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P60180 (TPIS_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 54. 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:
Putative triosephosphate isomerase

Short name=TIM
EC=5.3.1.1
Alternative name(s):
Triose-phosphate isomerase
Gene names
Name:tpiA
Ordered Locus Names:BC_5137
OrganismBacillus cereus (strain ATCC 14579 / DSM 31)
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceUncertain

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.

Caution

Could be the product of a pseudogene.

Sequence caution

The sequence AE016877 differs from that shown. Reason: Erroneous termination at position 132. Translated as Glu.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
Pentose shunt
   Cellular componentCytoplasm
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference 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 – 251251Putative triosephosphate isomerase HAMAP MF_00147_B
PRO_0000090175

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
P60180 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 65066B1BDE8FA601

FASTA25126,468
        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 EAAEAVRIQY GGSVKPENIK EYMAQSDIDG ALVGGASLEP 

       250 
ASFLGLLGAV K 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalP60180.
SMRP60180. Positions 2-249.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GenomeReviewsGene locus BC_5137 in contig AE016877_GR.

Phylogenomic databases

HOGENOMHBG708281.
OMAISGQWPR.
PhylomeDBP60180.

Family and domain databases

HAMAPMF_00147_B. TIM_B. Divergent sequence.
[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.
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_BACCR
AccessionPrimary (citable) accession number: P60180
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: December 14, 2011
This is version 54 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