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P00939 (TPIS_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate = glycerone phosphate.

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1.

Subunit structure

Homodimer. Ref.5

Post-translational modification

Asn-15 and Asn-71 undergo deamidation which gives rise to four extra negative charges. These are expected to decrease subunit-subunit interactions and so expose the hydrophobic interface to the aqueous environment.

Sequence similarities

Belongs to the triosephosphate isomerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 248248Triosephosphate isomerase
PRO_0000090119

Sites

Active site951Electrophile By similarity
Active site1651Proton acceptor By similarity Ref.4
Binding site111Substrate By similarity
Binding site131Substrate By similarity

Amino acid modifications

Modified residue131N6-acetyllysine By similarity
Modified residue151Deamidated asparagine Ref.4
Modified residue711Deamidated asparagine Ref.4
Modified residue791Phosphoserine By similarity
Modified residue1871N6-acetyllysine By similarity
Modified residue1931N6-acetyllysine By similarity
Modified residue2371N6-acetyllysine By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P00939 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: E5ADDE9641370D81

FASTA24826,625
        10         20         30         40         50         60 
APSRKFFVGG NWKMNGRKKN LGELITTLNA AKVPADTEVV CAPPTAYIDF ARQKLDPKIA 

        70         80         90        100        110        120 
VAAQNCYKVT NGAFTGEISP GMIKDCGATW VVLGHSERRH VFGESDELIG QKVAHALSEG 

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

       190        200        210        220        230        240 
AQEVHEKLRG WLKSNVSDAV AQSTRIIYGG SVTGATCKEL ASQPDVDGFL VGGASLKPEF 


VDIINAKQ 

« Hide

References

[1]"The amino acid sequence of rabbit muscle triose phosphate isomerase."
Corran P.H., Waley S.G.
Biochem. J. 145:335-344(1975) [PubMed: 1171682] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing."
Putney S.D., Herlihy W.C., Schimmel P.R.
Nature 302:718-721(1983) [PubMed: 6687628] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 56-83.
[3]"Haloacetol phosphates. Characterization of the active site of rabbit muscle triose phosphate isomerase."
Hartman F.C.
Biochemistry 10:146-154(1971) [PubMed: 4922541] [Abstract]
Cited for: ACTIVE SITE.
[4]"Terminal marking of triosephosphate isomerase: consequences of deamidation."
Sun A.-Q., Yueksel U., Gracy R.W.
Arch. Biochem. Biophys. 322:361-368(1995) [PubMed: 7574709] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, DEAMIDATION AT ASN-15 AND ASN-71.
[5]"Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity."
Aparicio R., Ferreira S.T., Polikarpov I.
J. Mol. Biol. 334:1023-1041(2003) [PubMed: 14643664] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), HOMODIMERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00902 mRNA. Translation: CAA24267.1.
PIRISRBT. A01165.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R2RX-ray1.50A/B/C/D1-248[»]
1R2SX-ray2.85A/B/C/D1-248[»]
1R2TX-ray2.25A/B1-248[»]
ProteinModelPortalP00939.
SMRP00939. Positions 2-248.
ModBaseSearch...

Protein-protein interaction databases

STRINGP00939.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

GeneTreeENSGT00390000013354.
HOVERGENHBG002599.
OrthoDBEOG40S0GF.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR21139. Triophos_ismrse. 1 hit.
PfamPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMSSF51351. Triophos_ismrse. 1 hit.
TIGRFAMsTIGR00419. Tim. 1 hit.
PROSITEPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB01093. Dimethyl sulfoxide.

Entry information

Entry nameTPIS_RABIT
AccessionPrimary (citable) accession number: P00939
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 16, 2011
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families