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Reviewed, UniProtKB/Swiss-Prot Q4MQ55 (TPIS_BACCE)

Last modified February 9, 2010. Version 31. 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
Synonyms: tim
ORF Names: BCE_G9241_5215
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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.

Induction

By salt stress and heat shock. Ref.3

Sequence similarities

Belongs to the triosephosphate isomerase family.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
Pentose shunt
Stress response
   Cellular componentCytoplasm
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termDirect protein sequencing
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

response to stress

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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Triosephosphate isomerase HAMAP MF_00147
PRO_0000271233

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
Q4MQ55-1 [UniParc].

Last modified January 9, 2007. Version 2.
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]"Identification of anthrax toxin genes in a Bacillus cereus associated with an illness resembling inhalation anthrax."
Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D., Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W., Maiden M.C.J., Priest F.G., Barker M., Jiang L., Cer R.Z., Rilstone J., Peterson S.N., Weyant R.S. expand/collapse author list , Galloway D.R., Read T.D., Popovic T., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004) [PubMed: 15155910] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: G9241.
[2]Nishizawa M., Itoi Y., Ito S., Inoue M.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-141.
Strain: Tim-r01.
[3]"Heat and salt stress in the food pathogen Bacillus cereus."
Browne N., Dowds B.C.A.
J. Appl. Microbiol. 91:1085-1094(2001) [PubMed: 11851817] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-15, INDUCTION.
Strain: NCIMB 11796 / DSM 626.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAEK01000016 Genomic DNA. Translation: EAL14302.1. Different initiation.
AB083542 Genomic DNA. Translation: BAB88970.1.

3D structure databases

HSSPHSSP built from PDB template 2BTM based on UniProtKB P00943.
SMRQ4MQ55. Positions 2-249.
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.3.1.1. 604.

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_BACCE
AccessionPrimary (citable) accession number: Q4MQ55
Secondary accession number(s): P83069, Q8RQH4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: February 9, 2010
This is version 31 of the entry and version 2 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