Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A7GUR9 (TPIS_BACCN)

Last modified November 3, 2009. Version 16. 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

Hide | Top

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: Bcer98_3680
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Hide | Top

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

Hide | Top

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.

Hide | Top

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
Pentose shunt
   Cellular componentCytoplasm
   Molecular functionIsomerase
   PTMPhosphoprotein
   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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Triosephosphate isomerase HAMAP MF_00147
PRO_1000076634

Sites

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

Amino acid modifications

Modified residue2131Phosphoserine By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
A7GUR9-1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: ADBD7CF8BAFB7832

FASTA25126,505
        10         20         30         40         50         60 
MRKPIIAGNW KMNKTLSEAV SFVEEVKGQI PAASAVDAVV CSPALFLERL VAATQGTDLK 

        70         80         90        100        110        120 
VGAQNMHFEK NGAFTGEISP VALSDLKVSY VVLGHSERRE MFAETDETVN KKTLAAFEHG 

       130        140        150        160        170        180 
LTPIVCCGET LEERESGKTF DLVAGQVTKA LAGLTEEQVK ATVIAYEPIW AIGTGKSSSA 

       190        200        210        220        230        240 
EDANEVCAHI RKVVAEAVSP AAAEAVRIQY GGSVKPGNIK EYMAQPDIDG ALVGGASLEP 

       250 
ASFLGLLEAV K

« Hide

Hide | Top

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Hide | Top

Cross-references

Sequence databases

CP000764 Genomic DNA. Translation: ABS23877.1.
RefSeqYP_001376872.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7GUR9.

Genome annotation databases

GeneID5345410.
GenomeReviewsGene locus Bcer98_3680 in contig CP000764_GR.
KEGGbcy:Bcer98_3680.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMANGCLVRM.

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]
TIGRFAMsTIGR00419. tim. 1 hit.
PROSITEPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameTPIS_BACCN
AccessionPrimary (citable) accession number: A7GUR9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 11, 2007
Last modified: November 3, 2009
This is version 16 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)

Hide | Top

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