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Protein

Triosephosphate isomerase

Gene

tpiA

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 4 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 annotation1 Publication

Catalytic activityi

D-glyceraldehyde 3-phosphate = glycerone phosphate.UniRule annotation1 Publication

Temperature dependencei

The enzyme is active over the temperature range 20-60 degrees Celsius, showing an increase in specific activity with temperature.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 sitei90 – 901ElectrophileUniRule annotation
Active sitei138 – 1381Proton acceptorUniRule annotation
Binding sitei143 – 1431Substrate; via carbonyl oxygenUniRule annotation
Binding sitei178 – 1781Substrate; 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-14589.
BRENDAi5.3.1.1. 3260.
UniPathwayiUPA00109; UER00189.
UPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Triosephosphate isomerase1 PublicationUniRule annotation (EC:5.3.1.1UniRule annotation1 Publication)
Short name:
TIM1 PublicationUniRule annotation
Short name:
TPIUniRule annotation
Alternative name(s):
Triose-phosphate isomeraseUniRule annotation
Gene namesi
Name:tpiAUniRule annotation
Ordered Locus Names:MJ1528
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

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
Chaini1 – 219219Triosephosphate isomerasePRO_0000090335Add
BLAST

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi243232.MJ_1528.

Structurei

Secondary structure

1
219
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Helixi11 – 133Combined sources
Helixi16 – 3217Combined sources
Beta strandi36 – 394Combined sources
Turni42 – 443Combined sources
Helixi45 – 517Combined sources
Beta strandi56 – 594Combined sources
Beta strandi66 – 683Combined sources
Helixi75 – 806Combined sources
Beta strandi85 – 906Combined sources
Helixi97 – 11014Combined sources
Beta strandi113 – 1219Combined sources
Helixi122 – 1276Combined sources
Turni128 – 1303Combined sources
Beta strandi133 – 1375Combined sources
Helixi158 – 16710Combined sources
Beta strandi172 – 1754Combined sources
Helixi182 – 1898Combined sources
Turni190 – 1923Combined sources
Beta strandi196 – 1994Combined sources
Helixi200 – 2034Combined sources
Helixi208 – 2158Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H6RX-ray2.30A/B/C/D/E/F/G/H1-219[»]
ProteinModelPortaliQ58923.
SMRiQ58923. Positions 1-217.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ58923.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni6 – 83Substrate bindingUniRule annotation
Regioni199 – 2002Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the triosephosphate isomerase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01087. Archaea.
COG0149. LUCA.
InParanoidiQ58923.
KOiK01803.
OMAiETWAQHV.
PhylomeDBiQ58923.

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.

Q58923-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIVINYKTY NESIGNRGLE IAKIAEKVSE ESGITIGVAP QFVDLRMIVE
60 70 80 90 100
NVNIPVYAQH IDNINPGSHT GHILAEAIKD CGCKGTLINH SEKRMLLADI
110 120 130 140 150
EAVINKCKNL GLETIVCTNN INTSKAVAAL SPDYIAVEPP ELIGTGIPVS
160 170 180 190 200
KANPEVVEGT VRAVKEINKD VKVLCGAGIS KGEDVKAALD LGAEGVLLAS
210
GVVKAKNVEE AIRELIKFI
Length:219
Mass (Da):23,319
Last modified:November 1, 1997 - v1
Checksum:iC6BC49A2DEE8A026
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99546.1.
PIRiG64490.

Genome annotation databases

EnsemblBacteriaiAAB99546; AAB99546; MJ_1528.
KEGGimja:MJ_1528.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99546.1.
PIRiG64490.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H6RX-ray2.30A/B/C/D/E/F/G/H1-219[»]
ProteinModelPortaliQ58923.
SMRiQ58923. Positions 1-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_1528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB99546; AAB99546; MJ_1528.
KEGGimja:MJ_1528.

Phylogenomic databases

eggNOGiarCOG01087. Archaea.
COG0149. LUCA.
InParanoidiQ58923.
KOiK01803.
OMAiETWAQHV.
PhylomeDBiQ58923.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00189.
UPA00138.
BioCyciMetaCyc:MONOMER-14589.
BRENDAi5.3.1.1. 3260.

Miscellaneous databases

EvolutionaryTraceiQ58923.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
  2. "Structure of triosephosphate isomerase (TIM) from Methanocaldococcus jannaschii."
    Gayathri P., Banerjee M., Vijayalakshmi A., Azeez S., Balaram H., Balaram P., Murthy M.R.
    Acta Crystallogr. D 63:206-220(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-219, FUNCTION AS A TRIOSEPHOSPHATE ISOMERASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Entry informationi

Entry nameiTPIS_METJA
AccessioniPrimary (citable) accession number: Q58923
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 16, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.