SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

G3V826

- G3V826_RAT

UniProt

G3V826 - G3V826_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Transketolase

Gene
Tkt, rCG_42377
Organism
Rattus norvegicus (Rat)
Status
Unreviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

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

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. transketolase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotation

Keywords - Ligandi

CalciumUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Thiamine pyrophosphateUniRule annotation

Enzyme and pathway databases

ReactomeiREACT_226758. Pentose phosphate pathway (hexose monophosphate shunt).

Names & Taxonomyi

Protein namesi
Recommended name:
TransketolaseUniRule annotation (EC:2.2.1.1UniRule annotation)
Gene namesi
Name:TktImported
ORF Names:rCG_42377Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 16

Organism-specific databases

RGDi621036. Tkt.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000005240.
OMAiPPNYKVG.
OrthoDBiEOG72RMXF.
TreeFamiTF313097.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
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.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

G3V826-1 [UniParc]FASTAAdd to Basket

« Hide

MDPVRQIQCD REGKRFPFLS APPASTSSPD RAMEGYHKPD QQKLQALKDT    50
ANRLRISSIQ ATTAAGSGHP TSCCSAAEIM AVLFFHTMRY KALDPRNPHN 100
DRFVLSKGHA APILYAVWAE AGFLPEAELL NLRKISSDLD GHPVPKQAFT 150
DVATGSLGQG LGAACGMAYT GKYFDKASYR VYCMLGDGEV SEGSVWEAMA 200
FAGIYKLDNL VAIFDINRLG QSDPAPLQHQ VDVYQKRCEA FGWHAIIVDG 250
HSVEELCKAF GQAKHQPTAI IAKTFKGRGI TGIEDKEAWH GKPLPKNMAE 300
QIIQEIYSQV QSKKKILATP PQEDAPSVDI ANIRMPTPPN YKVGDKIATR 350
KAYGLALAKL GHASDRIIAL DGDTKNSTFS ELFKKEHPDR FIECYIAEQN 400
MVSIAVGCAT RDRTVPFCST FAAFFTRAFD QIRMAAISES NINLCGSHCG 450
VSIGEDGPSQ MALEDLAMFR SVPMSTVFYP SDGVATEKAV ELAANTKGIC 500
FIRTSRPENA IIYSNNEDFQ VGQAKVVLKS KDDQVTVIGA GVTLHEALAA 550
AEMLKKEKIG VRVLDPFTIK PLDKKLILDC ARATKGRILT VEDHYYEGGI 600
GEAVSAAVVG EPGVTVTRLA VSQVPRSGKP AELLKMFGID KDAIVQAVKG 650
LVTKG 655
Length:655
Mass (Da):71,159
Last modified:November 16, 2011 - v1
Checksum:i879FF8EFF616343F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR06086358 Genomic DNA. No translation available.
CH474046 Genomic DNA. Translation: EDL88991.1.
UniGeneiRn.5950.

Genome annotation databases

EnsembliENSRNOT00000021862; ENSRNOP00000021862; ENSRNOG00000016064.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR06086358 Genomic DNA. No translation available.
CH474046 Genomic DNA. Translation: EDL88991.1 .
UniGenei Rn.5950.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000021862 ; ENSRNOP00000021862 ; ENSRNOG00000016064 .

Organism-specific databases

RGDi 621036. Tkt.

Phylogenomic databases

GeneTreei ENSGT00390000005240.
OMAi PPNYKVG.
OrthoDBi EOG72RMXF.
TreeFami TF313097.

Enzyme and pathway databases

Reactomei REACT_226758. Pentose phosphate pathway (hexose monophosphate shunt).

Miscellaneous databases

NextBioi 35584071.
PROi G3V826.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProi IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR020826. Transketolase_BS.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view ]
Pfami PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view ]
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
PROSITEi PS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Ensembl
    Submitted (SEP-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiG3V826_RAT
AccessioniPrimary (citable) accession number: G3V826
Entry historyi
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: September 3, 2014
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3

Similar proteinsi