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Reviewed, UniProtKB/Swiss-Prot P31746 (CDGT_BACS2)

Last modified June 16, 2009. Version 70. 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

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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 sp. (strain 1-1)
Taxonomic identifier29334 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length703 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 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.

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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 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 – 2929 Ref.1
Chain30 – 703674Cyclomaltodextrin glucanotransferase
PRO_0000001438

Regions

Domain520 – 59879IPT/TIG
Domain599 – 703105CBM20
Region30 – 160131A1
Region161 – 22464B
Region225 – 428204A2
Region429 – 51688C
Region517 – 60084D
Region601 – 703103E

Sites

Active site2511Nucleophile By similarity
Active site2791Proton donor By similarity
Active site3501 By similarity
Metal binding521Calcium 2 By similarity
Metal binding541Calcium 2; via carbonyl oxygen 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

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Sequences

Sequence LengthMass (Da)Tools
P31746-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 4D973FB21D0D9B0A

FASTA70378,663
        10         20         30         40         50         60 
MNDLNDFLKT ILLSFIFFLL LSLPTVAEAD VTNKVNYSKD VIYQIVTDRF SDGNPGNNPS 

        70         80         90        100        110        120 
GAIFSQNCID LHKYCGGDWQ GIIDKINDGY LTDLGITALW ISQPVENVYA LHPSGYTSYH 

       130        140        150        160        170        180 
GYWARDYKKT NPYYGNFDDF DRLMSTAHSN GIKVIMDFTP NHSSPALETN PNYVENGAIY 

       190        200        210        220        230        240 
DNGALLGNYS NDQQNLFHHN GGTDFSSYED SIYRNLYDLA DYDLNNTVMD QYLKESIKFW 

       250        260        270        280        290        300 
LDKGIDGIRV DAVKHMSEGW QTSLMSEIYS HKPVFTFGEW FLGSGEVDPQ NHHFANESGM 

       310        320        330        340        350        360 
SLLDFQFGQT IRNVLKDRTS NWYDFNEMIT STEKEYNEVI DQVTFIDNHD MSRFSVGSSS 

       370        380        390        400        410        420 
NRQTDMALAV LLTSRGVPTI YYGTEQYVTG GNDPENRKPL KTFDRSTNSY QIISKLASLR 

       430        440        450        460        470        480 
QTNSALGYGT TTERWLNEDI YIYERTFGNS IVLTAVNSSN SNQTITNLNT SLPQGNYTDE 

       490        500        510        520        530        540 
LQQRLDGNTI TVNANGAVNS FQLRANSVAV WQVSNPSTSP LIGQVGPMMG KAGNTITVSG 

       550        560        570        580        590        600 
EGFGDERGSV LFDSTSSEII SWSNTKISVK VPNVAGGYYD LSVVTAANIK SPTYKEFEVL 

       610        620        630        640        650        660 
SGNQVSVRFG VNNATTSPGT NLYIVGNVNE LGNWDADKAI GPMFNQVMYQ YPTWYYDISV 

       670        680        690        700 
PAGKNLEYKY IKKDQNGNVV WQSGNNRTYT SPTTGTDTVM INW

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References

[1]"Cloning and nucleotide sequence of a cyclodextrin glycosyltransferase gene from the alkalophilic Bacillus 1-1."
Schmid G., Englbrecht A., Schmid D.
(In) Huber O., Szejtli J. (eds.); Proceedings of the fourth international symposium on cyclodextrins, pp.71-76, Kluwer Academic Publishers, Dordrecht and Boston (1988)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-52.

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Cross-references

Sequence databases

PIRALBSX1. S26399.

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. 1000.

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 nameCDGT_BACS2
AccessionPrimary (citable) accession number: P31746
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 16, 2009
This is version 70 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

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