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Reviewed, UniProtKB/Swiss-Prot P09121 (CDGT_BACS3)

Last modified June 16, 2009. Version 80. 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 38-2)
Taxonomic identifier1412 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length712 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 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 – 2727 Ref.1
Chain28 – 712685Cyclomaltodextrin glucanotransferase
PRO_0000001439

Regions

Domain526 – 60681IPT/TIG
Domain607 – 712106CBM20
Region28 – 165138A1
Region166 – 22964B
Region230 – 433204A2
Region434 – 52289C
Region523 – 60886D
Region609 – 712104E

Sites

Active site2561Nucleophile By similarity
Active site2841Proton donor By similarity
Active site3551 By similarity
Metal binding541Calcium 2 By similarity
Metal binding561Calcium 2; via carbonyl oxygen By similarity
Metal binding591Calcium 2 By similarity
Metal binding601Calcium 2 By similarity
Metal binding781Calcium 2; via carbonyl oxygen By similarity
Metal binding801Calcium 2 By similarity
Metal binding1661Calcium 1 By similarity
Metal binding2171Calcium 1; via carbonyl oxygen By similarity
Metal binding2261Calcium 1 By similarity
Metal binding2601Calcium 1; via carbonyl oxygen By similarity

Amino acid modifications

Disulfide bond70 ↔ 77 By similarity

Experimental info

Sequence conflict582 – 5865VPGGI → SWRHL Ref.2

Sequences

Sequence LengthMass (Da)Tools
P09121-1 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: 4FAA8F70BEF818F9

FASTA71278,249
        10         20         30         40         50         60 
MKRFMKLTAV WTLWLSLTLG LLSPVHAAPD TSVSNKQNFS TDVIYQIFTD RFSDGNPANN 

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

       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 STINNYKPVF NFGEWFLGVN EISPEYHQFA 

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

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

       430        440        450        460        470        480 
LAPLRKSNPA IAYGSTQERW INNDVIIYER KFGNNVAVVA INRNMNTPAS ITGLVTSLPQ 

       490        500        510        520        530        540 
GSYNDVLGGI LNGNTLTVGA GGAASNFTLA PGGTAVWQYT TDATAPINGN VGPMMAKAGV 

       550        560        570        580        590        600 
TITIDGRASA RQGTVYFGTT AVTGADIVAW EDTQIQVKIL RVPGGIYDIR VANAAGAASN 

       610        620        630        640        650        660 
IYDNFEVLTG DQVTVRFVIN NATTALGQNV FLTGNVSELG NWDPNNAIGP MYNQVVYQYP 

       670        680        690        700        710 
TWYYDVSVPA GQTIEFKFLK KQGSTVTWEG GANRTFTTPT SGTATVNVNW QP 

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References

[1]"Molecular cloning and nucleotide sequence of the cyclomaltodextrin glucanotransferase gene from the alkalophilic Bacillus sp. strain no. 38-2."
Kaneko T., Hamamoto T., Horikoshi K.
J. Gen. Microbiol. 134:97-105(1988) [PubMed: 2972812] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-44.
[2]"Nucleotide sequence of the cyclomaltodextrin glucanotransferase (CGTase) gene from alkalophilic Bacillus sp. strain No. 38-2."
Hamamoto T., Kaneko T., Horikoshi K.
Agric. Biol. Chem. 51:2019-2022(1987)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-586.

Cross-references

Sequence databases

M19880 Genomic DNA. Translation: AAA22309.1.
D00129 Genomic DNA. Translation: BAA00077.1.

3D structure databases

HSSPHSSP built from PDB template 1PAM based on UniProtKB P05618.
SMRP09121. Positions 28-712.
ModBaseSearch...

Protein family/group databases

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

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_BACS3
AccessionPrimary (citable) accession number: P09121
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1993
Last modified: June 16, 2009
This is version 80 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