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P45694 (TKT_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 102. 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
Short name=TK
EC=2.2.1.1
Gene names
Name:tkt
Synonyms:tktA
Ordered Locus Names:BSU17890
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length667 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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
PRO_0000191852

Regions

Nucleotide binding115 – 1173Thiamine pyrophosphate By similarity

Sites

Active site4111Proton donor By similarity
Metal binding1561Magnesium By similarity
Metal binding1861Magnesium By similarity
Metal binding1881Magnesium; via carbonyl oxygen By similarity
Binding site271Substrate By similarity
Binding site671Thiamine pyrophosphate By similarity
Binding site1571Thiamine pyrophosphate; via amide nitrogen By similarity
Binding site1861Thiamine pyrophosphate By similarity
Binding site2621Substrate By similarity
Binding site2621Thiamine pyrophosphate By similarity
Binding site3571Substrate By similarity
Binding site3841Substrate By similarity
Binding site4371Thiamine pyrophosphate By similarity
Binding site4611Substrate By similarity
Binding site4691Substrate By similarity
Binding site5201Substrate By similarity
Site271Important for catalytic activity By similarity
Site2621Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P45694 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: D93BCACD246148AF

FASTA66772,344
        10         20         30         40         50         60 
MDTIEKKSVA TIRTLSIDAI EKANSGHPGM PMGAAPMAYT LWTKFMNVSP ANPGWFNRDR 

        70         80         90        100        110        120 
FVLSAGHGSA LLYSMLHLSG FDLSIEDLKG FRQWGSKTPG HPEFGHTAGV DATTGPLGQG 

       130        140        150        160        170        180 
IAMAVGMAIA ERHLAETYNR DSFNVVDHYT YSICGDGDLM EGISSEAASL AGHLQLGRLI 

       190        200        210        220        230        240 
VLYDSNDISL DGDLDRSFSE NVKQRFEAMN WEVLYVEDGN NIEELTAAIE KARQNEKKPT 

       250        260        270        280        290        300 
LIEVKTTIGF GSPNRAGTSG VHGAPLGKEE SKLTKEAYAW TYEEDFYVPS EVYEHFAVAV 

       310        320        330        340        350        360 
KESGEKKEQE WNAQFAKYKE VYPELAEQLE LAIKGELPKD WDQEVPVYEK GSSLASRASS 

       370        380        390        400        410        420 
GEVLNGLAKK IPFFVGGSAD LAGSNKTTIK NAGDFTAVDY SGKNFWFGVR EFAMGAALNG 

       430        440        450        460        470        480 
MALHGGLRVF GGTFFVFSDY LRPAIRLAAL MGLPVTYVFT HDSIAVGEDG PTHEPVEQLA 

       490        500        510        520        530        540 
SLRAMPNLSL IRPADGNETA AAWKLAVQST DHPTALVLTR QNLPTIDQTS EEALAGVEKG 

       550        560        570        580        590        600 
AYVVSKSKNE TPDALLIASG SEVGLAIEAQ AELAKENIDV SVVSMPSMDR FEKQSDEYKN 

       610        620        630        640        650        660 
EVLPADVKKR LAIEMGSSFG WGKYTGLEGD VLGIDRFGAS APGETIINEY GFSVPNVVNR 


VKALINK

« Hide

References

« Hide 'large scale' references
[1]"New genes in the 170 degrees region of the Bacillus subtilis genome encode DNA gyrase subunits, a thioredoxin, a xylanase and an amino acid transporter."
Rose M., Entian K.-D.
Microbiology 142:3097-3101(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Identification and characterization of the ccdA gene, required for cytochrome c synthesis in Bacillus subtilis."
Schioett T., von Wachenfeldt C., Hederstedt L.
J. Bacteriol. 179:1962-1973(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 561-667.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z73234 Genomic DNA. Translation: CAA97616.1.
AL009126 Genomic DNA. Translation: CAB13673.1.
X87845 Genomic DNA. Translation: CAA61113.1.
PIRG69723.
RefSeqNP_389672.1. NC_000964.3.

3D structure databases

ProteinModelPortalP45694.
SMRP45694. Positions 3-665.
ModBaseSearch...

Protein-protein interaction databases

IntActP45694. 2 interactions.
STRING224308.BSU17890.

Proteomic databases

PaxDbP45694.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13673; CAB13673; BSU17890.
GeneID937377.
KEGGbsu:BSU17890.
PATRIC18975407. VBIBacSub10457_1895.

Organism-specific databases

GenoListBSU17890. [Micado]

Phylogenomic databases

eggNOGCOG0021.
HOGENOMHOG000225954.
KOK00615.
OMAHSEICLN.
ProtClustDBCLSK887352.

Enzyme and pathway databases

BioCycBSUB:BSU17890-MONOMER.

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 nameTKT_BACSU
AccessionPrimary (citable) accession number: P45694
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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