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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)
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
Active sitei95 – 951ElectrophileUniRule annotation2 Publications
Active sitei167 – 1671Proton acceptorUniRule annotation1 Publication
Binding sitei173 – 1731Substrate; via amide nitrogenUniRule annotation2 Publications
Binding sitei213 – 2131SubstrateUniRule annotation2 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131H → N: Displays poor thermostability, with an inactivation temperature of 37 degrees Celsius; when associated with G-14. 1 Publication
Mutagenesisi14 – 141K → G: Displays poor thermostability, with an inactivation temperature of 37 degrees Celsius; when associated with N-13. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 253253Triosephosphate isomerasePRO_0000090178Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei213 – 2131PhosphoserineUniRule annotation

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Structurei

Secondary structure

1
253
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Helixi16 – 2611Combined sources
Turni27 – 293Combined sources
Turni33 – 353Combined sources
Beta strandi37 – 426Combined sources
Helixi44 – 463Combined sources
Helixi47 – 548Combined sources
Beta strandi57 – 648Combined sources
Beta strandi68 – 736Combined sources
Helixi80 – 867Combined sources
Beta strandi90 – 945Combined sources
Helixi96 – 1016Combined sources
Helixi106 – 11813Combined sources
Beta strandi122 – 1276Combined sources
Helixi131 – 1355Combined sources
Helixi139 – 15113Combined sources
Helixi156 – 1594Combined sources
Beta strandi163 – 1664Combined sources
Helixi169 – 1713Combined sources
Turni172 – 1743Combined sources
Helixi180 – 19819Combined sources
Helixi200 – 2034Combined sources
Beta strandi206 – 2138Combined sources
Turni216 – 2183Combined sources
Helixi219 – 2235Combined sources
Beta strandi230 – 2345Combined sources
Helixi235 – 2373Combined sources
Helixi240 – 2489Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00943.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 113Substrate bindingUniRule annotation2 Publications
Regioni234 – 2352Substrate bindingUniRule annotation2 Publications

Sequence similaritiesi

Belongs to the triosephosphate isomerase family.UniRule annotation

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371I → D AA sequence (PubMed:6105959).Curated
Sequence conflicti41 – 411Missing AA sequence (PubMed:6105959).Curated
Sequence conflicti47 – 482Missing AA sequence (PubMed:6105959).Curated
Sequence conflicti59 – 591L → LQ AA sequence (PubMed:6105959).Curated
Sequence conflicti100 – 1001Q → H AA sequence (PubMed:6105959).Curated
Sequence conflicti135 – 1351E → Q AA sequence (PubMed:6105959).Curated
Sequence conflicti138 – 1403QTN → ETD AA sequence (PubMed:6105959).Curated
Sequence conflicti144 – 1441Missing AA sequence (PubMed:6105959).Curated
Sequence conflicti157 – 1582EQ → QE AA sequence (PubMed:6105959).Curated
Sequence conflicti161 – 1644QAVI → IIL AA sequence (PubMed:6105959).Curated
Sequence conflicti169 – 1691I → L AA sequence (PubMed:6105959).Curated
Sequence conflicti231 – 2311P → A AA sequence (PubMed:6105959).Curated
Sequence conflicti248 – 2481E → Q AA sequence (PubMed:6105959).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1BTMX-ray2.80A/B2-253[»]
2BTMX-ray2.40A/B2-252[»]
ProteinModelPortaliP00943.
SMRiP00943. Positions 2-252.
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

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. "Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein sequences."
    Rentier-Delrue F., Mande S.C., Moyens S., Terpstra P., Mainfroid V., Goraj K., Lion M., Hol W.G.J., Martial J.A.
    J. Mol. Biol. 229:85-93(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  2. "Sequence of the triosephosphate isomerase-encoding gene isolated from the thermophile Bacillus stearothermophilus."
    Rentier-Delrue F., Moyens S., Lion M., Martial J.A.
    Gene 134:137-138(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Primary structure of triosephosphate isomerase from Bacillus stearothermophilus."
    Artavanis-Tsakonas S., Harris J.I.
    Eur. J. Biochem. 108:599-611(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE.
  4. "Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions."
    Delboni L.F., Mande S.C., Rentier-Delrue F., Mainfroid V., Turley S., Vellieux F.M.D., Martial J.A., Hol W.G.J.
    Protein Sci. 4:2594-2604(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT.
  5. "Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures."
    Alvarez M., Wouters J., Maes D., Mainfroid V., Rentier-Delrue F., Wyns L., Depiereux E., Martial J.A.
    J. Biol. Chem. 274:19181-19187(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT ASN-13 AND GLY-14 IN COMPLEX WITH SUBSTRATE ANALOG, MUTAGENESIS OF HIS-13 AND LYS-14, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

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: March 16, 2016
This is version 109 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.