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Reviewed, UniProtKB/Swiss-Prot Q723V9 (TPIS2_LISMF)

Last modified November 3, 2009. Version 38. 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 2
      Short name=TIM 2
    EC=5.3.1.1
Alternative name(s):
    Triose-phosphate isomerase 2
Gene names
Name: tpiA2
Ordered Locus Names: LMOf2365_0366
OrganismListeria monocytogenes serotype 4b (strain F2365) [Complete proteome] [HAMAP]
Taxonomic identifier265669 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesListeriaceaeListeria

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Subcellular location

Cytoplasm Probable.

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 – 254254Triosephosphate isomerase 2 HAMAP MF_00147
PRO_0000090241

Sites

Active site961Electrophile By similarity
Active site1681Proton acceptor By similarity
Binding site91Substrate By similarity
Binding site111Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q723V9-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 142D35B5BD7963C0

FASTA25428,083
        10         20         30         40         50         60 
MRKPLVGINM KNYINTRAQT SEWLEATIPL LKNFSDVDTF IFPSMGTLET TANLLAGTSF 

        70         80         90        100        110        120 
GFGPQNMAPE KSGPLTGEFS VESIIDLNAN YVEIGHAERK NLFHEKTSEI AKKIKLALDE 

       130        140        150        160        170        180 
KITPVVCVGE EVRANDTNEL KNALKKQIEA LFQTINLAQW ENVVLAYEPE WAIGKASSAE 

       190        200        210        220        230        240 
TNYIESAHQA LREIIRELGG DETLVRIIYG GSVSKENAAE IVRQKNVDGL FVGRFGHKPQ 

       250 
NFADIVSIVS KTKG 

« Hide

References

[1]"Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne pathogen Listeria monocytogenes reveal new insights into the core genome components of this species."
Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M., Daugherty S.C., Dodson R.J. expand/collapse author list , Durkin A.S., Madupu R., Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O., Luchansky J.B., Fraser C.M.
Nucleic Acids Res. 32:2386-2395(2004) [PubMed: 15115801] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE017262 Genomic DNA. Translation: AAT03152.1.
RefSeqYP_012975.1.

3D structure databases

HSSPHSSP built from PDB template 1AG1 based on UniProtKB P04789.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ723V9.

Genome annotation databases

GeneID2799316.
GenomeReviewsGene locus LMOf2365_0366 in contig AE017262_GR.
KEGGlmf:LMOf2365_0366.
TIGRLMOf2365_0366.

Phylogenomic databases

HOGENOMQ723V9.
OMAEWLEATI.

Enzyme and pathway databases

BioCycLMON265669:LMOF2365_0366-MON.

Family and domain databases

HAMAPMF_00147.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR000652. Triosephosphate_isomerase.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR21139. Triophos_ismrse. 1 hit.
PfamPF00121. TIM. 1 hit.
[Graphical view]
ProDomPD001005. Triophos_ismrse. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTPIS2_LISMF
AccessionPrimary (citable) accession number: Q723V9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: November 3, 2009
This is version 38 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