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P33570 (TKT2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transketolase 2
Short name=TK 2
EC=2.2.1.1
Gene names
Name:tktB
Ordered Locus Names:b2465, JW2449
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length667 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate. 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 By similarity.

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+ By similarity.

Binds 1 thiamine pyrophosphate per subunit By similarity.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the transketolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 667667Transketolase 2
PRO_0000191857

Regions

Nucleotide binding113 – 1153Thiamine pyrophosphate By similarity

Sites

Active site4101Proton donor By similarity
Metal binding1541Magnesium By similarity
Metal binding1841Magnesium By similarity
Metal binding1861Magnesium; via carbonyl oxygen By similarity
Binding site251Substrate By similarity
Binding site651Thiamine pyrophosphate By similarity
Binding site1551Thiamine pyrophosphate; via amide nitrogen By similarity
Binding site1841Thiamine pyrophosphate By similarity
Binding site2601Substrate By similarity
Binding site2601Thiamine pyrophosphate By similarity
Binding site3571Substrate By similarity
Binding site3841Substrate By similarity
Binding site4361Thiamine pyrophosphate By similarity
Binding site4601Substrate By similarity
Binding site4681Substrate By similarity
Binding site5191Substrate By similarity
Site251Important for catalytic activity By similarity
Site2601Important for catalytic activity By similarity

Amino acid modifications

Modified residue3421N6-acetyllysine Ref.5

Sequences

Sequence LengthMass (Da)Tools
P33570 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 451D748B13ED51E5

FASTA66773,043
        10         20         30         40         50         60 
MSRKDLANAI RALSMDAVQK ANSGHPGAPM GMADIAEVLW NDFLKHNPTD PTWYDRDRFI 

        70         80         90        100        110        120 
LSNGHASMLL YSLLHLTGYD LPLEELKNFR QLHSKTPGHP EIGYTPGVET TTGPLGQGLA 

       130        140        150        160        170        180 
NAVGLAIAER TLAAQFNQPD HEIVDHFTYV FMGDGCLMEG ISHEVCSLAG TLGLGKLIGF 

       190        200        210        220        230        240 
YDHNGISIDG ETEGWFTDDT AKRFEAYHWH VIHEIDGHDP QAVKEAILEA QSVKDKPSLI 

       250        260        270        280        290        300 
ICRTVIGFGS PNKAGKEEAH GAPLGEEEVA LARQKLGWHH PPFEIPKEIY HAWDAREKGE 

       310        320        330        340        350        360 
KAQQSWNEKF AAYKKAHPQL AEEFTRRMSG GLPKDWEKTT QKYINELQAN PAKIATRKAS 

       370        380        390        400        410        420 
QNTLNAYGPM LPELLGGSAD LAPSNLTIWK GSVSLKEDPA GNYIHYGVRE FGMTAIANGI 

       430        440        450        460        470        480 
AHHGGFVPYT ATFLMFVEYA RNAARMAALM KARQIMVYTH DSIGLGEDGP THQAVEQLAS 

       490        500        510        520        530        540 
LRLTPNFSTW RPCDQVEAAV GWKLAVERHN GPTALILSRQ NLAQVERTPD QVKEIARGGY 

       550        560        570        580        590        600 
VLKDSGGKPD IILIATGSEM EITLQAAEKL AGEGRNVRVV SLPSTDIFDA QDEEYRESVL 

       610        620        630        640        650        660 
PSNVAARVAV EAGIADYWYK YVGLKGAIVG MTGYGESAPA DKLFPFFGFT AENIVAKAHK 


VLGVKGA

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of the tktB gene encoding a second transketolase in Escherichia coli K-12."
Iida A., Teshiba S., Mizobuchi K.
J. Bacteriol. 175:5375-5383(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-342, MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D12473 Genomic DNA. Translation: BAA02039.1.
U00096 Genomic DNA. Translation: AAC75518.1.
AP009048 Genomic DNA. Translation: BAA16340.1.
PIRA48660.
RefSeqNP_416960.1. NC_000913.2.
YP_490692.1. NC_007779.1.

3D structure databases

ProteinModelPortalP33570.
SMRP33570. Positions 2-662.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10999N.
IntActP33570. 6 interactions.
STRING511145.b2465.

Proteomic databases

PaxDbP33570.
PRIDEP33570.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75518; AAC75518; b2465.
BAA16340; BAA16340; BAA16340.
GeneID12933222.
945865.
KEGGecj:Y75_p2417.
eco:b2465.
PATRIC32120313. VBIEscCol129921_2559.

Organism-specific databases

EchoBASEEB2024.
EcoGeneEG12100. tktB.

Phylogenomic databases

eggNOGCOG0021.
HOGENOMHOG000225953.
KOK00615.
OMAAYVKYDA.
ProtClustDBPRK12753.

Enzyme and pathway databases

BioCycEcoCyc:TRANSKETOII-MONOMER.
ECOL316407:JW2449-MONOMER.
MetaCyc:TRANSKETOII-MONOMER.

Gene expression databases

GenevestigatorP33570.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR005478. Transketolase_bac-like.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00232. tktlase_bact. 1 hit.
PROSITEPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTKT2_ECOLI
AccessionPrimary (citable) accession number: P33570
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents