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Protein

Transketolase

Gene

TKT

Organism
Leishmania mexicana mexicana
Status
Unreviewed-Annotation score: Annotation score: 3 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.UniRule annotation

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei29Thiamine pyrophosphate 1Combined sources1
Binding sitei66Thiamine pyrophosphate 1Combined sources1
Metal bindingi155CalciumCombined sources1
Binding sitei156Thiamine pyrophosphate 1; via amide nitrogenCombined sources1
Metal bindingi185CalciumCombined sources1
Metal bindingi187Calcium; via carbonyl oxygenCombined sources1
Binding sitei261Thiamine pyrophosphate 1Combined sources1
Binding sitei409Thiamine pyrophosphate 2Combined sources1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotationImported

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.2.1.1. 2951.

Names & Taxonomyi

Protein namesi
Recommended name:
TransketolaseUniRule annotation (EC:2.2.1.1UniRule annotation)
Gene namesi
Name:TKTImported
OrganismiLeishmania mexicana mexicanaImported
Taxonomic identifieri44270 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R9JX-ray2.22A/B1-671[»]
ProteinModelPortaliQ8MPM3.
SMRiQ8MPM3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8MPM3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 32TRANSKETOLASE_1InterPro annotationAdd BLAST21

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni114 – 116Thiamine pyrophosphate 1 bindingCombined sources3
Regioni185 – 187Thiamine pyrophosphate 1 bindingCombined sources3
Regioni435 – 438Thiamine pyrophosphate 2 bindingCombined sources4

Sequence similaritiesi

Belongs to the transketolase family.UniRule annotation

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.

Q8MPM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASIEKVANC IRCLAADIVQ GGKSGHPGTP MGMAPMSAVL WTEVMKYNSQ
60 70 80 90 100
DPDWVDRDRF VMSNGHGCAL QYALLHMAGY NLTMDDLKGF RQDGSRTPGH
110 120 130 140 150
PERFVTPGVE VTTGPLGQGI ANAVGLAIAE AHLAATFNRP GYNIVDHYTY
160 170 180 190 200
VYCGDGCLME GVCQEALSLA GHLALEKLIV IYDSNYISID GSTSLSFTEQ
210 220 230 240 250
CHQKYVAMGF HVIEVKNGDT DYEGLRKALA EAKATKGKPK MIVQTTTIGF
260 270 280 290 300
GSSKQGTEKV HGAPLGEEDI ANIKAKFGRD PQKKYDVDDD VRAVFRMHID
310 320 330 340 350
KCSAEQKAWE ELLAKYTAAF PAEGAAFVAQ MRGELPSGWE AKLPTNSSAI
360 370 380 390 400
ATRKASENCL AVLFPAIPAL MGGSADLTPS NLTRPASANL VDFSSSSKEG
410 420 430 440 450
RYIRFGVREH AMCAILNGLD AHDGIIPFGG TFLNFIGYAL GAVRLAAISH
460 470 480 490 500
HRVIYVATHD SIGVGEDGPT HQPVELVAAL RAMPNLQVIR PSDQTETSGA
510 520 530 540 550
WAVALSSIHT PTVLCLSRQN TEPQSGSSIE GVRHGAYSVV DVPDLQLVIV
560 570 580 590 600
ASGSEVSLAV DAAKALSGEL RVRVVSMPCQ ELFDAQPDTY RQAVLPAGVP
610 620 630 640 650
VVSVEAYVSF GWEKYSHAHV GMSGFGASAP AGVLYKKFGI TVEEVVRTGR
660 670
ELAKRFPDGT APLKNSSFSK M
Length:671
Mass (Da):71,828
Last modified:October 1, 2002 - v1
Checksum:i010E2EBD52229F3C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ427448 Genomic DNA. Translation: CAD20572.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ427448 Genomic DNA. Translation: CAD20572.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R9JX-ray2.22A/B1-671[»]
ProteinModelPortaliQ8MPM3.
SMRiQ8MPM3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.2.1.1. 2951.

Miscellaneous databases

EvolutionaryTraceiQ8MPM3.

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...

Entry informationi

Entry nameiQ8MPM3_LEIME
AccessioniPrimary (citable) accession number: Q8MPM3
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2002
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.