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P00940

- TPIS_CHICK

UniProt

P00940 - TPIS_CHICK

Protein

Triosephosphate isomerase

Gene

TPI1

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    D-glyceraldehyde 3-phosphate = glycerone phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei13 – 131Substrate
    Active sitei95 – 951Electrophile
    Active sitei165 – 1651Proton acceptor

    GO - Molecular functioni

    1. triose-phosphate isomerase activity Source: Reactome

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. embryo development Source: Ensembl
    3. gluconeogenesis Source: Reactome
    4. glyceraldehyde-3-phosphate metabolic process Source: Ensembl
    5. glycolytic process Source: Reactome
    6. pentose-phosphate shunt Source: UniProtKB-KW
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Gluconeogenesis, Glycolysis, Pentose shunt

    Enzyme and pathway databases

    ReactomeiREACT_115534. Gluconeogenesis.
    REACT_115767. Glycolysis.
    SABIO-RKP00940.
    UniPathwayiUPA00109; UER00189.
    UPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Triosephosphate isomerase (EC:5.3.1.1)
    Short name:
    TIM
    Alternative name(s):
    Triose-phosphate isomerase
    Gene namesi
    Name:TPI1
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Chromosome 1

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi95 – 951H → N: Reduces activity 5000-fold. 1 Publication
    Mutagenesisi165 – 1651E → D: Reduces activity 300-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 248247Triosephosphate isomerasePRO_0000090121Add
    BLAST

    Proteomic databases

    PaxDbiP00940.
    PRIDEiP00940.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi676684. 1 interaction.
    IntActiP00940. 1 interaction.
    STRINGi9031.ENSGALP00000023396.

    Structurei

    Secondary structure

    1
    248
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 116
    Helixi18 – 3013
    Beta strandi37 – 426
    Helixi45 – 473
    Helixi48 – 547
    Beta strandi59 – 646
    Beta strandi68 – 736
    Helixi80 – 856
    Beta strandi90 – 945
    Helixi96 – 1005
    Helixi106 – 11813
    Beta strandi122 – 1276
    Helixi131 – 1355
    Helixi139 – 15113
    Helixi157 – 1593
    Beta strandi160 – 1645
    Helixi167 – 1693
    Beta strandi170 – 1734
    Helixi178 – 19518
    Helixi198 – 2036
    Beta strandi206 – 2116
    Turni214 – 2163
    Helixi217 – 2215
    Beta strandi228 – 2325
    Helixi233 – 2364
    Helixi240 – 2445
    Turni245 – 2473

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SPQX-ray2.16A/B2-248[»]
    1SQ7X-ray2.85A/B2-248[»]
    1SSDX-ray2.90A/B2-248[»]
    1SSGX-ray2.90A/B2-248[»]
    1SU5X-ray2.70A/B2-248[»]
    1SW0X-ray1.71A/B1-248[»]
    1SW3X-ray2.03A/B1-248[»]
    1SW7X-ray2.22A/B1-248[»]
    1TIMX-ray2.50A/B2-248[»]
    1TPBX-ray1.901/22-248[»]
    1TPCX-ray1.901/22-248[»]
    1TPHX-ray1.801/22-248[»]
    1TPUX-ray1.90A/B2-248[»]
    1TPVX-ray1.90A/B2-248[»]
    1TPWX-ray1.90A/B2-248[»]
    8TIMX-ray2.50A/B2-248[»]
    ProteinModelPortaliP00940.
    SMRiP00940. Positions 2-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00940.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the triosephosphate isomerase family.Curated

    Phylogenomic databases

    eggNOGiCOG0149.
    GeneTreeiENSGT00390000013354.
    HOGENOMiHOG000226413.
    HOVERGENiHBG002599.
    InParanoidiP00940.
    KOiK01803.
    OMAiPAIYLDQ.
    OrthoDBiEOG76DTT8.
    PhylomeDBiP00940.
    TreeFamiTF300829.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00147_B. TIM_B.
    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.

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

    P00940-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPRKFFVGG NWKMNGDKKS LGELIHTLNG AKLSADTEVV CGAPSIYLDF    50
    ARQKLDAKIG VAAQNCYKVP KGAFTGEISP AMIKDIGAAW VILGHSERRH 100
    VFGESDELIG QKVAHALAEG LGVIACIGEK LDEREAGITE KVVFEQTKAI 150
    ADNVKDWSKV VLAYEPVWAI GTGKTATPQQ AQEVHEKLRG WLKSHVSDAV 200
    AQSTRIIYGG SVTGGNCKEL ASQHDVDGFL VGGASLKPEF VDIINAKH 248
    Length:248
    Mass (Da):26,620
    Last modified:January 23, 2007 - v2
    Checksum:iAFCC258E574DE982
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 182DK → KR AA sequence (PubMed:4463937)Curated
    Sequence conflicti29 – 291N → D AA sequence (PubMed:4463937)Curated
    Sequence conflicti145 – 1462EQ → QE AA sequence (PubMed:4463937)Curated
    Sequence conflicti194 – 1941S → T AA sequence (PubMed:4463937)Curated
    Sequence conflicti202 – 2043QST → VQS AA sequence (PubMed:4463937)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11314 mRNA. Translation: AAA49094.1.
    M11941 Genomic DNA. Translation: AAA49095.1.
    PIRiA23448. ISCHT.
    RefSeqiNP_990782.1. NM_205451.1.
    UniGeneiGga.4148.

    Genome annotation databases

    EnsembliENSGALT00000023442; ENSGALP00000023396; ENSGALG00000014526.
    GeneIDi396435.
    KEGGigga:396435.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11314 mRNA. Translation: AAA49094.1 .
    M11941 Genomic DNA. Translation: AAA49095.1 .
    PIRi A23448. ISCHT.
    RefSeqi NP_990782.1. NM_205451.1.
    UniGenei Gga.4148.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SPQ X-ray 2.16 A/B 2-248 [» ]
    1SQ7 X-ray 2.85 A/B 2-248 [» ]
    1SSD X-ray 2.90 A/B 2-248 [» ]
    1SSG X-ray 2.90 A/B 2-248 [» ]
    1SU5 X-ray 2.70 A/B 2-248 [» ]
    1SW0 X-ray 1.71 A/B 1-248 [» ]
    1SW3 X-ray 2.03 A/B 1-248 [» ]
    1SW7 X-ray 2.22 A/B 1-248 [» ]
    1TIM X-ray 2.50 A/B 2-248 [» ]
    1TPB X-ray 1.90 1/2 2-248 [» ]
    1TPC X-ray 1.90 1/2 2-248 [» ]
    1TPH X-ray 1.80 1/2 2-248 [» ]
    1TPU X-ray 1.90 A/B 2-248 [» ]
    1TPV X-ray 1.90 A/B 2-248 [» ]
    1TPW X-ray 1.90 A/B 2-248 [» ]
    8TIM X-ray 2.50 A/B 2-248 [» ]
    ProteinModelPortali P00940.
    SMRi P00940. Positions 2-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 676684. 1 interaction.
    IntActi P00940. 1 interaction.
    STRINGi 9031.ENSGALP00000023396.

    Proteomic databases

    PaxDbi P00940.
    PRIDEi P00940.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSGALT00000023442 ; ENSGALP00000023396 ; ENSGALG00000014526 .
    GeneIDi 396435.
    KEGGi gga:396435.

    Organism-specific databases

    CTDi 7167.

    Phylogenomic databases

    eggNOGi COG0149.
    GeneTreei ENSGT00390000013354.
    HOGENOMi HOG000226413.
    HOVERGENi HBG002599.
    InParanoidi P00940.
    KOi K01803.
    OMAi PAIYLDQ.
    OrthoDBi EOG76DTT8.
    PhylomeDBi P00940.
    TreeFami TF300829.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00189 .
    UPA00138 .
    Reactomei REACT_115534. Gluconeogenesis.
    REACT_115767. Glycolysis.
    SABIO-RK P00940.

    Miscellaneous databases

    EvolutionaryTracei P00940.
    NextBioi 20816476.
    PROi P00940.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00147_B. TIM_B.
    InterProi IPR013785. Aldolase_TIM.
    IPR022896. TrioseP_Isoase_bac/euk.
    IPR000652. Triosephosphate_isomerase.
    IPR020861. Triosephosphate_isomerase_AS.
    [Graphical view ]
    PANTHERi PTHR21139. PTHR21139. 1 hit.
    Pfami PF00121. TIM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51351. SSF51351. 1 hit.
    TIGRFAMsi TIGR00419. tim. 1 hit.
    PROSITEi PS00171. TIM_1. 1 hit.
    PS51440. TIM_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Chicken triosephosphate isomerase complements an Escherichia coli deficiency."
      Straus D., Gilbert W.
      Proc. Natl. Acad. Sci. U.S.A. 82:2014-2018(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Genetic engineering in the Precambrian: structure of the chicken triosephosphate isomerase gene."
      Straus D., Gilbert W.
      Mol. Cell. Biol. 5:3497-3506(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Studies on the subunit structure and amino acid sequence of trisoe phosphate isomerase from chicken breast muscle."
      Furth A.J., Milman J.D., Priddle J.D., Offord R.E.
      Biochem. J. 139:11-22(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-248.
    4. "Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5-A resolution using amino acid sequence data."
      Banner D.W., Bloomer A.C., Petsko G.A., Phillips D.C., Pogson C.I., Wilson I.A., Corran P.H., Furth A.J., Milman J.D., Offord R.E., Priddle J.D., Waley S.G.
      Nature 255:609-614(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SEQUENCE REVISION.
    5. "How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases."
      Blacklow S.C., Knowles J.R.
      Biochemistry 29:4099-4108(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MUTAGENESIS OF HIS-95 AND GLU-165.
    6. "Atomic coordinates for triose phosphate isomerase from chicken muscle."
      Banner D.W., Bloomer A.C., Petsko G.A., Phillips D.C., Wilson I.A.
      Biochem. Biophys. Res. Commun. 72:146-155(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    7. "Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase."
      Wierenga R.K., Noble M.E.M., Davenport R.C.
      J. Mol. Biol. 224:1115-1126(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPARISON OF X-RAY STRUCTURES.
    8. "Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution."
      Zhang Z., Sugio S., Komives E.A., Liu K.D., Knowles J.R., Petsko G.A., Ringe D.
      Biochemistry 33:2830-2837(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ASP-165 IN COMPLEX WITH SUBSTRATE ANALOG.
    9. Artymiuk P.J., Taylor W.R., Phillips D.C.
      Submitted (AUG-1998) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiTPIS_CHICK
    AccessioniPrimary (citable) accession number: P00940
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    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

    External Data

    Dasty 3