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Protein

Triosephosphate isomerase

Gene

tpiA

Organism
Escherichia coli (strain K12)
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 annotation1 Publication

Catalytic activityi

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

Kineticsi

Kcat is 54000 min(-1) for isomerase activity with D-glyceraldehyde 3-phosphate as substrate (at 25 degrees Celsius).1 Publication

Manual assertion based on experiment ini

  1. KM=1030 µM for D-glyceraldehyde 3-phosphate (at 25 degrees Celsius)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)DescriptionActionsGraphical viewLength
    Active sitei95ElectrophileUniRule annotation1
    Active sitei167Proton acceptorUniRule annotation1
    Binding sitei173Substrate; via amide nitrogenUniRule annotation1
    Binding sitei212SubstrateUniRule annotation1

    GO - Molecular functioni

    • triose-phosphate isomerase activity Source: EcoCyc

    GO - Biological processi

    • gluconeogenesis Source: EcoliWiki
    • glyceraldehyde-3-phosphate biosynthetic process Source: GO_Central
    • glycerol catabolic process Source: GO_Central
    • glycolytic process Source: EcoCyc
    • pentose-phosphate shunt Source: UniProtKB-HAMAP
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Gluconeogenesis, Glycolysis, Pentose shunt

    Enzyme and pathway databases

    BioCyciEcoCyc:TPI-MONOMER.
    ECOL316407:JW3890-MONOMER.
    MetaCyc:TPI-MONOMER.
    BRENDAi5.3.1.1. 2026.
    SABIO-RKP0A858.
    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:
    TPI1 PublicationUniRule annotation
    Alternative name(s):
    Triose-phosphate isomeraseUniRule annotation
    Gene namesi
    Name:tpiA1 PublicationUniRule annotation
    Synonyms:tpi
    Ordered Locus Names:b3919, JW3890
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11015. tpiA.

    Subcellular locationi

    • Cytoplasm UniRule annotationCurated

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene accumulates methylglyoxal and are unable to grow on glucose, lactate or other carbon sources.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000902171 – 255Triosephosphate isomeraseAdd BLAST255

    Proteomic databases

    EPDiP0A858.
    PaxDbiP0A858.
    PRIDEiP0A858.

    2D gel databases

    SWISS-2DPAGEP0A858.

    Expressioni

    Inductioni

    Induced by CsrA and repressed by spermidine.2 Publications

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-368978,EBI-368978
    pepTP297454EBI-368978,EBI-555639
    pflBP093735EBI-368978,EBI-546682

    Protein-protein interaction databases

    DIPiDIP-31849N.
    IntActiP0A858. 28 interactors.
    MINTiMINT-1228759.
    STRINGi511145.b3919.

    Structurei

    Secondary structure

    1255
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 9Combined sources5
    Helixi16 – 30Combined sources15
    Beta strandi37 – 41Combined sources5
    Turni44 – 46Combined sources3
    Helixi47 – 54Combined sources8
    Beta strandi57 – 64Combined sources8
    Beta strandi70 – 73Combined sources4
    Helixi80 – 86Combined sources7
    Beta strandi90 – 94Combined sources5
    Helixi96 – 101Combined sources6
    Helixi106 – 118Combined sources13
    Beta strandi122 – 127Combined sources6
    Helixi131 – 135Combined sources5
    Helixi139 – 154Combined sources16
    Helixi156 – 159Combined sources4
    Beta strandi163 – 166Combined sources4
    Helixi169 – 171Combined sources3
    Beta strandi172 – 175Combined sources4
    Helixi180 – 204Combined sources25
    Beta strandi206 – 209Combined sources4
    Turni215 – 217Combined sources3
    Helixi218 – 222Combined sources5
    Beta strandi224 – 226Combined sources3
    Beta strandi229 – 233Combined sources5
    Helixi234 – 237Combined sources4
    Helixi239 – 253Combined sources15

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1TMHX-ray2.80A/B/C/D1-255[»]
    1TREX-ray2.60A/B1-255[»]
    ProteinModelPortaliP0A858.
    SMRiP0A858.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A858.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni9 – 11Substrate bindingUniRule annotation3
    Regioni233 – 234Substrate bindingUniRule annotation2

    Sequence similaritiesi

    Belongs to the triosephosphate isomerase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105CP7. Bacteria.
    COG0149. LUCA.
    HOGENOMiHOG000226413.
    InParanoidiP0A858.
    KOiK01803.
    OMAiWKMNNDL.
    PhylomeDBiP0A858.

    Family and domain databases

    CDDicd00311. TIM. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00147_B. TIM_B. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR022896. TrioseP_Isoase_bac/euk.
    IPR000652. Triosephosphate_isomerase.
    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.

    P0A858-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRHPLVMGNW KLNGSRHMVH ELVSNLRKEL AGVAGCAVAI APPEMYIDMA
    60 70 80 90 100
    KREAEGSHIM LGAQNVDLNL SGAFTGETSA AMLKDIGAQY IIIGHSERRT
    110 120 130 140 150
    YHKESDELIA KKFAVLKEQG LTPVLCIGET EAENEAGKTE EVCARQIDAV
    160 170 180 190 200
    LKTQGAAAFE GAVIAYEPVW AIGTGKSATP AQAQAVHKFI RDHIAKVDAN
    210 220 230 240 250
    IAEQVIIQYG GSVNASNAAE LFAQPDIDGA LVGGASLKAD AFAVIVKAAE

    AAKQA
    Length:255
    Mass (Da):26,972
    Last modified:June 7, 2005 - v1
    Checksum:iE398251020012D94
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti67D → N in CAA25253 (PubMed:6092857).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X00617 Genomic DNA. Translation: CAA25253.1.
    L19201 Genomic DNA. Translation: AAB03051.1.
    U00096 Genomic DNA. Translation: AAC76901.1.
    AP009048 Genomic DNA. Translation: BAE77391.1.
    PIRiB65198. ISECT.
    RefSeqiNP_418354.1. NC_000913.3.
    WP_001216325.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76901; AAC76901; b3919.
    BAE77391; BAE77391; BAE77391.
    GeneIDi948409.
    KEGGiecj:JW3890.
    eco:b3919.
    PATRICi32123351. VBIEscCol129921_4036.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X00617 Genomic DNA. Translation: CAA25253.1.
    L19201 Genomic DNA. Translation: AAB03051.1.
    U00096 Genomic DNA. Translation: AAC76901.1.
    AP009048 Genomic DNA. Translation: BAE77391.1.
    PIRiB65198. ISECT.
    RefSeqiNP_418354.1. NC_000913.3.
    WP_001216325.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1TMHX-ray2.80A/B/C/D1-255[»]
    1TREX-ray2.60A/B1-255[»]
    ProteinModelPortaliP0A858.
    SMRiP0A858.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-31849N.
    IntActiP0A858. 28 interactors.
    MINTiMINT-1228759.
    STRINGi511145.b3919.

    2D gel databases

    SWISS-2DPAGEP0A858.

    Proteomic databases

    EPDiP0A858.
    PaxDbiP0A858.
    PRIDEiP0A858.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76901; AAC76901; b3919.
    BAE77391; BAE77391; BAE77391.
    GeneIDi948409.
    KEGGiecj:JW3890.
    eco:b3919.
    PATRICi32123351. VBIEscCol129921_4036.

    Organism-specific databases

    EchoBASEiEB1008.
    EcoGeneiEG11015. tpiA.

    Phylogenomic databases

    eggNOGiENOG4105CP7. Bacteria.
    COG0149. LUCA.
    HOGENOMiHOG000226413.
    InParanoidiP0A858.
    KOiK01803.
    OMAiWKMNNDL.
    PhylomeDBiP0A858.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00189.
    UPA00138.
    BioCyciEcoCyc:TPI-MONOMER.
    ECOL316407:JW3890-MONOMER.
    MetaCyc:TPI-MONOMER.
    BRENDAi5.3.1.1. 2026.
    SABIO-RKP0A858.

    Miscellaneous databases

    EvolutionaryTraceiP0A858.
    PROiP0A858.

    Family and domain databases

    CDDicd00311. TIM. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00147_B. TIM_B. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR022896. TrioseP_Isoase_bac/euk.
    IPR000652. Triosephosphate_isomerase.
    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...

    Entry informationi

    Entry nameiTPIS_ECOLI
    AccessioniPrimary (citable) accession number: P0A858
    Secondary accession number(s): P04790, Q2M8L5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: June 7, 2005
    Last modified: November 2, 2016
    This is version 109 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, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    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.