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UniProtKB/Swiss-Prot entry P27876


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TPIS_BACSU
Primary accession number P27876
Secondary accession number O32251
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on July 15, 1999 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 75)
Name and origin of the protein
Protein name Triosephosphate isomerase
Synonyms TIM
EC 5.3.1.1
Triose-phosphate isomerase
Gene name
Name: tpiA
Synonyms: tpi
OrderedLocusNames: BSU33920
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / Marburg;
PubMed=8021172 [NCBI, ExPASy, EBI, Israel, Japan]
Leyva-Vazquez M.A., Setlow P.;
"Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis.";
J. Bacteriol. 176:3903-3910(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[3]
PROTEIN SEQUENCE OF 1-19.
STRAIN=168 / DB100;
PubMed=1495386 [NCBI, ExPASy, EBI, Israel, Japan]
Mitchell C., Morris P.W., Vary J.C.;
"Amino acid sequences of several Bacillus subtilis proteins modified by apparent guanylylation.";
Mol. Microbiol. 6:1579-1581(1992).
[4]
PROTEIN SEQUENCE OF 1-27.
STRAIN=168 / JH642;
PubMed=8755892 [NCBI, ExPASy, EBI, Israel, Japan]
Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
"Cold shock stress-induced proteins in Bacillus subtilis.";
J. Bacteriol. 178:4611-4619(1996).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M600464-MCP200; PubMed=17218307 [NCBI, ExPASy, EBI, Israel, Japan]
Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.;
"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.";
Mol. Cell. Proteomics 6:697-707(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L29475; AAA21679.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99121; CAB15397.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A69725; A69725.
RefSeq NP_391272.1; -.
3D structure databases
HSSP P00943; 2BTM. [HSSP ENTRY / PDB]
ModBase P27876.
Enzyme and pathway databases
BioCyc BSUB224308:BSU3389-MON; -.
Organism-specific databases
SubtiList BG10897; tpiA. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004807; Molecular function: triose-phosphate isomerase activity (inferred from electronic annotation from HAMAP).
GO:0006094; Biological process: gluconeogenesis (inferred from electronic annotation from HAMAP).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from HAMAP).
GO:0006098; Biological process: pentose-phosphate shunt (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00147; -; 1.
PBIL [Tree]
InterPro IPR013785; Aldolase_TIM.
IPR000652; Triophos_ismrse.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
PANTHER PTHR21139; Triophos_ismrse; 1.
Pfam PF00121; TIM; 1.
Pfam graphical view of domain structure.
ProDom PD001005; Triophos_ismrse; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00419; tim; 1.
PROSITE PS00171; TIM; 1.
BLOCKS P27876.
ProtoNet P27876.
Genome annotation databases
GeneID 938626; -.
GenomeReviews AL009126_GR; BSU33920.
KEGG bsu:BSU33920; -.
NMPDR fig|224308.1.peg.3398; -.
Phylogenomic databases
HOGENOM P27876; -.
Genome annotation databases
CMR P27876; BSU33920.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Direct protein sequencing; Gluconeogenesis; Glycolysis; Isomerase; Pentose shunt; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   253  253     Triosephosphate isomerase. PRO_0000090179
ACT_SITE   95    95        Electrophile (By similarity). 
ACT_SITE   167   167        Proton acceptor (By similarity). 
BINDING   9     9        Substrate (By similarity). 
BINDING   11    11        Substrate (By similarity). 
MOD_RES   213   213        Phosphoserine. 
CONFLICT   41    42        CA -> S (in Ref. 1; AAA21679). 
Sequence information
Length: 253 AA [This is the length of the unprocessed precursor] Molecular weight: 27030 Da [This is the MW of the unprocessed precursor] CRC64: 39B7D3EFBDA74D65 [This is a checksum on the sequence]
        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 

P27876 in FASTA format

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