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Protein

Cycloisomaltooligosaccharide glucanotransferase

Gene
N/A
Organism
Bacillus circulans
Status
Reviewed-Annotation score: 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
  1. 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

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.248. 649.

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)DescriptionActionsGraphical viewLength
Mutagenesisi183D → N: Has 1% of wild-type activity. 1 Publication1
Mutagenesisi308D → N: No activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 38Sequence analysisAdd BLAST38
ChainiPRO_000001224139 – 972Cycloisomaltooligosaccharide glucanotransferaseAdd BLAST934

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1972
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 50Combined sources7
Beta strandi52 – 54Combined sources3
Beta strandi59 – 67Combined sources9
Beta strandi70 – 72Combined sources3
Beta strandi74 – 84Combined sources11
Beta strandi87 – 98Combined sources12
Beta strandi103 – 111Combined sources9
Beta strandi114 – 125Combined sources12
Helixi127 – 129Combined sources3
Beta strandi131 – 138Combined sources8
Helixi142 – 144Combined sources3
Beta strandi148 – 151Combined sources4
Helixi160 – 174Combined sources15
Beta strandi178 – 181Combined sources4
Beta strandi185 – 187Combined sources3
Beta strandi201 – 204Combined sources4
Beta strandi210 – 212Combined sources3
Helixi213 – 225Combined sources13
Beta strandi229 – 242Combined sources14
Helixi244 – 246Combined sources3
Helixi250 – 252Combined sources3
Beta strandi253 – 257Combined sources5
Beta strandi265 – 267Combined sources3
Beta strandi269 – 272Combined sources4
Beta strandi274 – 278Combined sources5
Helixi283 – 300Combined sources18
Beta strandi303 – 308Combined sources6
Beta strandi315 – 318Combined sources4
Helixi326 – 328Combined sources3
Helixi330 – 344Combined sources15
Helixi346 – 348Combined sources3
Beta strandi350 – 357Combined sources8
Helixi365 – 371Combined sources7
Beta strandi375 – 380Combined sources6
Beta strandi383 – 385Combined sources3
Helixi388 – 401Combined sources14
Beta strandi407 – 410Combined sources4
Turni413 – 416Combined sources4
Beta strandi420 – 424Combined sources5
Helixi425 – 427Combined sources3
Beta strandi428 – 432Combined sources5
Beta strandi434 – 436Combined sources3
Beta strandi439 – 441Combined sources3
Beta strandi447 – 451Combined sources5
Beta strandi457 – 477Combined sources21
Beta strandi480 – 482Combined sources3
Beta strandi484 – 490Combined sources7
Beta strandi493 – 500Combined sources8
Beta strandi504 – 507Combined sources4
Beta strandi509 – 519Combined sources11
Beta strandi521 – 529Combined sources9
Beta strandi538 – 547Combined sources10
Helixi550 – 562Combined sources13
Beta strandi566 – 568Combined sources3
Turni572 – 574Combined sources3
Beta strandi579 – 581Combined sources3
Beta strandi586 – 588Combined sources3
Helixi591 – 606Combined sources16
Helixi608 – 612Combined sources5
Beta strandi621 – 623Combined sources3
Beta strandi626 – 628Combined sources3
Beta strandi633 – 636Combined sources4
Beta strandi641 – 648Combined sources8
Beta strandi650 – 659Combined sources10
Beta strandi665 – 669Combined sources5
Beta strandi677 – 686Combined sources10
Beta strandi692 – 698Combined sources7
Helixi703 – 705Combined sources3
Beta strandi708 – 710Combined sources3
Beta strandi713 – 717Combined sources5
Beta strandi720 – 738Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP94286.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini421 – 546CBM6 1PROSITE-ProRule annotationAdd BLAST126
Domaini748 – 871CBM6 2PROSITE-ProRule annotationAdd BLAST124

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

CDDicd14745. GH66. 1 hit.
Gene3Di2.60.120.260. 2 hits.
InterProiIPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR025092. Glyco_hydro_66.
[Graphical view]
PfamiPF16990. CBM_35. 1 hit.
PF03422. CBM_6. 1 hit.
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.

Genome annotation databases

KEGGiag:BAA09604.

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
PDB 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.
SMRiP94286.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAA09604.

Enzyme and pathway databases

BRENDAi2.4.1.248. 649.

Family and domain databases

CDDicd14745. GH66. 1 hit.
Gene3Di2.60.120.260. 2 hits.
InterProiIPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR025092. Glyco_hydro_66.
[Graphical view]
PfamiPF16990. CBM_35. 1 hit.
PF03422. CBM_6. 1 hit.
PF13199. Glyco_hydro_66. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
PROSITEiPS51175. CBM6. 2 hits.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 67 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.