Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P27036 (CDGT_BACOH)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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 ohbensis
Taxonomic identifier1481 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length704 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929
Chain30 – 704675Cyclomaltodextrin glucanotransferase
PRO_0000001436

Regions

Domain520 – 59879IPT/TIG
Domain599 – 704106CBM20

Sites

Active site2511 By similarity
Active site2791 By similarity
Active site3501 By similarity
Metal binding521Calcium 2 By similarity
Metal binding571Calcium 2 By similarity
Metal binding581Calcium 2 By similarity
Metal binding761Calcium 2; via carbonyl oxygen By similarity
Metal binding781Calcium 2 By similarity
Metal binding1611Calcium 1 By similarity
Metal binding2121Calcium 1; via carbonyl oxygen By similarity
Metal binding2211Calcium 1 By similarity
Metal binding2551Calcium 1; via carbonyl oxygen By similarity

Amino acid modifications

Disulfide bond68 ↔ 75 By similarity

Sequences

Sequence LengthMass (Da)Tools
P27036-1 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 04FA14951D5ACECB

FASTA70478,621
        10         20         30         40         50         60 
MKNLTVLLKT IPLALLLFIL LSLPTAAQAD VTNKVNYTRD VIYQIVTDRF SDGDPSNNPT 

        70         80         90        100        110        120 
GAIYSQDCSD LHKYCGGDWQ GIIDKINDGY LTDLGITAIW ISQPVENVYA LHPSGYTSYH 

       130        140        150        160        170        180 
GYWARDYKRT NPFYGDFSDF DRLMDTAHSN GIKVIMDFTP NHSSPALETD PSYAENGAVY 

       190        200        210        220        230        240 
NDGVLIGNYS NDPNNLFHHN GGTDFSSYED SIYRNLYDLA DYDLNNTVMD QYLKESIKLW 

       250        260        270        280        290        300 
LDKGIDGIRV DAVKHMSEGW QTSLMSDIYA HEPVFTFGEW FLGSGEVDPQ NHHFANESGM 

       310        320        330        340        350        360 
SLLDFQFGQT IRDVLMDGSS NWYDFNEMIA STEEDYDEVI DQVTFIDNHD MSRFSFEQSS 

       370        380        390        400        410        420 
NRHTDIALAV LLTSRGVPTI YYGTEQYLTG GNDPENRKPM SDFDRTTNSY QIISTLASLR 

       430        440        450        460        470        480 
QNNPALGYGN TSERWINSDV YIYERSFGDS VVLTAVNSGD TSYTINNLNT SLPQGQYTDE 

       490        500        510        520        530        540 
LQQLLDGNEI TVNSNGAVDS FQLSANGVSV WQITEEHASP LIGHVGPMMG KHGNTVTITG 

       550        560        570        580        590        600 
EGFGDNEGSV LFDSDFSDVL SWSDTKIEVS VPDVTAGHYD ISVVNAGDSQ SPTYDKFEVL 

       610        620        630        640        650        660 
TGDQVSIRFA VNNATTSLGT NLYMVGNVNE LGNWDPDQAI GPMFNQVMYQ YPTWYYDISV 

       670        680        690        700 
PAEENLEYKF IKKDSSGNVV WESGNNHTYT TPATGTDTVL VDWQ 

« Hide

References

[1]"Cloning and sequencing of a cyclodextrin glucanotransferase gene from Bacillus ohbensis and its expression in Escherichia coli."
Sin K.A., Nakamura A., Kobayashi K., Masaki H., Uozumi T.
Appl. Microbiol. Biotechnol. 35:600-605(1991) [PubMed: 1368710] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

D90243 Genomic DNA. Translation: BAA14289.2.
PIRI39805.

3D structure databases

HSSPHSSP built from PDB template 1CYG based on UniProtKB P31797.
ModBaseSearch...

Protein family/group databases

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

Enzyme and pathway databases

BRENDA2.4.1.19. 264714.

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...

Entry information

Entry nameCDGT_BACOH
AccessionPrimary (citable) accession number: P27036
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

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