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Q72XY3 (TPIS_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:BCE_5240
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate = glycerone phosphate. HAMAP MF_00147_B

Pathway

Carbohydrate biosynthesis; gluconeogenesis. HAMAP MF_00147_B

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. HAMAP MF_00147_B

Subunit structure

Homodimer By similarity. HAMAP MF_00147_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00147_B.

Sequence similarities

Belongs to the triosephosphate isomerase family.

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: UniProtKB-KW

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

pentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontriose-phosphate isomerase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Triosephosphate isomerase HAMAP MF_00147_B
PRO_0000307425

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

Sequences

Sequence LengthMass (Da)Tools
Q72XY3 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 65066C03D33E6601

FASTA25126,482
        10         20         30         40         50         60 
MRKPIIAGNW KMNKTLSEAV SFVEEVKGQI PAASAVDAVV CSPALFLERL VAATEGTDLQ 

        70         80         90        100        110        120 
VGAQNMHFEK NGAFTGEISP VALSDLKVGY VVLGHSERRE MFAETDESVN KKTIAAFEHG 

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

       190        200        210        220        230        240 
ADANEVCAHI RKVVAEAVSP AAAEAVRIQY GGSVKPENIK EYMAQSDIDG ALVGGASLEP 

       250 
ASFLGLLEAV K 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS44141.1.
RefSeqNP_981533.1. NC_003909.8.

3D structure databases

HSSPHSSP built from PDB template 2BTM based on UniProtKB P00943.
ProteinModelPortalQ72XY3.
SMRQ72XY3. Positions 2-249.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ72XY3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000028629; EBBACP00000027979; EBBACG00000028620.
GeneID2747690.
GenomeReviewsGene locus BCE_5240 in contig AE017194_GR.
KEGGbca:BCE_5240.
NMPDRfig|222523.1.peg.5205.
PATRIC18859104. VBIBacCer118379_5022.
TIGRBCE_5240.

Phylogenomic databases

eggNOGCOG0149.
GeneTreeEBGT00050000002739.
HOGENOMHBG708281.
OMAISGQWPR.
ProtClustDBPRK00042.

Enzyme and pathway databases

BioCycBCER405917:BCE_5240-MONOMER.

Family and domain databases

HAMAPMF_00147_B. TIM_B.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR022896. TrioseP_Isoase_bac/euk.
IPR000652. Triosephosphate_isomerase.
IPR020861. Triosephosphate_isomerase_AS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK01803.
PANTHERPTHR21139. Triophos_ismrse. 1 hit.
PfamPF00121. TIM. 1 hit.
[Graphical view]
SUPFAMSSF51351. Triophos_ismrse. 1 hit.
TIGRFAMsTIGR00419. Tim. 1 hit.
PROSITEPS00171. TIM_1. 1 hit.
PS51440. TIM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTPIS_BACC1
AccessionPrimary (citable) accession number: Q72XY3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families