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Protein

Triosephosphate isomerase

Gene

tpiA

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).UniRule annotation1 Publication

Catalytic activityi

D-glyceraldehyde 3-phosphate = glycerone phosphate.UniRule annotation

Temperature dependencei

Optimum temperature is 60 degrees Celsius (PubMed:8421318). Thermostable (PubMed:10383424).2 Publications

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.UniRule annotation
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.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Triosephosphate isomerase (tpiA), Triosephosphate isomerase (tpiA), Triosephosphate isomerase (tpiA), Triosephosphate isomerase (tpiA)
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
Active sitei95ElectrophileUniRule annotation2 Publications1
Active sitei167Proton acceptorUniRule annotation1 Publication1
Binding sitei173Substrate; via amide nitrogenUniRule annotation2 Publications1
Binding sitei213SubstrateUniRule annotation2 Publications1

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. 623.
UniPathwayiUPA00109; UER00189.
UPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Triosephosphate isomerase1 PublicationUniRule annotation (EC:5.3.1.1UniRule annotation)
Short name:
TIM1 PublicationUniRule annotation
Short name:
TPI1 PublicationUniRule annotation
Alternative name(s):
Triose-phosphate isomerase1 PublicationUniRule annotation
Gene namesi
Name:tpiAUniRule annotation
Synonyms:tpi
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi13H → N: Displays poor thermostability, with an inactivation temperature of 37 degrees Celsius; when associated with G-14. 1 Publication1
Mutagenesisi14K → G: Displays poor thermostability, with an inactivation temperature of 37 degrees Celsius; when associated with N-13. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000901781 – 253Triosephosphate isomeraseAdd BLAST253

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei213PhosphoserineUniRule annotation1

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Structurei

Secondary structure

1253
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Helixi16 – 26Combined sources11
Turni27 – 29Combined sources3
Turni33 – 35Combined sources3
Beta strandi37 – 42Combined sources6
Helixi44 – 46Combined sources3
Helixi47 – 54Combined sources8
Beta strandi57 – 64Combined sources8
Beta strandi68 – 73Combined sources6
Helixi80 – 86Combined sources7
Beta strandi90 – 94Combined sources5
Helixi96 – 101Combined sources6
Helixi106 – 118Combined sources13
Beta strandi122 – 127Combined sources6
Helixi131 – 135Combined sources5
Helixi139 – 151Combined sources13
Helixi156 – 159Combined sources4
Beta strandi163 – 166Combined sources4
Helixi169 – 171Combined sources3
Turni172 – 174Combined sources3
Helixi180 – 198Combined sources19
Helixi200 – 203Combined sources4
Beta strandi206 – 213Combined sources8
Turni216 – 218Combined sources3
Helixi219 – 223Combined sources5
Beta strandi230 – 234Combined sources5
Helixi235 – 237Combined sources3
Helixi240 – 248Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BTMX-ray2.80A/B2-253[»]
2BTMX-ray2.40A/B2-252[»]
ProteinModelPortaliP00943.
SMRiP00943.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00943.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 11Substrate bindingUniRule annotation2 Publications3
Regioni234 – 235Substrate bindingUniRule annotation2 Publications2

Sequence similaritiesi

Belongs to the triosephosphate isomerase family.UniRule annotation

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.

P00943-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKPIIAGNW KMHKTLAEAV QFVEDVKGHV PPADEVISVV CAPFLFLDRL
60 70 80 90 100
VQAADGTDLK IGAQTMHFAD QGAYTGEVSP VMLKDLGVTY VILGHSERRQ
110 120 130 140 150
MFAETDETVN KKVLAAFTRG LIPIICCGES LEEREAGQTN AVVASQVEKA
160 170 180 190 200
LAGLTPEQVK QAVIAYEPIW AIGTGKSSTP EDANSVCGHI RSVVSRLFGP
210 220 230 240 250
EAAEAIRIQY GGSVKPDNIR DFLAQQQIDG PLVGGASLEP ASFLQLVEAG

RHE
Length:253
Mass (Da):27,206
Last modified:December 1, 1992 - v2
Checksum:i6532B5235362946C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37I → D AA sequence (PubMed:6105959).Curated1
Sequence conflicti41Missing AA sequence (PubMed:6105959).Curated1
Sequence conflicti47 – 48Missing AA sequence (PubMed:6105959).Curated2
Sequence conflicti59L → LQ AA sequence (PubMed:6105959).Curated1
Sequence conflicti100Q → H AA sequence (PubMed:6105959).Curated1
Sequence conflicti135E → Q AA sequence (PubMed:6105959).Curated1
Sequence conflicti138 – 140QTN → ETD AA sequence (PubMed:6105959).Curated3
Sequence conflicti144Missing AA sequence (PubMed:6105959).Curated1
Sequence conflicti157 – 158EQ → QE AA sequence (PubMed:6105959).Curated2
Sequence conflicti161 – 164QAVI → IIL AA sequence (PubMed:6105959).Curated4
Sequence conflicti169I → L AA sequence (PubMed:6105959).Curated1
Sequence conflicti231P → A AA sequence (PubMed:6105959).Curated1
Sequence conflicti248E → Q AA sequence (PubMed:6105959).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66129 Genomic DNA. Translation: CAA46920.1.
PIRiJT0768. ISBSTF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66129 Genomic DNA. Translation: CAA46920.1.
PIRiJT0768. ISBSTF.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BTMX-ray2.80A/B2-253[»]
2BTMX-ray2.40A/B2-252[»]
ProteinModelPortaliP00943.
SMRiP00943.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00189.
UPA00138.
BRENDAi5.3.1.1. 623.

Miscellaneous databases

EvolutionaryTraceiP00943.

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_GEOSE
AccessioniPrimary (citable) accession number: P00943
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 1, 1992
Last modified: November 2, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.