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Reviewed, UniProtKB/Swiss-Prot P31747 (CDGT_BACSS)

Last modified June 16, 2009. Version 73. 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 sp. (strain 6.6.3)
Taxonomic identifier29335 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length718 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 – 3434 Potential
Chain35 – 718684Cyclomaltodextrin glucanotransferase
PRO_0000001441

Regions

Domain532 – 61281IPT/TIG
Domain613 – 718106CBM20
Region35 – 172138A1
Region173 – 23664B
Region237 – 440204A2
Region441 – 52888C
Region529 – 61486D
Region615 – 718104E

Sites

Active site2631Nucleophile By similarity
Active site2911Proton donor By similarity
Active site3621 By similarity
Metal binding611Calcium 2 By similarity
Metal binding631Calcium 2; via carbonyl oxygen By similarity
Metal binding661Calcium 2 By similarity
Metal binding671Calcium 2 By similarity
Metal binding851Calcium 2; via carbonyl oxygen By similarity
Metal binding871Calcium 2 By similarity
Metal binding1731Calcium 1 By similarity
Metal binding2241Calcium 1; via carbonyl oxygen By similarity
Metal binding2331Calcium 1 By similarity
Metal binding2671Calcium 1; via carbonyl oxygen By similarity

Amino acid modifications

Disulfide bond77 ↔ 84 By similarity

Sequences

Sequence LengthMass (Da)Tools
P31747-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 7644096D402707E5

FASTA71878,015
        10         20         30         40         50         60 
MFQMAKRAFL STTLTLGLLA GSALPFLPAS AAYADPDIAV TNKQSFSTDV IYQVFTDRFL 

        70         80         90        100        110        120 
DGNPSNNPTG AAYDATCSNL KLYCGGDWQG LINKINDNYF SDLGVTALWI SQPVENIFAT 

       130        140        150        160        170        180 
INYSGVTNTA YHGYWARDFK KTNPYFGTMA DFQNLITTAH AKGIKIIIDF APNHTSPAME 

       190        200        210        220        230        240 
TDTSFAENGK LYDNGTLVGG YTNDTNGYFH HNGGSDFSSL ENGIYKNLYD LADFNHNNAT 

       250        260        270        280        290        300 
IDKYFKDAIK LWLDMGVDGI RVDAVKHIAL GWQKSWMSSI YVHKPVFTFG EWFLGSAASD 

       310        320        330        340        350        360 
ADNTDFANKS GMSLLDFRFN SAVRNVFRDN TSNMYALDSM INSTATDYNQ VNDQVTFIDN 

       370        380        390        400        410        420 
HDMDRFKTSA VNNRRLEQAL AFTLTSRGVP AIYYGTEQYL TGNGDPDNRA KMPSFSKSTT 

       430        440        450        460        470        480 
AFNVISKLAP LRKSNPAIAY GSTQQRWINN DVYVYERKFG KSVAVVAVNR NLSTPANITG 

       490        500        510        520        530        540 
LSTSLPTGSY TDVLGGVLNG NNITSSNGSV NSFTLAAGAT AVWQYTAAET TPTIGHVGPV 

       550        560        570        580        590        600 
MGKPGNVVTI DGRGFGSTKG TVYFGTTAVT GAAITSWEDT QIKVTIPSVA AGNYAVKVAA 

       610        620        630        640        650        660 
NGVNSNAYNH FTILTGDQVT VRFVINNAST TLGQNIYLTG NVAELGNWST GSTAIGPAFN 

       670        680        690        700        710 
QVIHQYPTWY YDVSVPAGKE LEFKFFKKNG STITWEGGSN HKFTTPASGT ATVTVNWQ 

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References

[1]Akhmetzjanov A.A.
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

X66106 Genomic DNA. Translation: CAA46901.1.
PIRALBSG6. S21532.

3D structure databases

HSSPHSSP built from PDB template 1CGT based on UniProtKB P30920.
SMRP31747. Positions 36-718.
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.
IPR017909. Twin_arg_translocation_Tat.
[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.
PS51318. TAT. 1 hit. Uncertain.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDGT_BACSS
AccessionPrimary (citable) accession number: P31747
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 16, 2009
This is version 73 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)

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