UniProtKB - P9WG25 (TKT_MYCTU)
Protein
Transketolase
Gene
tkt
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
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.1 Publication
Catalytic activityi
- D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate1 PublicationEC:2.2.1.11 Publication
Cofactori
Protein has several cofactor binding sites:- Mg2+1 Publication, Ca2+1 Publication, Mn2+1 Publication, Co2+1 PublicationNote: Binds 1 Mg2+ ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+.1 Publication
- thiamine diphosphate1 PublicationNote: Binds 1 thiamine pyrophosphate per subunit.1 Publication
Kineticsi
- KM=0.8 mM for ribose 5-phosphate1 Publication
- KM=0.6 mM for fructose 6-phosphate1 Publication
- KM=0.35 mM for xylulose 5-phosphate1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 45 | SubstrateBy similarity | 1 | |
Sitei | 45 | Important for catalytic activityBy similarity | 1 | |
Binding sitei | 48 | Thiamine pyrophosphate | 1 | |
Binding sitei | 85 | Thiamine pyrophosphate | 1 | |
Binding sitei | 135 | Thiamine pyrophosphate; via amide nitrogen | 1 | |
Metal bindingi | 177 | Magnesium1 Publication | 1 | |
Binding sitei | 178 | Thiamine pyrophosphate; via amide nitrogen | 1 | |
Metal bindingi | 207 | Magnesium1 Publication | 1 | |
Binding sitei | 207 | Thiamine pyrophosphate | 1 | |
Metal bindingi | 209 | Magnesium; via carbonyl oxygen1 Publication | 1 | |
Binding sitei | 283 | SubstrateBy similarity | 1 | |
Binding sitei | 283 | Thiamine pyrophosphate | 1 | |
Sitei | 283 | Important for catalytic activityBy similarity | 1 | |
Binding sitei | 378 | SubstrateBy similarity | 1 | |
Binding sitei | 405 | SubstrateBy similarity | 1 | |
Active sitei | 441 | Proton donorCurated | 1 | |
Binding sitei | 467 | Thiamine pyrophosphate | 1 | |
Binding sitei | 491 | SubstrateBy similarity | 1 | |
Binding sitei | 499 | SubstrateBy similarity | 1 | |
Binding sitei | 552 | SubstrateBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 133 – 135 | Thiamine pyrophosphate | 3 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- transketolase activity Source: GO_Central
GO - Biological processi
- pentose-phosphate shunt Source: GO_Central
Keywordsi
Molecular function | Transferase |
Ligand | Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-5632-MONOMER |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:tkt Ordered Locus Names:Rv1449c ORF Names:MTCY493.05 |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv1449c |
Subcellular locationi
GO - Cellular componenti
- cell wall Source: MTBBASE
- cytosol Source: MTBBASE
- extracellular region Source: MTBBASE
- plasma membrane Source: MTBBASE
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000191863 | 2 – 700 | TransketolaseAdd BLAST | 699 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylthreonineCombined sources | 1 |
Keywords - PTMi
AcetylationProteomic databases
PaxDbi | P9WG25 |
PRIDEi | P9WG25 |
PTM databases
iPTMneti | P9WG25 |
Interactioni
Subunit structurei
Homodimer.
1 PublicationProtein-protein interaction databases
STRINGi | 83332.Rv1449c |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P9WG25 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the transketolase family.Curated
Phylogenomic databases
eggNOGi | ENOG4105CV1 Bacteria COG0021 LUCA |
KOi | K00615 |
OMAi | GCAPMGY |
PhylomeDBi | P9WG25 |
Family and domain databases
CDDi | cd02012 TPP_TK, 1 hit |
Gene3Di | 3.40.50.920, 1 hit |
InterProi | View protein in InterPro IPR029061 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 |
PANTHERi | PTHR43522 PTHR43522, 1 hit |
Pfami | View protein in Pfam PF02779 Transket_pyr, 1 hit PF02780 Transketolase_C, 1 hit PF00456 Transketolase_N, 1 hit |
SMARTi | View protein in SMART SM00861 Transket_pyr, 1 hit |
SUPFAMi | SSF52518 SSF52518, 2 hits SSF52922 SSF52922, 1 hit |
TIGRFAMsi | TIGR00232 tktlase_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00801 TRANSKETOLASE_1, 1 hit PS00802 TRANSKETOLASE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P9WG25-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTTLEEISAL TRPRHPDYWT EIDSAAVDTI RVLAADAVQK VGNGHPGTAM
60 70 80 90 100
SLAPLAYTLF QRTMRHDPSD THWLGRDRFV LSAGHSSLTL YIQLYLGGFG
110 120 130 140 150
LELSDIESLR TWGSKTPGHP EFRHTPGVEI TTGPLGQGLA SAVGMAMASR
160 170 180 190 200
YERGLFDPDA EPGASPFDHY IYVIASDGDI EEGVTSEASS LAAVQQLGNL
210 220 230 240 250
IVFYDRNQIS IEDDTNIALC EDTAARYRAY GWHVQEVEGG ENVVGIEEAI
260 270 280 290 300
ANAQAVTDRP SFIALRTVIG YPAPNLMDTG KAHGAALGDD EVAAVKKIVG
310 320 330 340 350
FDPDKTFQVR EDVLTHTRGL VARGKQAHER WQLEFDAWAR REPERKALLD
360 370 380 390 400
RLLAQKLPDG WDADLPHWEP GSKALATRAA SGAVLSALGP KLPELWGGSA
410 420 430 440 450
DLAGSNNTTI KGADSFGPPS ISTKEYTAHW YGRTLHFGVR EHAMGAILSG
460 470 480 490 500
IVLHGPTRAY GGTFLQFSDY MRPAVRLAAL MDIDTIYVWT HDSIGLGEDG
510 520 530 540 550
PTHQPIEHLS ALRAIPRLSV VRPADANETA YAWRTILARR NGSGPVGLIL
560 570 580 590 600
TRQGVPVLDG TDAEGVARGG YVLSDAGGLQ PGEEPDVILI ATGSEVQLAV
610 620 630 640 650
AAQTLLADND ILARVVSMPC LEWFEAQPYE YRDAVLPPTV SARVAVEAGV
660 670 680 690 700
AQCWHQLVGD TGEIVSIEHY GESADHKTLF REYGFTAEAV AAAAERALDN
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44208.1 |
PIRi | D70917 |
RefSeqi | NP_215965.1, NC_000962.3 WP_003916819.1, NZ_NVQJ01000071.1 |
Genome annotation databases
EnsemblBacteriai | CCP44208; CCP44208; Rv1449c |
GeneIDi | 886638 |
KEGGi | mtu:Rv1449c mtv:RVBD_1449c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44208.1 |
PIRi | D70917 |
RefSeqi | NP_215965.1, NC_000962.3 WP_003916819.1, NZ_NVQJ01000071.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3RIM | X-ray | 2.49 | A/B/C/D | 1-700 | [»] | |
SMRi | P9WG25 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv1449c |
PTM databases
iPTMneti | P9WG25 |
Proteomic databases
PaxDbi | P9WG25 |
PRIDEi | P9WG25 |
Genome annotation databases
EnsemblBacteriai | CCP44208; CCP44208; Rv1449c |
GeneIDi | 886638 |
KEGGi | mtu:Rv1449c mtv:RVBD_1449c |
Organism-specific databases
TubercuListi | Rv1449c |
Phylogenomic databases
eggNOGi | ENOG4105CV1 Bacteria COG0021 LUCA |
KOi | K00615 |
OMAi | GCAPMGY |
PhylomeDBi | P9WG25 |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-5632-MONOMER |
Family and domain databases
CDDi | cd02012 TPP_TK, 1 hit |
Gene3Di | 3.40.50.920, 1 hit |
InterProi | View protein in InterPro IPR029061 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 |
PANTHERi | PTHR43522 PTHR43522, 1 hit |
Pfami | View protein in Pfam PF02779 Transket_pyr, 1 hit PF02780 Transketolase_C, 1 hit PF00456 Transketolase_N, 1 hit |
SMARTi | View protein in SMART SM00861 Transket_pyr, 1 hit |
SUPFAMi | SSF52518 SSF52518, 2 hits SSF52922 SSF52922, 1 hit |
TIGRFAMsi | TIGR00232 tktlase_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00801 TRANSKETOLASE_1, 1 hit PS00802 TRANSKETOLASE_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TKT_MYCTU | |
Accessioni | P9WG25Primary (citable) accession number: P9WG25 Secondary accession number(s): L0T9N4, O06811 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | October 16, 2019 | |
This is version 33 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references