Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P26827 (CDGT_THETU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
Cyclomaltodextrin glucanotransferase

EC=2.4.1.19
Alternative name(s):
Cyclodextrin-glycosyltransferase
Short name=CGTase
Gene names
Name:amyA
OrganismThermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes)
Taxonomic identifier33950 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisThermoanaerobacterium

Protein attributes

Sequence length710 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degrades starch to alpha-, beta-, and gamma-cyclodextrins, as well as linear sugars.

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.

Subcellular location

Secreted Ref.1.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Contains 1 CBM20 (carbohydrate binding type-20) domain.

Contains 1 IPT/TIG domain.

Caution

Was originally (Ref.1) thought to be an alpha-amylase.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   Technical term3D-structure
Direct 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_functioncyclomaltodextrin glucanotransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

starch binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.1
Chain28 – 710683Cyclomaltodextrin glucanotransferase
PRO_0000001444

Regions

Domain526 – 60378IPT/TIG
Domain605 – 710106CBM20
Region128 – 1292Substrate binding
Region221 – 2244Substrate binding By similarity
Region260 – 2612Substrate binding

Sites

Active site2571Nucleophile Ref.5
Active site2851Proton donor Ref.5
Metal binding541Calcium 1
Metal binding561Calcium 1; via carbonyl oxygen
Metal binding591Calcium 1
Metal binding601Calcium 1
Metal binding781Calcium 1; via carbonyl oxygen
Metal binding801Calcium 1
Metal binding1671Calcium 2
Metal binding2181Calcium 2; via carbonyl oxygen
Metal binding2271Calcium 2
Metal binding2611Calcium 2; via carbonyl oxygen
Binding site1681Substrate By similarity
Binding site2551Substrate By similarity
Binding site3551Substrate By similarity
Binding site3981Substrate
Binding site4021Substrate
Site3561Transition state stabilizer By similarity

Experimental info

Sequence conflict1281Missing no nucleotide entry Ref.3
Sequence conflict133 – 1386FKRTNP → LREQS no nucleotide entry Ref.3
Sequence conflict390 – 3989EQYMTGNGD → VYDRQWR AA sequence Ref.1

Secondary structure

....................................................................................................................................... 710
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26827 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: F5260AE60D3F27D2

FASTA71078,417
        10         20         30         40         50         60 
MKKTFKLILV LMLSLTLVFG LTAPIQAASD TAVSNVVNYS TDVIYQIVTD RFVDGNTSNN 

        70         80         90        100        110        120 
PTGDLYDPTH TSLKKYFGGD WQGIINKIND GYLTGMGVTA IWISQPVENI YAVLPDSTFG 

       130        140        150        160        170        180 
GSTSYHGYWA RDFKRTNPYF GSFTDFQNLI NTAHAHNIKV IIDFAPNHTS PASETDPTYA 

       190        200        210        220        230        240 
ENGRLYDNGT LLGGYTNDTN GYFHHYGGTD FSSYEDGIYR NLFDLADLNQ QNSTIDSYLK 

       250        260        270        280        290        300 
SAIKVWLDMG IDGIRLDAVK HMPFGWQKNF MDSILSYRPV FTFGEWFLGT NEIDVNNTYF 

       310        320        330        340        350        360 
ANESGMSLLD FRFSQKVRQV FRDNTDTMYG LDSMIQSTAS DYNFINDMVT FIDNHDMDRF 

       370        380        390        400        410        420 
YNGGSTRPVE QALAFTLTSR GVPAIYYGTE QYMTGNGDPY NRAMMTSFNT STTAYNVIKK 

       430        440        450        460        470        480 
LAPLRKSNPA IAYGTTQQRW INNDVYIYER KFGNNVALVA INRNLSTSYN ITGLYTALPA 

       490        500        510        520        530        540 
GTYTDVLGGL LNGNSISVAS DGSVTPFTLS AGEVAVWQYV SSSNSPLIGH VGPTMTKAGQ 

       550        560        570        580        590        600 
TITIDGRGFG TTSGQVLFGS TAGTIVSWDD TEVKVKVPSV TPGKYNISLK TSSGATSNTY 

       610        620        630        640        650        660 
NNINILTGNQ ICVRFVVNNA STVYGENVYL TGNVAELGNW DTSKAIGPMF NQVVYQYPTW 

       670        680        690        700        710 
YYDVSVPAGT TIQFKFIKKN GNTITWEGGS NHTYTVPSSS TGTVIVNWQQ 

« Hide

References

[1]"Alpha-amylase of Clostridium thermosulfurogenes EM1: nucleotide sequence of the gene, processing of the enzyme, and comparison of other alpha-amylases."
Bahl H., Burchhardt G., Spreinat A., Haeckel K., Wienecke A., Schmidt B., Antranikian G.
Appl. Environ. Microbiol. 57:1554-1559(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-48, SUBCELLULAR LOCATION.
Strain: DSM 3896 / EM1.
[2]Sahm K., Matuschek M., Mueller H., Mitchell W.J., Bahl H.
Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 3896 / EM1.
[3]"Nucleotide sequence of two Clostridium thermosulfurogenes EM1 genes homologous to Escherichia coli genes encoding integral membrane components of binding protein-dependent transport systems."
Bahl H., Burchhardt G., Wienecke A.
FEMS Microbiol. Lett. 65:83-87(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-255.
Strain: DSM 3896 / EM1.
[4]"Cyclodextrin formation by the thermostable alpha-amylase of Thermoanaerobacterium thermosulfurigenes EM1 and reclassification of the enzyme as a cyclodextrin glycosyltransferase."
Wind R.D., Liebl W., Buitelaar R.M., Penninga D., Spreinat A., Dijkhuizen L., Bahl H.
Appl. Environ. Microbiol. 61:1257-1265(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Crystal structure at 2.3 A resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermonanaerobacterium thermosulfurigenes EM1."
Knegtel R.M.A., Wind R.D., Rozeboom H.J., Kalk K.H., Buitelaar R.M., Dijkhuizen L., Dijkstra B.W.
J. Mol. Biol. 256:611-622(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 28-710.
[6]"Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1."
Wind R.D., Uitdehaag J.C., Buitelaar R.M., Dijkstra B.W., Dijkhuizen L.
J. Biol. Chem. 273:5771-5779(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 28-710 IN COMPLEX WITH MALTOHEPTAOSE AND CALCIUM IONS.
Strain: DSM 3896 / EM1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57692 Genomic DNA. Translation: AAB00845.1.
PIRS63598.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A47X-ray2.56A28-710[»]
1CIUX-ray2.30A28-710[»]
3BMVX-ray1.60A28-710[»]
3BMWX-ray1.60A28-710[»]
ProteinModelPortalP26827.
SMRP26827. Positions 28-710.
ModBaseSearch...
MobiDBSearch...

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. 6287.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 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. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26827.

Entry information

Entry nameCDGT_THETU
AccessionPrimary (citable) accession number: P26827
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1996
Last modified: January 22, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries