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Reviewed, UniProtKB/Swiss-Prot P27876 (TPIS_BACSU)

Last modified November 3, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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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: tpi
Ordered Locus Names: BSU33920
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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. HAMAP MF_00147

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the triosephosphate isomerase family.

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Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
Pentose shunt
   Cellular componentCytoplasm
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct 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

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontriose-phosphate isomerase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 253253Triosephosphate isomerase HAMAP MF_00147
PRO_0000090179

Sites

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

Amino acid modifications

Modified residue2131Phosphoserine Ref.5

Experimental info

Sequence conflict41 – 422CA → S in AAA21679. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P27876-1 [UniParc].

Last modified July 15, 1999. Version 3.
Checksum: 39B7D3EFBDA74D65

FASTA25327,030
        10         20         30         40         50         60 
MRKPIIAGNW KMNKTLGEAV SFVEEVKSSI PAADKAEAVV CAPALFLEKL ASAVKGTDLK 

        70         80         90        100        110        120 
VGAQNMHFEE SGAFTGEISP VALKDLGVDY CVIGHSERRE MFAETDETVN KKAHAAFKHG 

       130        140        150        160        170        180 
IVPIICVGET LEEREAGKTN DLVADQVKKG LAGLSEEQVA ASVIAYEPIW AIGTGKSSTA 

       190        200        210        220        230        240 
KDANDVCAHI RKTVAESFSQ EAADKLRIQY GGSVKPANIK EYMAESDIDG ALVGGASLEP 

       250 
QSFVQLLEEG QYE

« Hide

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References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis."
Leyva-Vazquez M.A., Setlow P.
J. Bacteriol. 176:3903-3910(1994) [PubMed: 8021172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Amino acid sequences of several Bacillus subtilis proteins modified by apparent guanylylation."
Mitchell C., Morris P.W., Vary J.C.
Mol. Microbiol. 6:1579-1581(1992) [PubMed: 1495386] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-19.
Strain: 168 / DB100.
[4]"Cold shock stress-induced proteins in Bacillus subtilis."
Graumann P., Schroeder K., Schmid R., Marahiel M.A.
J. Bacteriol. 178:4611-4619(1996) [PubMed: 8755892] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-27.
Strain: 168 / JH642.
[5]"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
Mol. Cell. Proteomics 6:697-707(2007) [PubMed: 17218307] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, MASS SPECTROMETRY.

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Cross-references

Sequence databases

L29475 Genomic DNA. Translation: AAA21679.1.
AL009126 Genomic DNA. Translation: CAB15397.1.
PIRA69725.
RefSeqNP_391272.1.

3D structure databases

HSSPHSSP built from PDB template 2BTM based on UniProtKB P00943.
ModBaseSearch...

PTM databases

PhosSiteP27876.

Genome annotation databases

GeneID938626.
GenomeReviewsGene locus BSU33920 in contig AL009126_GR.
KEGGbsu:BSU33920.
NMPDRfig|224308.1.peg.3398.

Organism-specific databases

SubtiListBG10897. tpiA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP27876.
OMANGCLVRM.

Enzyme and pathway databases

BioCycBSUB224308:BSU3389-MON.
BRENDA5.3.1.1. 150.

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...

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Entry information

Entry nameTPIS_BACSU
AccessionPrimary (citable) accession number: P27876
Secondary accession number(s): O32251
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 15, 1999
Last modified: November 3, 2009
This is version 80 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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