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P94286

- CTA1_BACCI

UniProt

P94286 - CTA1_BACCI

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Protein

Cycloisomaltooligosaccharide glucanotransferase

Gene
N/A
Organism
Bacillus circulans
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=0.063 mM for dextran T-401 Publication

Vmax=0.872 pmol/min/µg enzyme with dextran T-40 as substrate1 Publication

pH dependencei

Optimum pH is 5.5.2 Publications

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. transferase activity, transferring glycosyl groups Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Protein family/group databases

CAZyiCBM35. Carbohydrate-Binding Module Family 35.
GH66. Glycoside Hydrolase Family 66.

Names & Taxonomyi

Protein namesi
Recommended name:
Cycloisomaltooligosaccharide glucanotransferase (EC:2.4.1.248)
Short name:
CITase
OrganismiBacillus circulans
Taxonomic identifieri1397 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi183 – 1831D → N: Has 1% of wild-type activity. 1 Publication
Mutagenesisi308 – 3081D → N: No activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3838Sequence AnalysisAdd
BLAST
Chaini39 – 972934Cycloisomaltooligosaccharide glucanotransferasePRO_0000012241Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
972
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 507Combined sources
Beta strandi52 – 543Combined sources
Beta strandi59 – 679Combined sources
Beta strandi70 – 723Combined sources
Beta strandi74 – 8411Combined sources
Beta strandi87 – 9812Combined sources
Beta strandi103 – 1119Combined sources
Beta strandi114 – 12512Combined sources
Helixi127 – 1293Combined sources
Beta strandi131 – 1388Combined sources
Helixi142 – 1443Combined sources
Beta strandi148 – 1514Combined sources
Helixi160 – 17415Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi201 – 2044Combined sources
Beta strandi210 – 2123Combined sources
Helixi213 – 22513Combined sources
Beta strandi229 – 24214Combined sources
Helixi244 – 2463Combined sources
Helixi250 – 2523Combined sources
Beta strandi253 – 2575Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi269 – 2724Combined sources
Beta strandi274 – 2785Combined sources
Helixi283 – 30018Combined sources
Beta strandi303 – 3086Combined sources
Beta strandi315 – 3184Combined sources
Helixi326 – 3283Combined sources
Helixi330 – 34415Combined sources
Helixi346 – 3483Combined sources
Beta strandi350 – 3578Combined sources
Helixi365 – 3717Combined sources
Beta strandi375 – 3806Combined sources
Beta strandi383 – 3853Combined sources
Helixi388 – 40114Combined sources
Beta strandi407 – 4104Combined sources
Turni413 – 4164Combined sources
Beta strandi420 – 4245Combined sources
Helixi425 – 4273Combined sources
Beta strandi428 – 4325Combined sources
Beta strandi434 – 4363Combined sources
Beta strandi439 – 4413Combined sources
Beta strandi447 – 4515Combined sources
Beta strandi457 – 47721Combined sources
Beta strandi480 – 4823Combined sources
Beta strandi484 – 4907Combined sources
Beta strandi493 – 5008Combined sources
Beta strandi504 – 5074Combined sources
Beta strandi509 – 51911Combined sources
Beta strandi521 – 5299Combined sources
Beta strandi538 – 54710Combined sources
Helixi550 – 56213Combined sources
Beta strandi566 – 5683Combined sources
Turni572 – 5743Combined sources
Beta strandi579 – 5813Combined sources
Beta strandi586 – 5883Combined sources
Helixi591 – 60616Combined sources
Helixi608 – 6125Combined sources
Beta strandi621 – 6233Combined sources
Beta strandi626 – 6283Combined sources
Beta strandi633 – 6364Combined sources
Beta strandi641 – 6488Combined sources
Beta strandi650 – 65910Combined sources
Beta strandi665 – 6695Combined sources
Beta strandi677 – 68610Combined sources
Beta strandi692 – 6987Combined sources
Helixi703 – 7053Combined sources
Beta strandi708 – 7103Combined sources
Beta strandi713 – 7175Combined sources
Beta strandi720 – 73819Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP94286.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini421 – 546126CBM6 1PROSITE-ProRule annotationAdd
BLAST
Domaini748 – 871124CBM6 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 66 family.Curated
Contains 2 CBM6 (carbohydrate binding type-6) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
InterProiIPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR025092. Glyco_hydro_66.
[Graphical view]
PfamiPF03422. CBM_6. 2 hits.
PF13199. Glyco_hydro_66. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
PROSITEiPS51175. CBM6. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P94286-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVRFMYALRK RRLSLLLAMS LLVMCVASVV SPPPQALASG SGGIERVFTD
60 70 80 90 100
KARYNPGDAV SIRVQAKNGT GSSWSGAARL EIFHLENSVY TSSQSLSLTN
110 120 130 140 150
GQSTTLTFTW TAPSTDFRGY FVRIDAGTLG QGATAIDVSS DFTKYPRYGY
160 170 180 190 200
ISEFESGETA LESKAKVDQL AQDYHINAWQ FYDWMWRHDK MIKRTGGSID
210 220 230 240 250
STWLDLFNRE ISWSTLQNQI DAVHDVNGKA MAYAMIYASR ENYSPLGISP
260 270 280 290 300
TWGIYEDSSH TNQFDVDFGD GSTYLYMSDP QNPNWQNYIH AEYIDSINTA
310 320 330 340 350
GFDGIHVDQM GQRSNVYDYN GNSIDLSTRF SPFLDQAKSV LSANNPARDN
360 370 380 390 400
LTYNIVDGTV NGWAVNDVSK NADLDFLYSE IWYLSDSYNQ LKNYIEQLRA
410 420 430 440 450
NGGNKAVVLA AYMNYADNAG TRYEAESASM TNVSTNTNHA GYTGSGFVDQ
460 470 480 490 500
FASTGDKVSF AINAPEAGDY SLVFRYGNNT GANSTLNLYV DGNFVQKLYF
510 520 530 540 550
FNQSSWGTWK HDAWYQVPLT QGAHTVELRY ESGNVGAVNL DSLTLGTFDE
560 570 580 590 600
HSVRLADAMM SASGATHIEL GDDNQMLPHE YYPNRSKTMR SSLKNAMKDH
610 620 630 640 650
YNFITAYENL LFDSDVVPND TGSQFVNLTG VSASGDGSAN TVWYINKRTS
660 670 680 690 700
DYNIVHLINL LGNDNQWRNT ASQPSFQTNL PAKIYIGADE TISDVYLASP
710 720 730 740 750
DLSGGETQEL AFTSGTDAGG KYVSFTVPEL KYWNMIYMKR TFSVPANDIY
760 770 780 790 800
EAETAIKSNV STNTNHAGYT GSGFVDGFSS TNDGVSFVVK STASDDYALR
810 820 830 840 850
FRYANGGSDA TRDVYVDGKL AGTVSFKSTG SWSTWSYGEI TARLEPGHHT
860 870 880 890 900
IVLWQTSGNT GAINLDHLDL DKTYIWQFDR QIVSVPAGYR ITFRTGLPGW
910 920 930 940 950
VHWGVNGWTG VTDTPLRSNG SLDGNLDHET SIGPFATGTA VDVTFLWDDN
960 970
NNGILEPSTD RWEGTDFGIN VS
Length:972
Mass (Da):107,431
Last modified:May 1, 1997 - v1
Checksum:i2827BEA61782CC22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D61382 Genomic DNA. Translation: BAA09604.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D61382 Genomic DNA. Translation: BAA09604.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3WNK X-ray 2.30 A 39-738 [» ]
3WNL X-ray 2.60 A 39-738 [» ]
3WNM X-ray 2.25 A 39-738 [» ]
3WNN X-ray 2.25 A/B 39-738 [» ]
3WNO X-ray 1.90 A/B 39-738 [» ]
3WNP X-ray 2.80 A/B 39-738 [» ]
ProteinModelPortali P94286.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM35. Carbohydrate-Binding Module Family 35.
GH66. Glycoside Hydrolase Family 66.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.120.260. 2 hits.
InterProi IPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR025092. Glyco_hydro_66.
[Graphical view ]
Pfami PF03422. CBM_6. 2 hits.
PF13199. Glyco_hydro_66. 1 hit.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 2 hits.
PROSITEi PS51175. CBM6. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCTA1_BACCI
AccessioniPrimary (citable) accession number: P94286
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: November 26, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3