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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)DescriptionActionsGraphical viewLength
Binding sitei11SubstrateBy similarity1
Binding sitei13SubstrateBy similarity1
Active sitei95ElectrophileBy similarity1
Active sitei165Proton acceptorBy similarity1

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 databases

ChEMBLiCHEMBL3930.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000901191 – 248Triosephosphate isomeraseAdd BLAST248

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei13N6-acetyllysineBy similarity1
Modified residuei15Deamidated asparagine1 Publication1
Modified residuei67Nitrated tyrosineBy similarity1
Modified residuei71Deamidated asparagine1 Publication1
Modified residuei79PhosphoserineBy similarity1
Modified residuei105PhosphoserineBy similarity1
Cross-linki141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei148N6-succinyllysineBy similarity1
Modified residuei155N6-acetyllysine; alternateBy similarity1
Modified residuei155N6-succinyllysine; alternateBy similarity1
Modified residuei158PhosphoserineBy similarity1
Modified residuei172PhosphothreonineBy similarity1
Modified residuei193N6-acetyllysine; alternateBy similarity1
Modified residuei193N6-methyllysine; alternateBy similarity1
Modified residuei193N6-succinyllysine; alternateBy similarity1
Modified residuei197PhosphoserineBy similarity1
Modified residuei208Nitrated tyrosineBy similarity1
Modified residuei211PhosphoserineBy similarity1
Modified residuei213PhosphothreonineBy similarity1
Modified residuei222PhosphoserineBy similarity1
Modified residuei237N6-acetyllysineBy similarity1

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, Methylation, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP00939.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000019840.

Chemistry databases

BindingDBiP00939.

Structurei

Secondary structure

1248
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 11Combined sources6
Helixi18 – 30Combined sources13
Beta strandi37 – 42Combined sources6
Helixi45 – 47Combined sources3
Helixi48 – 54Combined sources7
Beta strandi59 – 64Combined sources6
Beta strandi68 – 73Combined sources6
Helixi80 – 85Combined sources6
Beta strandi90 – 94Combined sources5
Helixi96 – 100Combined sources5
Helixi106 – 118Combined sources13
Beta strandi122 – 127Combined sources6
Helixi131 – 135Combined sources5
Helixi139 – 152Combined sources14
Helixi157 – 159Combined sources3
Beta strandi160 – 164Combined sources5
Helixi167 – 169Combined sources3
Beta strandi170 – 173Combined sources4
Helixi178 – 195Combined sources18
Helixi198 – 203Combined sources6
Beta strandi206 – 208Combined sources3
Turni214 – 216Combined sources3
Helixi217 – 221Combined sources5
Beta strandi228 – 232Combined sources5
Helixi233 – 236Combined sources4
Helixi239 – 244Combined sources6
Turni245 – 247Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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

CDDicd00311. TIM. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_B. TIM_B. 1 hit.
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.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000019840.

Chemistry databases

BindingDBiP00939.
ChEMBLiCHEMBL3930.

Proteomic databases

PRIDEiP00939.

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

CDDicd00311. TIM. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00147_B. TIM_B. 1 hit.
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...

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: November 2, 2016
This is version 121 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.