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Protein

Triosephosphate isomerase

Gene

tpiA

Organism
Pyrococcus woesei
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).UniRule annotation

Catalytic activityi

D-glyceraldehyde 3-phosphate = glycerone phosphate.UniRule annotation

Temperature dependencei

Thermostable. The formation of the dimer of dimers is important to increase the thermostability.1 Publication

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate from glycerone phosphate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Triosephosphate isomerase (tpiA)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate from glycerone phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei96 – 961ElectrophileUniRule annotation
Active sitei144 – 1441Proton acceptorUniRule annotation
Binding sitei149 – 1491Substrate; via carbonyl oxygenUniRule annotation1 Publication
Binding sitei184 – 1841Substrate; via amide nitrogenUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Gluconeogenesis, Glycolysis, Pentose shunt

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11811.
BRENDAi5.3.1.1. 5249.
UniPathwayiUPA00109; UER00189.
UPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Triosephosphate isomerase1 PublicationUniRule annotation (EC:5.3.1.1UniRule annotation)
Short name:
TIM1 PublicationUniRule annotation
Short name:
TPIUniRule annotation
Alternative name(s):
Triose-phosphate isomeraseUniRule annotation
Gene namesi
Name:tpiAUniRule annotation
Synonyms:tpi
OrganismiPyrococcus woesei
Taxonomic identifieri2262 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 228227Triosephosphate isomerasePRO_0000090344Add
BLAST

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.UniRule annotation2 Publications

Structurei

Secondary structure

1
228
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Helixi17 – 193Combined sources
Helixi21 – 3616Combined sources
Beta strandi41 – 455Combined sources
Helixi48 – 569Combined sources
Beta strandi62 – 654Combined sources
Beta strandi72 – 743Combined sources
Helixi81 – 866Combined sources
Beta strandi91 – 955Combined sources
Helixi97 – 993Combined sources
Helixi103 – 11614Combined sources
Beta strandi119 – 1268Combined sources
Helixi127 – 1348Combined sources
Beta strandi139 – 1435Combined sources
Turni146 – 1516Combined sources
Turni155 – 1573Combined sources
Helixi161 – 17313Combined sources
Beta strandi177 – 1848Combined sources
Helixi188 – 1969Combined sources
Beta strandi200 – 2056Combined sources
Helixi206 – 2094Combined sources
Helixi214 – 22310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HG3X-ray2.70A/B/C/D/E/F/G/H1-225[»]
ProteinModelPortaliP62003.
SMRiP62003. Positions 2-225.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62003.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni12 – 143Substrate bindingUniRule annotation1 Publication
Regioni205 – 2062Substrate bindingUniRule annotation1 Publication

Sequence similaritiesi

Belongs to the triosephosphate isomerase family.UniRule annotation

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_A. TIM_A.
InterProiIPR013785. Aldolase_TIM.
IPR000652. Triosephosphate_isomerase.
IPR022891. Triosephosphate_isomerase_arc.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
PANTHERiPTHR21139. PTHR21139. 1 hit.
PfamiPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMiSSF51351. SSF51351. 1 hit.
TIGRFAMsiTIGR00419. tim. 1 hit.
PROSITEiPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62003-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKLKEPIIA INFKTYIEAT GKRALEIAKA AEKVYKETGV TIVVAPQLVD
60 70 80 90 100
LRMIAESVEI PVFAQHIDPI KPGSHTGHVL PEAVKEAGAV GTLLNHSENR
110 120 130 140 150
MILADLEAAI RRAEEVGLMT MVCSNNPAVS AAVAALNPDY VAVEPPELIG
160 170 180 190 200
TGIPVSKAKP EVITNTVELV KKVNPEVKVL CGAGISTGED VKKAIELGTV
210 220
GVLLASGVTK AKDPEKAIWD LVSGIIKE
Length:228
Mass (Da):24,066
Last modified:January 23, 2007 - v2
Checksum:i1F24C7A2D71BB6F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09481 Genomic DNA. Translation: CAA70690.2.
PIRiS66212.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09481 Genomic DNA. Translation: CAA70690.2.
PIRiS66212.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HG3X-ray2.70A/B/C/D/E/F/G/H1-225[»]
ProteinModelPortaliP62003.
SMRiP62003. Positions 2-225.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00189.
UPA00138.
BioCyciMetaCyc:MONOMER-11811.
BRENDAi5.3.1.1. 5249.

Miscellaneous databases

EvolutionaryTraceiP62003.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_A. TIM_A.
InterProiIPR013785. Aldolase_TIM.
IPR000652. Triosephosphate_isomerase.
IPR022891. Triosephosphate_isomerase_arc.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
PANTHERiPTHR21139. PTHR21139. 1 hit.
PfamiPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMiSSF51351. SSF51351. 1 hit.
TIGRFAMsiTIGR00419. tim. 1 hit.
PROSITEiPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Tetrameric triosephosphate isomerase from hyperthermophilic Archaea."
    Kohlhoff M., Dahm A., Hensel R.
    FEBS Lett. 383:245-250(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-29, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: DSM 3773.
  2. Schramm A.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 211-228.
  3. "Tiny TIM: a small, tetrameric, hyperthermostable triosephosphate isomerase."
    Walden H., Bell G.S., Russell R.J., Siebers B., Hensel R., Taylor G.L.
    J. Mol. Biol. 306:745-757(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT.

Entry informationi

Entry nameiTPIS_PYRWO
AccessioniPrimary (citable) accession number: P62003
Secondary accession number(s): P95583
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.