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B1XB85 (TPIS_ECODH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:tpiA
Ordered Locus Names:ECDH10B_4108
OrganismEscherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP]
Taxonomic identifier316385 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate = glycerone phosphate. HAMAP-Rule MF_00147

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP-Rule MF_00147

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. HAMAP-Rule MF_00147

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00147

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00147.

Sequence similarities

Belongs to the triosephosphate isomerase family.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
Pentose shunt
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glycolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontriose-phosphate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 255255Triosephosphate isomerase HAMAP-Rule MF_00147
PRO_1000096495

Sites

Active site951Electrophile By similarity
Active site1671Proton acceptor By similarity
Binding site91Substrate By similarity
Binding site111Substrate By similarity

Secondary structure

................................................. 255
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
B1XB85 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: E398251020012D94

FASTA25526,972
        10         20         30         40         50         60 
MRHPLVMGNW KLNGSRHMVH ELVSNLRKEL AGVAGCAVAI APPEMYIDMA KREAEGSHIM 

        70         80         90        100        110        120 
LGAQNVDLNL SGAFTGETSA AMLKDIGAQY IIIGHSERRT YHKESDELIA KKFAVLKEQG 

       130        140        150        160        170        180 
LTPVLCIGET EAENEAGKTE EVCARQIDAV LKTQGAAAFE GAVIAYEPVW AIGTGKSATP 

       190        200        210        220        230        240 
AQAQAVHKFI RDHIAKVDAN IAEQVIIQYG GSVNASNAAE LFAQPDIDGA LVGGASLKAD 

       250 
AFAVIVKAAE AAKQA 

« Hide

References

[1]"The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse."
Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R.
J. Bacteriol. 190:2597-2606(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / DH10B.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000948 Genomic DNA. Translation: ACB04931.1.
RefSeqYP_001732709.1. NC_010473.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IOTX-ray1.85A/B1-255[»]
ProteinModelPortalB1XB85.
SMRB1XB85. Positions 1-255.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316385.ECDH10B_4108.

Proteomic databases

PRIDEB1XB85.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB04931; ACB04931; ECDH10B_4108.
GeneID6061229.
KEGGecd:ECDH10B_4108.
PATRIC18468207. VBIEscCol59506_4140.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0149.
HOGENOMHOG000226413.
KOK01803.
OMAAKLGCTF.
OrthoDBEOG66QM23.
ProtClustDBPRK00042.

Enzyme and pathway databases

BioCycECOL316385:GJ8B-3929-MONOMER.
UniPathwayUPA00109; UER00189.
UPA00138.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00147_B. TIM_B.
InterProIPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
PANTHERPTHR21139. PTHR21139. 1 hit.
PfamPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMSSF51351. SSF51351. 1 hit.
TIGRFAMsTIGR00419. tim. 1 hit.
PROSITEPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTPIS_ECODH
AccessionPrimary (citable) accession number: B1XB85
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways