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P00940

- TPIS_CHICK

UniProt

P00940 - TPIS_CHICK

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Protein

Triosephosphate isomerase

Gene

TPI1

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. gluconeogenesis Source: Reactome
  3. glyceraldehyde-3-phosphate metabolic process Source: Ensembl
  4. glycolytic process Source: Reactome
  5. multicellular organismal development Source: Ensembl
  6. pentose-phosphate shunt Source: UniProtKB-KW
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

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
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. nucleus Source: Ensembl
Complete GO annotation...

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[»]
4P61X-ray1.34A/B1-248[»]
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

        10         20         30         40         50
MAPRKFFVGG NWKMNGDKKS LGELIHTLNG AKLSADTEVV CGAPSIYLDF
60 70 80 90 100
ARQKLDAKIG VAAQNCYKVP KGAFTGEISP AMIKDIGAAW VILGHSERRH
110 120 130 140 150
VFGESDELIG QKVAHALAEG LGVIACIGEK LDEREAGITE KVVFEQTKAI
160 170 180 190 200
ADNVKDWSKV VLAYEPVWAI GTGKTATPQQ AQEVHEKLRG WLKSHVSDAV
210 220 230 240
AQSTRIIYGG SVTGGNCKEL ASQHDVDGFL VGGASLKPEF VDIINAKH
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 [» ]
4P61 X-ray 1.34 A/B 1-248 [» ]
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 29, 2014
This is version 126 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