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P00940 (TPIS_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Triosephosphate isomerase

Short name=TIM
EC=5.3.1.1
Alternative name(s):
Triose-phosphate isomerase
Gene names
Name:TPI1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 248247Triosephosphate isomerase HAMAP-Rule MF_00147_B
PRO_0000090121

Sites

Active site951Electrophile
Active site1651Proton acceptor
Binding site131Substrate

Experimental info

Mutagenesis951H → N: Reduces activity 5000-fold. Ref.5
Mutagenesis1651E → D: Reduces activity 300-fold. Ref.5
Sequence conflict17 – 182DK → KR AA sequence Ref.3
Sequence conflict291N → D AA sequence Ref.3
Sequence conflict145 – 1462EQ → QE AA sequence Ref.3
Sequence conflict1941S → T AA sequence Ref.3
Sequence conflict202 – 2043QST → VQS AA sequence Ref.3

Secondary structure

................................................. 248
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00940 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AFCC258E574DE982

FASTA24826,620
        10         20         30         40         50         60 
MAPRKFFVGG NWKMNGDKKS LGELIHTLNG AKLSADTEVV CGAPSIYLDF ARQKLDAKIG 

        70         80         90        100        110        120 
VAAQNCYKVP KGAFTGEISP AMIKDIGAAW VILGHSERRH VFGESDELIG QKVAHALAEG 

       130        140        150        160        170        180 
LGVIACIGEK LDEREAGITE KVVFEQTKAI ADNVKDWSKV VLAYEPVWAI GTGKTATPQQ 

       190        200        210        220        230        240 
AQEVHEKLRG WLKSHVSDAV AQSTRIIYGG SVTGGNCKEL ASQHDVDGFL VGGASLKPEF 


VDIINAKH 

« Hide

References

[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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11314 mRNA. Translation: AAA49094.1.
M11941 Genomic DNA. Translation: AAA49095.1.
PIRISCHT. A23448.
RefSeqNP_990782.1. NM_205451.1.
UniGeneGga.4148.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP00940.
SMRP00940. Positions 2-248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676684. 1 interaction.
IntActP00940. 1 interaction.
STRING9031.ENSGALP00000023396.

Proteomic databases

PaxDbP00940.
PRIDEP00940.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000023442; ENSGALP00000023396; ENSGALG00000014526.
GeneID396435.
KEGGgga:396435.

Organism-specific databases

CTD7167.

Phylogenomic databases

eggNOGCOG0149.
GeneTreeENSGT00390000013354.
HOGENOMHOG000226413.
HOVERGENHBG002599.
InParanoidP00940.
KOK01803.
OMAPAIYLDQ.
OrthoDBEOG76DTT8.
PhylomeDBP00940.
TreeFamTF300829.

Enzyme and pathway databases

ReactomeREACT_115655. Metabolism.
SABIO-RKP00940.
UniPathwayUPA00109; UER00189.
UPA00138.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00147_B. TIM_B.
InterProIPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
PANTHERPTHR21139. PTHR21139. 1 hit.
PfamPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMSSF51351. SSF51351. 1 hit.
TIGRFAMsTIGR00419. tim. 1 hit.
PROSITEPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00940.
NextBio20816476.
PROP00940.

Entry information

Entry nameTPIS_CHICK
AccessionPrimary (citable) accession number: P00940
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways