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P94286 (CTA1_BACCI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:
Cycloisomaltooligosaccharide glucanotransferase

Short name=CITase
EC=2.4.1.248
OrganismBacillus circulans
Taxonomic identifier1397 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length972 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Produces cycloisomaltooligosaccharide from dextran containing 7, 8 or 9 glucose units. The enzyme is specific for (1->6)-alpha-D-glucans (dextrans) and, without activity toward (1->4)-alpha-D-glucans, such as amylose. It also has no activity on oligosaccharides, such as amylopectin and pullulan, containing (1->6)-alpha-D-glucosidic linkages at branch points. Ref.2

Catalytic activity

Cyclizes part of a (1->6)-alpha-D-glucan chain by formation of a (1->6)-alpha-D-glucosidic bond. Ref.2

Subunit structure

Monomer. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 66 family.

Contains 2 CBM6 (carbohydrate binding type-6) domains.

Biophysicochemical properties

Kinetic parameters:

KM=0.063 mM for dextran T-40 Ref.4

Vmax=0.872 pmol/min/µg enzyme with dextran T-40 as substrate

pH dependence:

Optimum pH is 5.5.

Ontologies

Keywords
   DomainRepeat
Signal
   Molecular functionGlycosyltransferase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

transferase activity, transferring glycosyl groups

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3838 Potential
Chain39 – 972934Cycloisomaltooligosaccharide glucanotransferase
PRO_0000012241

Regions

Domain421 – 546126CBM6 1
Domain748 – 871124CBM6 2

Experimental info

Mutagenesis1831D → N: Has 1% of wild-type activity. Ref.4
Mutagenesis3081D → N: No activity. Ref.4

Secondary structure

........................................................................................................................................... 972
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P94286 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 2827BEA61782CC22

FASTA972107,431
        10         20         30         40         50         60 
MVRFMYALRK RRLSLLLAMS LLVMCVASVV SPPPQALASG SGGIERVFTD KARYNPGDAV 

        70         80         90        100        110        120 
SIRVQAKNGT GSSWSGAARL EIFHLENSVY TSSQSLSLTN GQSTTLTFTW TAPSTDFRGY 

       130        140        150        160        170        180 
FVRIDAGTLG QGATAIDVSS DFTKYPRYGY ISEFESGETA LESKAKVDQL AQDYHINAWQ 

       190        200        210        220        230        240 
FYDWMWRHDK MIKRTGGSID STWLDLFNRE ISWSTLQNQI DAVHDVNGKA MAYAMIYASR 

       250        260        270        280        290        300 
ENYSPLGISP TWGIYEDSSH TNQFDVDFGD GSTYLYMSDP QNPNWQNYIH AEYIDSINTA 

       310        320        330        340        350        360 
GFDGIHVDQM GQRSNVYDYN GNSIDLSTRF SPFLDQAKSV LSANNPARDN LTYNIVDGTV 

       370        380        390        400        410        420 
NGWAVNDVSK NADLDFLYSE IWYLSDSYNQ LKNYIEQLRA NGGNKAVVLA AYMNYADNAG 

       430        440        450        460        470        480 
TRYEAESASM TNVSTNTNHA GYTGSGFVDQ FASTGDKVSF AINAPEAGDY SLVFRYGNNT 

       490        500        510        520        530        540 
GANSTLNLYV DGNFVQKLYF FNQSSWGTWK HDAWYQVPLT QGAHTVELRY ESGNVGAVNL 

       550        560        570        580        590        600 
DSLTLGTFDE HSVRLADAMM SASGATHIEL GDDNQMLPHE YYPNRSKTMR SSLKNAMKDH 

       610        620        630        640        650        660 
YNFITAYENL LFDSDVVPND TGSQFVNLTG VSASGDGSAN TVWYINKRTS DYNIVHLINL 

       670        680        690        700        710        720 
LGNDNQWRNT ASQPSFQTNL PAKIYIGADE TISDVYLASP DLSGGETQEL AFTSGTDAGG 

       730        740        750        760        770        780 
KYVSFTVPEL KYWNMIYMKR TFSVPANDIY EAETAIKSNV STNTNHAGYT GSGFVDGFSS 

       790        800        810        820        830        840 
TNDGVSFVVK STASDDYALR FRYANGGSDA TRDVYVDGKL AGTVSFKSTG SWSTWSYGEI 

       850        860        870        880        890        900 
TARLEPGHHT IVLWQTSGNT GAINLDHLDL DKTYIWQFDR QIVSVPAGYR ITFRTGLPGW 

       910        920        930        940        950        960 
VHWGVNGWTG VTDTPLRSNG SLDGNLDHET SIGPFATGTA VDVTFLWDDN NNGILEPSTD 

       970 
RWEGTDFGIN VS 

« Hide

References

[1]"Cloning and sequence analysis of the cycloisomaltooligosaccharide glucanotransferase gene from Bacillus circulans T-3040 and expression in Escherichia coli cells."
Oguma T., Kurokawa T., Tobe K., Kobayashi M.
J. Appl. Glycosci. 42:415-419(1995)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: T-3040.
[2]"Purification and properties of a novel enzyme from Bacillus spp. T-3040, which catalyzes the conversion of dextran to cyclic isomaltooligosaccharides."
Oguma T., Tobe K., Kobayashi M.
FEBS Lett. 345:135-138(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PH DEPENDENCE.
Strain: T-3040.
[3]Erratum
Oguma T., Tobe K., Kobayashi M.
FEBS Lett. 349:442-442(1994)
[4]"Identification of catalytic amino acids of cyclodextran glucanotransferase from Bacillus circulans T-3040."
Yamamoto T., Terasawa K., Kim Y.M., Kimura A., Kitamura Y., Kobayashi M., Funane K.
Biosci. Biotechnol. Biochem. 70:1947-1953(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-183 AND ASP-308, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: T-3040.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D61382 Genomic DNA. Translation: BAA09604.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3WNKX-ray2.30A39-738[»]
3WNLX-ray2.60A39-738[»]
3WNMX-ray2.25A39-738[»]
3WNNX-ray2.25A/B39-738[»]
3WNOX-ray1.90A/B39-738[»]
3WNPX-ray2.80A/B39-738[»]
ProteinModelPortalP94286.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM35. Carbohydrate-Binding Module Family 35.
GH66. Glycoside Hydrolase Family 66.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.260. 2 hits.
InterProIPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR025092. Glyco_hydro_66.
[Graphical view]
PfamPF03422. CBM_6. 2 hits.
PF13199. Glyco_hydro_66. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 2 hits.
PROSITEPS51175. CBM6. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCTA1_BACCI
AccessionPrimary (citable) accession number: P94286
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: May 14, 2014
This is version 58 of the entry and version 1 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