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P0AA25

- THIO_ECOLI

UniProt

P0AA25 - THIO_ECOLI

Protein

Thioredoxin-1

Gene

trxA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei27 – 271Deprotonates C-terminal active site Cys
    Active sitei33 – 331Nucleophile
    Sitei34 – 341Contributes to redox potential value
    Sitei35 – 351Contributes to redox potential value
    Active sitei36 – 361Nucleophile

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein disulfide oxidoreductase activity Source: EcoCyc

    GO - Biological processi

    1. cell redox homeostasis Source: EcoCyc
    2. glycerol ether metabolic process Source: InterPro
    3. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Electron transport, Host-virus interaction, Transport

    Enzyme and pathway databases

    BioCyciEcoCyc:RED-THIOREDOXIN-MONOMER.
    ECOL316407:JW5856-MONOMER.
    MetaCyc:RED-THIOREDOXIN-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin-1
    Short name:
    Trx-1
    Gene namesi
    Name:trxA
    Synonyms:fipA, tsnC
    Ordered Locus Names:b3781, JW5856
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11031. trxA.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 109108Thioredoxin-1PRO_0000120096Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi33 ↔ 36Redox-active1 PublicationPROSITE-ProRule annotation
    Modified residuei70 – 701N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    PaxDbiP0AA25.
    PRIDEiP0AA25.

    2D gel databases

    SWISS-2DPAGEP0AA25.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AA25.

    Interactioni

    Subunit structurei

    Monomer. Interacts with bacteriophage T3 DNA polymerase.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    At2g44920O221602EBI-368542,EBI-2895776From a different organism.
    At5g53490P817602EBI-368542,EBI-449573From a different organism.
    FKBP13Q9SCY22EBI-368542,EBI-2895757From a different organism.
    PPD6Q9LXX52EBI-368542,EBI-2895738From a different organism.
    PRXQQ9LU862EBI-368542,EBI-540311From a different organism.
    PSBO1P233212EBI-368542,EBI-449414From a different organism.
    PSBO2Q9S8412EBI-368542,EBI-449424From a different organism.
    TL29P822812EBI-368542,EBI-2895799From a different organism.
    trxBP0A9P42EBI-368542,EBI-1029826
    VDE1Q392492EBI-368542,EBI-2895666From a different organism.

    Protein-protein interaction databases

    DIPiDIP-31856N.
    IntActiP0AA25. 98 interactions.
    MINTiMINT-1530752.
    STRINGi511145.b3781.

    Structurei

    Secondary structure

    1
    109
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84
    Turni10 – 123
    Helixi13 – 164
    Turni17 – 193
    Beta strandi22 – 298
    Helixi34 – 4916
    Turni50 – 534
    Beta strandi55 – 606
    Turni61 – 633
    Helixi65 – 706
    Beta strandi75 – 839
    Beta strandi86 – 938
    Helixi97 – 1059

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F6MX-ray2.95C/D/G/H2-109[»]
    1KEBX-ray1.80A/B2-109[»]
    1M7TNMR-A34-108[»]
    1OAZX-ray2.77A/B1-109[»]
    1SKRX-ray2.40B2-109[»]
    1SKSX-ray2.30B2-109[»]
    1SKWX-ray2.30B2-109[»]
    1SL0X-ray3.20B/D2-109[»]
    1SL1X-ray2.20B2-109[»]
    1SL2X-ray2.30B2-109[»]
    1SRXX-ray2.80A2-109[»]
    1T7PX-ray2.20B2-109[»]
    1T8EX-ray2.54B2-109[»]
    1THOX-ray2.30A2-109[»]
    1TK0X-ray2.30B2-109[»]
    1TK5X-ray2.20B2-109[»]
    1TK8X-ray2.50B2-109[»]
    1TKDX-ray2.49B2-109[»]
    1TXXX-ray2.20A2-109[»]
    1X9MX-ray2.10B2-109[»]
    1X9SX-ray2.70B2-109[»]
    1X9WX-ray2.30B2-109[»]
    1XOANMR-A2-109[»]
    1XOBNMR-A2-109[»]
    1ZCPX-ray2.30A/B/C/D2-109[»]
    1ZYQX-ray2.70B2-109[»]
    1ZZYX-ray2.50A/B2-109[»]
    2AJQX-ray2.60B/I2-109[»]
    2BTOX-ray2.50T2-109[»]
    2EIOX-ray2.60A/B/C/D2-109[»]
    2EIQX-ray1.90A/B2-109[»]
    2EIRX-ray2.50A/B/C/D2-109[»]
    2FCHX-ray2.60A/B/C/D/E/F/G2-109[»]
    2FD3X-ray2.45A/B2-109[»]
    2H6XX-ray2.60A/B2-109[»]
    2H6YX-ray2.40A/B2-109[»]
    2H6ZX-ray2.25A/B2-109[»]
    2H70X-ray2.70A/B2-109[»]
    2H71X-ray2.20A/B2-109[»]
    2H72X-ray2.25A/B2-109[»]
    2H73X-ray2.45A/B2-109[»]
    2H74X-ray2.40A/B4-109[»]
    2H75X-ray2.20A/B2-109[»]
    2H76X-ray2.25A/B2-109[»]
    2O8VX-ray3.00B2-109[»]
    2TIRX-ray2.00A2-109[»]
    2TRXX-ray1.68A/B2-109[»]
    3DYRX-ray2.00A/B2-109[»]
    4HU7X-ray1.40A/B2-109[»]
    4HU9X-ray1.55A2-109[»]
    4HUAX-ray1.10A2-109[»]
    ProteinModelPortaliP0AA25.
    SMRiP0AA25. Positions 2-109.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AA25.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 109108ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the thioredoxin family.Curated
    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0526.
    HOGENOMiHOG000292977.
    KOiK03671.
    OMAiIHITSAD.
    OrthoDBiEOG6QG8RK.
    PhylomeDBiP0AA25.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR005746. Thioredoxin.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PANTHERiPTHR10438. PTHR10438. 1 hit.
    PfamiPF00085. Thioredoxin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000077. Thioredoxin. 1 hit.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
    PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0AA25-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA PILDEIADEY    50
    QGKLTVAKLN IDQNPGTAPK YGIRGIPTLL LFKNGEVAAT KVGALSKGQL 100
    KEFLDANLA 109
    Length:109
    Mass (Da):11,807
    Last modified:January 23, 2007 - v2
    Checksum:iEF5933EA29668EE9
    GO

    Sequence cautioni

    The sequence AAA24534.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAA67582.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti72 – 732GI → IG AA sequence (PubMed:4883076)Curated
    Sequence conflicti88 – 881A → AS in AAA24696. (PubMed:1379743)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26133 Genomic DNA. Translation: AAA24693.1.
    K02845 Genomic DNA. Translation: AAA24534.1. Different initiation.
    M10424 Genomic DNA. Translation: AAA24533.1.
    M54881 Genomic DNA. Translation: AAA24696.1.
    M12779 Genomic DNA. Translation: AAA24694.1.
    M87049 Genomic DNA. Translation: AAA67582.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76786.2.
    AP009048 Genomic DNA. Translation: BAE77517.1.
    PIRiA91519. TXEC.
    RefSeqiNP_418228.2. NC_000913.3.
    YP_491658.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76786; AAC76786; b3781.
    BAE77517; BAE77517; BAE77517.
    GeneIDi12934322.
    948289.
    KEGGiecj:Y75_p3394.
    eco:b3781.
    PATRICi32123053. VBIEscCol129921_3896.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26133 Genomic DNA. Translation: AAA24693.1 .
    K02845 Genomic DNA. Translation: AAA24534.1 . Different initiation.
    M10424 Genomic DNA. Translation: AAA24533.1 .
    M54881 Genomic DNA. Translation: AAA24696.1 .
    M12779 Genomic DNA. Translation: AAA24694.1 .
    M87049 Genomic DNA. Translation: AAA67582.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC76786.2 .
    AP009048 Genomic DNA. Translation: BAE77517.1 .
    PIRi A91519. TXEC.
    RefSeqi NP_418228.2. NC_000913.3.
    YP_491658.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F6M X-ray 2.95 C/D/G/H 2-109 [» ]
    1KEB X-ray 1.80 A/B 2-109 [» ]
    1M7T NMR - A 34-108 [» ]
    1OAZ X-ray 2.77 A/B 1-109 [» ]
    1SKR X-ray 2.40 B 2-109 [» ]
    1SKS X-ray 2.30 B 2-109 [» ]
    1SKW X-ray 2.30 B 2-109 [» ]
    1SL0 X-ray 3.20 B/D 2-109 [» ]
    1SL1 X-ray 2.20 B 2-109 [» ]
    1SL2 X-ray 2.30 B 2-109 [» ]
    1SRX X-ray 2.80 A 2-109 [» ]
    1T7P X-ray 2.20 B 2-109 [» ]
    1T8E X-ray 2.54 B 2-109 [» ]
    1THO X-ray 2.30 A 2-109 [» ]
    1TK0 X-ray 2.30 B 2-109 [» ]
    1TK5 X-ray 2.20 B 2-109 [» ]
    1TK8 X-ray 2.50 B 2-109 [» ]
    1TKD X-ray 2.49 B 2-109 [» ]
    1TXX X-ray 2.20 A 2-109 [» ]
    1X9M X-ray 2.10 B 2-109 [» ]
    1X9S X-ray 2.70 B 2-109 [» ]
    1X9W X-ray 2.30 B 2-109 [» ]
    1XOA NMR - A 2-109 [» ]
    1XOB NMR - A 2-109 [» ]
    1ZCP X-ray 2.30 A/B/C/D 2-109 [» ]
    1ZYQ X-ray 2.70 B 2-109 [» ]
    1ZZY X-ray 2.50 A/B 2-109 [» ]
    2AJQ X-ray 2.60 B/I 2-109 [» ]
    2BTO X-ray 2.50 T 2-109 [» ]
    2EIO X-ray 2.60 A/B/C/D 2-109 [» ]
    2EIQ X-ray 1.90 A/B 2-109 [» ]
    2EIR X-ray 2.50 A/B/C/D 2-109 [» ]
    2FCH X-ray 2.60 A/B/C/D/E/F/G 2-109 [» ]
    2FD3 X-ray 2.45 A/B 2-109 [» ]
    2H6X X-ray 2.60 A/B 2-109 [» ]
    2H6Y X-ray 2.40 A/B 2-109 [» ]
    2H6Z X-ray 2.25 A/B 2-109 [» ]
    2H70 X-ray 2.70 A/B 2-109 [» ]
    2H71 X-ray 2.20 A/B 2-109 [» ]
    2H72 X-ray 2.25 A/B 2-109 [» ]
    2H73 X-ray 2.45 A/B 2-109 [» ]
    2H74 X-ray 2.40 A/B 4-109 [» ]
    2H75 X-ray 2.20 A/B 2-109 [» ]
    2H76 X-ray 2.25 A/B 2-109 [» ]
    2O8V X-ray 3.00 B 2-109 [» ]
    2TIR X-ray 2.00 A 2-109 [» ]
    2TRX X-ray 1.68 A/B 2-109 [» ]
    3DYR X-ray 2.00 A/B 2-109 [» ]
    4HU7 X-ray 1.40 A/B 2-109 [» ]
    4HU9 X-ray 1.55 A 2-109 [» ]
    4HUA X-ray 1.10 A 2-109 [» ]
    ProteinModelPortali P0AA25.
    SMRi P0AA25. Positions 2-109.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-31856N.
    IntActi P0AA25. 98 interactions.
    MINTi MINT-1530752.
    STRINGi 511145.b3781.

    2D gel databases

    SWISS-2DPAGE P0AA25.

    Proteomic databases

    PaxDbi P0AA25.
    PRIDEi P0AA25.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76786 ; AAC76786 ; b3781 .
    BAE77517 ; BAE77517 ; BAE77517 .
    GeneIDi 12934322.
    948289.
    KEGGi ecj:Y75_p3394.
    eco:b3781.
    PATRICi 32123053. VBIEscCol129921_3896.

    Organism-specific databases

    EchoBASEi EB1024.
    EcoGenei EG11031. trxA.

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000292977.
    KOi K03671.
    OMAi IHITSAD.
    OrthoDBi EOG6QG8RK.
    PhylomeDBi P0AA25.

    Enzyme and pathway databases

    BioCyci EcoCyc:RED-THIOREDOXIN-MONOMER.
    ECOL316407:JW5856-MONOMER.
    MetaCyc:RED-THIOREDOXIN-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AA25.
    PROi P0AA25.

    Gene expression databases

    Genevestigatori P0AA25.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR005746. Thioredoxin.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    PANTHERi PTHR10438. PTHR10438. 1 hit.
    Pfami PF00085. Thioredoxin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000077. Thioredoxin. 1 hit.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    TIGRFAMsi TIGR01068. thioredoxin. 1 hit.
    PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Genetic and physical analysis of the thioredoxin (trxA) gene of Escherichia coli K-12."
      Wallace B.J., Kushner S.R.
      Gene 32:399-408(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning and nucleotide sequence of the trxA gene of Escherichia coli K-12."
      Lim C.-J., Geraghty D., Fuchs J.A.
      J. Bacteriol. 163:311-316(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Physical analysis of the thioredoxin gene from Escherichia coli K-12."
      Wallace B.J., Zownir O., Kushner S.R.
      (In) Holmgren A. (eds.); Thioredoxin and glutaredoxin systems, structure and function, pp.11-19, Raven Press, New York (1986)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
      Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
      Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Thioredoxin. 6. The amino acid sequence of the protein from Escherichia coli B."
      Holmgren A.
      Eur. J. Biochem. 6:475-484(1968) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-109.
      Strain: B.
    9. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    10. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    11. "Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8-A resolution."
      Holmgren A., Soederberg B.-O., Eklund H., Braenden C.-I.
      Proc. Natl. Acad. Sci. U.S.A. 72:2305-2309(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    12. "Structure of oxidized thioredoxin to 4 with 5-A resolution."
      Soederberg B.-O., Holmgren A., Braenden C.-I.
      J. Mol. Biol. 90:143-152(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS).
    13. "Crystal structure of thioredoxin from Escherichia coli at 1.68-A resolution."
      Katti S.K., le Master D.M., Eklund H.
      J. Mol. Biol. 212:167-184(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS).
    14. "Crystal structure analysis of a mutant Escherichia coli thioredoxin in which lysine 36 is replaced by glutamic acid."
      Nikkola M., Gleason F.K., Fuchs J.A., Eklund H.
      Biochemistry 32:5093-5098(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT GLU-37.
    15. "The CXXC motif: crystal structure of an active-site variant of Escherichia coli thioredoxin."
      Schultz L.W., Chivers P.T., Raines R.T.
      Acta Crystallogr. D 55:1533-1538(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), DISULFIDE BOND.
    16. "Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase."
      Lennon B.W., Williams C.H. Jr., Ludwig M.L.
      Science 289:1190-1194(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TRXB.
    17. "Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy."
      Dyson H.J., Gippert G.P., Case D.A., Holmgren A., Wright P.E.
      Biochemistry 29:4129-4136(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    18. "High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin."
      Jeng M.F., Campbell A.P., Begley T., Holmgren A., Case D.A., Wright P.E., Dyson H.J.
      Structure 2:853-868(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiTHIO_ECOLI
    AccessioniPrimary (citable) accession number: P0AA25
    Secondary accession number(s): P00274
    , P76750, Q2M889, Q47674, Q8XAT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 97 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3