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Reviewed, UniProtKB/Swiss-Prot Q0A773 (TPIS_ALHEH)

Last modified February 9, 2010. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Mlg_1972
OrganismAlkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeAlkalilimnicola

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_00147

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

Subunit structure

Homodimer By similarity. HAMAP MF_00147

Subcellular location

Cytoplasm Probable HAMAP MF_00147.

Sequence similarities

Belongs to the triosephosphate isomerase family.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
Pentose shunt
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processgluconeogenesis

Inferred from electronic annotation. Source: HAMAP

glycolysis

Inferred from electronic annotation. Source: HAMAP

pentose-phosphate shunt

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontriose-phosphate isomerase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 250250Triosephosphate isomerase HAMAP MF_00147
PRO_0000307422

Sites

Active site941Electrophile By similarity
Active site1651Proton acceptor By similarity
Binding site91Substrate By similarity
Binding site111Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0A773-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 75DFB29834414F59

FASTA25026,220
        10         20         30         40         50         60 
MRKPMVAGNW KMNGSLALVN DMGRALADVD CSAVDVLVCP PFPYIGPLRR AVPDESGVAL 

        70         80         90        100        110        120 
GGQDVSRYDS GAYTGEVAGA MLAEMGCRHV IVGHSERRAM HAETDEVVVD KVQAALRAGL 

       130        140        150        160        170        180 
TPIVCVGETL EARDAGETEQ VVGRQLDAVL ELGGFVVEKL VLAYEPVWAI GTGRTASPEQ 

       190        200        210        220        230        240 
AQAVHAFIRQ RAADALGDEL AQRLPILYGG SVKPGNAREL FGCADVDGGL IGGASLDPDG 

       250 
FLEIISAARP 

« Hide

References

[1]"Complete sequence of Alkalilimnicola ehrilichei MLHE-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000453 Genomic DNA. Translation: ABI57314.1.
RefSeqYP_742804.1.

3D structure databases

SMRQ0A773. Positions 1-249.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0A773.

Genome annotation databases

GeneID4268515.
GenomeReviewsGene locus Mlg_1972 in contig CP000453_GR.
KEGGaeh:Mlg_1972.
NMPDRfig|187272.6.peg.1879.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0149.
HOGENOMHBG708281.
OMADIRSVQT.
PhylomeDBQ0A773.

Family and domain databases

HAMAPMF_00147_B. TIM_B.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR21139. Triophos_ismrse. 1 hit.
PfamPF00121. TIM. 1 hit.
[Graphical view]
TIGRFAMsTIGR00419. tim. 1 hit.
PROSITEPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTPIS_ALHEH
AccessionPrimary (citable) accession number: Q0A773
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 17, 2006
Last modified: February 9, 2010
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents