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Protein

Transketolase 2

Gene

TKL2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301SubstrateBy similarity
Sitei30 – 301Important for catalytic activityBy similarity
Binding sitei69 – 691Thiamine pyrophosphateBy similarity
Metal bindingi157 – 1571MagnesiumBy similarity
Binding sitei158 – 1581Thiamine pyrophosphate; via amide nitrogenBy similarity
Metal bindingi187 – 1871MagnesiumBy similarity
Binding sitei187 – 1871Thiamine pyrophosphateBy similarity
Metal bindingi189 – 1891Magnesium; via carbonyl oxygenBy similarity
Binding sitei263 – 2631SubstrateBy similarity
Binding sitei263 – 2631Thiamine pyrophosphateBy similarity
Sitei263 – 2631Important for catalytic activityBy similarity
Binding sitei359 – 3591SubstrateBy similarity
Binding sitei386 – 3861SubstrateBy similarity
Active sitei418 – 4181Proton donorBy similarity
Binding sitei418 – 4181Thiamine pyrophosphateBy similarity
Binding sitei445 – 4451Thiamine pyrophosphateBy similarity
Binding sitei469 – 4691SubstrateBy similarity
Binding sitei477 – 4771SubstrateBy similarity
Binding sitei528 – 5281SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi116 – 1183Thiamine pyrophosphateBy similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • transketolase activity Source: SGD

GO - Biological processi

  • pentose-phosphate shunt Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciYEAST:YBR117C-MONOMER.
BRENDAi2.2.1.1. 984.
ReactomeiR-SCE-163754. Insulin effects increased synthesis of Xylulose-5-Phosphate.
R-SCE-71336. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RKP33315.

Names & Taxonomyi

Protein namesi
Recommended name:
Transketolase 2 (EC:2.2.1.1)
Short name:
TK 2
Gene namesi
Name:TKL2
Ordered Locus Names:YBR117C
ORF Names:YBR0912
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR117C.
SGDiS000000321. TKL2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 681680Transketolase 2PRO_0000191905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei286 – 2861PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP33315.
TopDownProteomicsiP33315.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi32819. 19 interactions.
DIPiDIP-757N.
IntActiP33315. 2 interactions.
MINTiMINT-545508.

Structurei

3D structure databases

ProteinModelPortaliP33315.
SMRiP33315. Positions 3-681.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.Curated

Phylogenomic databases

HOGENOMiHOG000225953.
InParanoidiP33315.
KOiK00615.
OMAiDDMESIS.
OrthoDBiEOG78H42J.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33315-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQFSDIDKL AVSTLRLLSV DQVESAQSGH PGAPLGLAPV AHVIFKQLRC
60 70 80 90 100
NPNNEHWINR DRFVLSNGHS CALLYSMLHL LGYDYSIEDL RQFRQVNSRT
110 120 130 140 150
PGHPEFHSAG VEITSGPLGQ GISNAVGMAI AQANFAATYN EDGFPISDSY
160 170 180 190 200
TFAIVGDGCL QEGVSSETSS LAGHLQLGNL ITFYDSNSIS IDGKTSYSFD
210 220 230 240 250
EDVLKRYEAY GWEVMEVDKG DDDMESISSA LEKAKLSKDK PTIIKVTTTI
260 270 280 290 300
GFGSLQQGTA GVHGSALKAD DVKQLKKRWG FDPNKSFVVP QEVYDYYKKT
310 320 330 340 350
VVEPGQKLNE EWDRMFEEYK TKFPEKGKEL QRRLNGELPE GWEKHLPKFT
360 370 380 390 400
PDDDALATRK TSQQVLTNMV QVLPELIGGS ADLTPSNLTR WEGAVDFQPP
410 420 430 440 450
ITQLGNYAGR YIRYGVREHG MGAIMNGISA FGANYKPYGG TFLNFVSYAA
460 470 480 490 500
GAVRLAALSG NPVIWVATHD SIGLGEDGPT HQPIETLAHL RAIPNMHVWR
510 520 530 540 550
PADGNETSAA YYSAIKSGRT PSVVALSRQN LPQLEHSSFE KALKGGYVIH
560 570 580 590 600
DVENPDIILV STGSEVSISI DAAKKLYDTK KIKARVVSLP DFYTFDRQSE
610 620 630 640 650
EYRFSVLPDG VPIMSFEVLA TSSWGKYAHQ SFGLDEFGRS GKGPEIYKLF
660 670 680
DFTADGVASR AEKTINYYKG KQLLSPMGRA F
Length:681
Mass (Da):75,029
Last modified:February 1, 1994 - v1
Checksum:i84D7477916D136D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73532 Genomic DNA. Translation: CAA51937.1.
X78993 Genomic DNA. Translation: CAA55619.1.
Z35985 Genomic DNA. Translation: CAA85074.1.
BK006936 Genomic DNA. Translation: DAA07235.1.
PIRiS37809.
RefSeqiNP_009675.3. NM_001178465.3.

Genome annotation databases

EnsemblFungiiYBR117C; YBR117C; YBR117C.
GeneIDi852414.
KEGGisce:YBR117C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73532 Genomic DNA. Translation: CAA51937.1.
X78993 Genomic DNA. Translation: CAA55619.1.
Z35985 Genomic DNA. Translation: CAA85074.1.
BK006936 Genomic DNA. Translation: DAA07235.1.
PIRiS37809.
RefSeqiNP_009675.3. NM_001178465.3.

3D structure databases

ProteinModelPortaliP33315.
SMRiP33315. Positions 3-681.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32819. 19 interactions.
DIPiDIP-757N.
IntActiP33315. 2 interactions.
MINTiMINT-545508.

Proteomic databases

MaxQBiP33315.
TopDownProteomicsiP33315.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR117C; YBR117C; YBR117C.
GeneIDi852414.
KEGGisce:YBR117C.

Organism-specific databases

EuPathDBiFungiDB:YBR117C.
SGDiS000000321. TKL2.

Phylogenomic databases

HOGENOMiHOG000225953.
InParanoidiP33315.
KOiK00615.
OMAiDDMESIS.
OrthoDBiEOG78H42J.

Enzyme and pathway databases

BioCyciYEAST:YBR117C-MONOMER.
BRENDAi2.2.1.1. 984.
ReactomeiR-SCE-163754. Insulin effects increased synthesis of Xylulose-5-Phosphate.
R-SCE-71336. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RKP33315.

Miscellaneous databases

PROiP33315.

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. "TKL2, a second transketolase gene of Saccharomyces cerevisiae. Cloning, sequence and deletion analysis of the gene."
    Schaaff-Gerstenschlaeger I., Mannhaupt G., Vetter I., Zimmermann F.K., Feldmann H.
    Eur. J. Biochem. 217:487-492(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Analysis of a 70 kb region on the right arm of yeast chromosome II."
    Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
    Yeast 10:1363-1381(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTKT2_YEAST
AccessioniPrimary (citable) accession number: P33315
Secondary accession number(s): D6VQB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 8, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 149 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

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.