTENGIYKN LYDLADLNHN NSTVDTYLKD 

       250        260        270        280        290        300 
AIKMWLDLGI DGIRMDAVKH MPFGWQKSFM ATVNNYKPVF TFGEWFLGVN EVSAENHKFA 

       310        320        330        340        350        360 
NVSGMSLLDF RFAQKVRQVF KDNTDNMYGL KSMLEGSATD YAQMEDQVTF IDNHDMERFH 

       370        380        390        400        410        420 
NNSANRRKLE QALAFTLTSR GVPAIYYGTE QYMSGGNDPD NRARIPSFST TTTAYQVSKK 

       430        440        450        460        470        480 
LAPLRKSNPA IAYGTTQERW INNDVLIYER KFGNNVAVIA VNRNVNTSAS ITGLVTSLPA 

       490        500        510        520        530        540 
GSYTDVLGGL LNGNNLTVGS GGSASIFTLA AGGTAVWQYT TAVTAPTIGH VGPMMAKPGA 

       550        560        570        580        590        600 
AVTIDGRGFG ATKGTVYFGT TAVTGANITA WEDTQIKVKI PAVAGGVYNI KIANSAGTSS 

       610        620        630        640        650        660 
NVHDNFEVLS GDQVSVRFVV NNATTALGQN VYLAGSVSEL GNWDPAKAIG PLYNQVIYQY 

       670        680        690        700        710 
PTWYYDVTVP AGKTIEFKFL KKQGSTVTWE GGSNHTFTAP TSGTATINVN WQP

« Hide

References

[1]"Construction of a chimeric series of Bacillus cyclomaltodextrin glucanotransferases and analysis of the thermal stabilities and pH optima of the enzymes."
Kaneko T., Song K.B., Hamamoto T., Kudo T., Horikoshi K.
J. Gen. Microbiol. 135:3447-3457(1989) [PubMed: 2534600] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-44.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M28053 Genomic DNA. Translation: AAA22310.1.

3D structure databases

ProteinModelPortalP30921.
SMRP30921. 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

InterProIPR006048. A-amylase_b_C.
IPR015902. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
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.
PANTHERPTHR10357. Alpha_amylase. 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...

Entry information

Entry nameCDGT_BAC11
AccessionPrimary (citable) accession number: P30921
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: January 25, 2012
This is version 86 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

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