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Protein

Triosephosphate isomerase

Gene

tpiA

Organism
Moritella marina (Vibrio marinus)
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 420000 min(-1) for isomerase activity with D-glyceraldehyde 3-phosphate as substrate (at pH 7.6 and 10 degrees Celsius).1 Publication

Manual assertion based on experiment ini

  1. KM=1.9 mM for D-glyceraldehyde 3-phosphate (at pH 7.6 and 10 degrees Celsius)1 Publication

    Temperature dependencei

    Optimum temperature is 15 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 sitei97ElectrophileUniRule annotation1 Publication1
    Active sitei169Proton acceptorUniRule annotation1
    Binding sitei175Substrate; via amide nitrogenUniRule annotation1 Publication1
    Binding sitei214SubstrateUniRule annotation1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Gluconeogenesis, Glycolysis, Pentose shunt

    Enzyme and pathway databases

    BRENDAi5.3.1.1. 6633.
    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 isomerase1 PublicationUniRule annotation
    Gene namesi
    Name:tpiA1 PublicationUniRule annotation
    Synonyms:tim, tpi
    OrganismiMoritella marina (Vibrio marinus)
    Taxonomic identifieri90736 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesMoritellaceaeMoritella

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi238A → S: Reduces catalytic efficiency and affinity, but increases thermal stability. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000903141 – 256Triosephosphate isomeraseAdd BLAST256

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Structurei

    Secondary structure

    1256
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 9Combined sources5
    Helixi16 – 29Combined sources14
    Turni30 – 32Combined sources3
    Beta strandi35 – 41Combined sources7
    Helixi44 – 46Combined sources3
    Helixi47 – 57Combined sources11
    Beta strandi62 – 66Combined sources5
    Beta strandi72 – 75Combined sources4
    Helixi82 – 87Combined sources6
    Beta strandi92 – 96Combined sources5
    Helixi98 – 103Combined sources6
    Helixi108 – 120Combined sources13
    Beta strandi124 – 129Combined sources6
    Helixi133 – 137Combined sources5
    Helixi141 – 156Combined sources16
    Helixi158 – 161Combined sources4
    Beta strandi165 – 168Combined sources4
    Turni171 – 175Combined sources5
    Helixi182 – 197Combined sources16
    Helixi201 – 206Combined sources6
    Beta strandi208 – 211Combined sources4
    Turni217 – 219Combined sources3
    Helixi220 – 223Combined sources4
    Beta strandi231 – 235Combined sources5
    Helixi236 – 239Combined sources4
    Helixi241 – 254Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1AW1X-ray2.70A/B/D/E/G/H/J/K1-256[»]
    1AW2X-ray2.65A/B/D/E/G/H/J/K1-256[»]
    ProteinModelPortaliP50921.
    SMRiP50921.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50921.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni9 – 11Substrate bindingUniRule annotation1 Publication3
    Regioni235 – 236Substrate bindingUniRule annotation1 Publication2

    Sequence similaritiesi

    Belongs to the triosephosphate isomerase family.UniRule annotation

    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.

    P50921-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRHPVVMGNW KLNGSKEMVV DLLNGLNAEL EGVTGVDVAV APPALFVDLA
    60 70 80 90 100
    ERTLTEAGSA IILGAQNTDL NNSGAFTGDM SPAMLKEFGA THIIIGHSER
    110 120 130 140 150
    REYHAESDEF VAKKFAFLKE NGLTPVLCIG ESDAQNEAGE TMAVCARQLD
    160 170 180 190 200
    AVINTQGVEA LEGAIIAYEP IWAIGTGKAA TAEDAQRIHA QIRAHIAEKS
    210 220 230 240 250
    EAVAKNVVIQ YGGSVKPENA AAYFAQPDID GALVGGAALD AKSFAAIAKA

    AAEAKA
    Length:256
    Mass (Da):26,740
    Last modified:October 1, 1996 - v1
    Checksum:i5CC4BB8CFF27070A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U48935 Genomic DNA. Translation: AAA88910.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U48935 Genomic DNA. Translation: AAA88910.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1AW1X-ray2.70A/B/D/E/G/H/J/K1-256[»]
    1AW2X-ray2.65A/B/D/E/G/H/J/K1-256[»]
    ProteinModelPortaliP50921.
    SMRiP50921.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00189.
    UPA00138.
    BRENDAi5.3.1.1. 6633.

    Miscellaneous databases

    EvolutionaryTraceiP50921.

    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_MORMI
    AccessioniPrimary (citable) accession number: P50921
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: November 2, 2016
    This is version 95 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

    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.