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Protein

Transketolase

Gene

tkt

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.UniRule annotation

Catalytic activityi

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation, Ca2+UniRule annotation, Mn2+UniRule annotation, Co2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+.UniRule annotation
  • thiamine diphosphateUniRule annotationNote: Binds 1 thiamine pyrophosphate per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei67 – 671Thiamine pyrophosphateCombined sources
Metal bindingi152 – 1521CalciumCombined sources
Metal bindingi152 – 1521MagnesiumCombined sources
Metal bindingi182 – 1821CalciumCombined sources
Metal bindingi182 – 1821MagnesiumCombined sources
Metal bindingi184 – 1841Calcium; via carbonyl oxygenCombined sources
Metal bindingi184 – 1841Magnesium; via carbonyl oxygenCombined sources
Binding sitei256 – 2561Thiamine pyrophosphateCombined sources
Binding sitei391 – 3911Thiamine pyrophosphateCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotationSAAS annotationImported

Keywords - Ligandi

CalciumUniRule annotationCombined sources, MagnesiumUniRule annotationCombined sourcesSAAS annotation, Metal-bindingUniRule annotationCombined sourcesSAAS annotation, Thiamine pyrophosphateUniRule annotationCombined sourcesSAAS annotation

Enzyme and pathway databases

BioCyciCJEJ192222:GJTS-1608-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
TransketolaseUniRule annotation (EC:2.2.1.1UniRule annotation)
Gene namesi
Name:tktImported
Ordered Locus Names:Cj1645Imported
OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)Imported
Taxonomic identifieri192222 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
Proteomesi
  • UP000000799 Componenti: Chromosome

PTM / Processingi

Proteomic databases

PaxDbiQ0P7Y3.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ0P7Y3. 10 interactions.
STRINGi192222.Cj1645.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L84X-ray1.36A1-632[»]
3M34X-ray1.65A1-632[»]
3M6LX-ray1.59A1-632[»]
3M7IX-ray1.75A1-632[»]
ProteinModelPortaliQ0P7Y3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0P7Y3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 3421TRANSKETOLASE_1InterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni114 – 1163Thiamine pyrophosphate bindingCombined sources
Regioni152 – 1532Thiamine pyrophosphate bindingCombined sources
Regioni182 – 1843Thiamine pyrophosphate bindingCombined sources
Regioni417 – 4204Thiamine pyrophosphate bindingCombined sources

Sequence similaritiesi

Belongs to the transketolase family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiENOG4105CV1. Bacteria.
COG0021. LUCA.
HOGENOMiHOG000225954.
KOiK00615.
OMAiESKDAKF.
OrthoDBiEOG6N3CRG.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR005478. Transketolase_bac-like.
IPR020826. Transketolase_BS.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 2 hits.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00232. tktlase_bact. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0P7Y3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIQILQEQA NTLRFLSADM VQKANSGHPG APLGLADILS VLSYHLKHNP
60 70 80 90 100
KNPTWLNRDR LVFSGGHASA LLYSFLHLSG YDLSLEDLKN FRQLHSKTPG
110 120 130 140 150
HPEISTLGVE IATGPLGQGV ANAVGFAMAA KKAQNLLGSD LIDHKIYCLC
160 170 180 190 200
GDGDLQEGIS YEACSLAGLH KLDNFILIYD SNNISIEGDV GLAFNENVKM
210 220 230 240 250
RFEAQGFEVL SINGHDYEEI NKALEQAKKS TKPCLIIAKT TIAKGAGELE
260 270 280 290 300
GSHKSHGAPL GEEVIKKAKE QAGFDPNISF HIPQASKIRF ESAVELGDLE
310 320 330 340 350
EAKWKDKLEK SAKKELLERL LNPDFNKIAY PDFKGKDLAT RDSNGEILNV
360 370 380 390 400
LAKNLEGFLG GSADLGPSNK TELHSMGDFV EGKNIHFGIR EHAMAAINNA
410 420 430 440 450
FARYGIFLPF SATFFIFSEY LKPAARIAAL MKIKHFFIFT HDSIGVGEDG
460 470 480 490 500
PTHQPIEQLS TFRAMPNFLT FRPADGVENV KAWQIALNAD IPSAFVLSRQ
510 520 530 540 550
KLKALNEPVF GDVKNGAYLL KESKEAKFTL LASGSEVWLC LESANELEKQ
560 570 580 590 600
GFACNVVSMP CFELFEKQDK AYQERLLKGE VIGVEAAHSN ELYKFCHKVY
610 620 630
GIESFGESGK DKDVFERFGF SVSKLVNFIL SK
Length:632
Mass (Da):69,636
Last modified:September 19, 2006 - v1
Checksum:iFE55D337D3638D9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35742.1.
PIRiC81261.
RefSeqiWP_002858130.1. NC_002163.1.
YP_002345014.1. NC_002163.1.

Genome annotation databases

EnsemblBacteriaiCAL35742; CAL35742; Cj1645.
GeneIDi905918.
KEGGicje:Cj1645.
PATRICi20060258. VBICamJej33762_1621.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35742.1.
PIRiC81261.
RefSeqiWP_002858130.1. NC_002163.1.
YP_002345014.1. NC_002163.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L84X-ray1.36A1-632[»]
3M34X-ray1.65A1-632[»]
3M6LX-ray1.59A1-632[»]
3M7IX-ray1.75A1-632[»]
ProteinModelPortaliQ0P7Y3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ0P7Y3. 10 interactions.
STRINGi192222.Cj1645.

Proteomic databases

PaxDbiQ0P7Y3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL35742; CAL35742; Cj1645.
GeneIDi905918.
KEGGicje:Cj1645.
PATRICi20060258. VBICamJej33762_1621.

Phylogenomic databases

eggNOGiENOG4105CV1. Bacteria.
COG0021. LUCA.
HOGENOMiHOG000225954.
KOiK00615.
OMAiESKDAKF.
OrthoDBiEOG6N3CRG.

Enzyme and pathway databases

BioCyciCJEJ192222:GJTS-1608-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ0P7Y3.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR005478. Transketolase_bac-like.
IPR020826. Transketolase_BS.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
IPR005474. Transketolase_N.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 2 hits.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00232. tktlase_bact. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700819 / NCTC 11168Imported.
  2. "High resolution crystal structure of transketolase from Campylobacter jejuni subsp. jejuni NCTC 11168."
    Nocek B., Makowska-Grzysa M., Maltseva N., Grimshaw S., Anderson W.F., Joachimiak A.
    Submitted (DEC-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS).
  3. "Crystal structure of transketolase in complex with thiamin diphosphate and calcium ion."
    Nocek B., Makowska-Grzyska M., Maltseva N., Grimshaw S., Joachimiak A., Anderson W., CSGID, NIAID
    Submitted (MAR-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH CALCIUM AND THIAMINE PYROPHOSPHATE.
  4. "Crystal structure of transketolase in complex with thiamine diphosphate, ribose-5-phosphate and calcium ion."
    Nocek B., Makowska-Grzyska M., Maltseva N., Grimshaw S., Joachimiak A., Anderson W.
    Submitted (MAR-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) IN COMPLEX WITH CALCIUM AND THIAMINE PYROPHOSPHATE.
  5. "Crystal structure of transketolase in complex with thiamine diphosphate, ribose-5-phosphate(pyranose form) and magnesium ion."
    Center for Structural Genomics of Infectious Diseases (CSGID)
    Nocek B., Makowska-Grzyska M., Maltseva N., Anderson W., Joachimiak A.
    Submitted (MAR-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND THIAMINE PYROPHOSPHATE.

Entry informationi

Entry nameiQ0P7Y3_CAMJE
AccessioniPrimary (citable) accession number: Q0P7Y3
Entry historyi
Integrated into UniProtKB/TrEMBL: September 19, 2006
Last sequence update: September 19, 2006
Last modified: May 11, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.