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Protein

Triosephosphate isomerase

Gene

TPI1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glyceraldehyde 3-phosphate = glycerone phosphate.

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
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.
Proteins known to be involved in this subpathway in this organism are:
  1. Triosephosphate isomerase (TPI1), Triosephosphate isomerase (TPI1)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111SubstrateBy similarity
Binding sitei13 – 131SubstrateBy similarity
Active sitei95 – 951ElectrophileBy similarity
Active sitei165 – 1651Proton acceptorBy similarity

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. 1749.
SABIO-RKP00939.
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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3930.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 248248Triosephosphate isomerasePRO_0000090119Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131N6-acetyllysineBy similarity
Modified residuei15 – 151Deamidated asparagine1 Publication
Modified residuei67 – 671Nitrated tyrosineBy similarity
Modified residuei71 – 711Deamidated asparagine1 Publication
Modified residuei79 – 791PhosphoserineBy similarity
Modified residuei105 – 1051PhosphoserineBy similarity
Cross-linki141 – 141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei148 – 1481N6-succinyllysineBy similarity
Modified residuei155 – 1551N6-acetyllysine; alternateBy similarity
Modified residuei155 – 1551N6-succinyllysine; alternateBy similarity
Modified residuei158 – 1581PhosphoserineBy similarity
Modified residuei172 – 1721PhosphothreonineBy similarity
Modified residuei193 – 1931N6-acetyllysine; alternateBy similarity
Modified residuei193 – 1931N6-succinyllysine; alternateBy similarity
Modified residuei197 – 1971PhosphoserineBy similarity
Modified residuei208 – 2081Nitrated tyrosineBy similarity
Modified residuei211 – 2111PhosphoserineBy similarity
Modified residuei213 – 2131PhosphothreonineBy similarity
Modified residuei222 – 2221PhosphoserineBy similarity
Modified residuei237 – 2371N6-acetyllysineBy similarity

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Nitration, Phosphoprotein, Ubl conjugation

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000019840.

Chemistry

BindingDBiP00939.

Structurei

Secondary structure

1
248
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116Combined sources
Helixi18 – 3013Combined sources
Beta strandi37 – 426Combined sources
Helixi45 – 473Combined sources
Helixi48 – 547Combined sources
Beta strandi59 – 646Combined sources
Beta strandi68 – 736Combined sources
Helixi80 – 856Combined sources
Beta strandi90 – 945Combined sources
Helixi96 – 1005Combined sources
Helixi106 – 11813Combined sources
Beta strandi122 – 1276Combined sources
Helixi131 – 1355Combined sources
Helixi139 – 15214Combined sources
Helixi157 – 1593Combined sources
Beta strandi160 – 1645Combined sources
Helixi167 – 1693Combined sources
Beta strandi170 – 1734Combined sources
Helixi178 – 19518Combined sources
Helixi198 – 2036Combined sources
Beta strandi206 – 2083Combined sources
Turni214 – 2163Combined sources
Helixi217 – 2215Combined sources
Beta strandi228 – 2325Combined sources
Helixi233 – 2364Combined sources
Helixi239 – 2446Combined sources
Turni245 – 2473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R2RX-ray1.50A/B/C/D1-248[»]
1R2SX-ray2.85A/B/C/D1-248[»]
1R2TX-ray2.25A/B1-248[»]
4OWGX-ray1.55A/B1-248[»]
ProteinModelPortaliP00939.
SMRiP00939. Positions 2-248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00939.

Family & Domainsi

Sequence similaritiesi

Belongs to the triosephosphate isomerase family.Curated

Phylogenomic databases

eggNOGiKOG1643. Eukaryota.
COG0149. LUCA.
HOGENOMiHOG000226413.
HOVERGENiHBG002599.
InParanoidiP00939.

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.

P00939-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
APSRKFFVGG NWKMNGRKKN LGELITTLNA AKVPADTEVV CAPPTAYIDF
60 70 80 90 100
ARQKLDPKIA VAAQNCYKVT NGAFTGEISP GMIKDCGATW VVLGHSERRH
110 120 130 140 150
VFGESDELIG QKVAHALSEG LGVIACIGEK LDEREAGITE KVVFEQTKVI
160 170 180 190 200
ADNVKDWSKV VLAYEPVWAI GTGKTATPQQ AQEVHEKLRG WLKSNVSDAV
210 220 230 240
AQSTRIIYGG SVTGATCKEL ASQPDVDGFL VGGASLKPEF VDIINAKQ
Length:248
Mass (Da):26,625
Last modified:July 21, 1986 - v1
Checksum:iE5ADDE9641370D81
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00902 mRNA. Translation: CAA24267.1.
PIRiA01165. ISRBT.
UniGeneiOcu.398.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00902 mRNA. Translation: CAA24267.1.
PIRiA01165. ISRBT.
UniGeneiOcu.398.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R2RX-ray1.50A/B/C/D1-248[»]
1R2SX-ray2.85A/B/C/D1-248[»]
1R2TX-ray2.25A/B1-248[»]
4OWGX-ray1.55A/B1-248[»]
ProteinModelPortaliP00939.
SMRiP00939. Positions 2-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000019840.

Chemistry

BindingDBiP00939.
ChEMBLiCHEMBL3930.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1643. Eukaryota.
COG0149. LUCA.
HOGENOMiHOG000226413.
HOVERGENiHBG002599.
InParanoidiP00939.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00189.
UPA00138.
BRENDAi5.3.1.1. 1749.
SABIO-RKP00939.

Miscellaneous databases

EvolutionaryTraceiP00939.

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]
ProtoNetiSearch...

Publicationsi

  1. "The amino acid sequence of rabbit muscle triose phosphate isomerase."
    Corran P.H., Waley S.G.
    Biochem. J. 145:335-344(1975) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), HOMODIMERIZATION.

Entry informationi

Entry nameiTPIS_RABIT
AccessioniPrimary (citable) accession number: P00939
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 118 of the entry and version 1 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

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.