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P0A884

- TYSY_ECOLI

UniProt

P0A884 - TYSY_ECOLI

Protein

Thymidylate synthase

Gene

thyA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Provides the sole de novo source of dTMP for DNA biosynthesis. This protein also binds to its mRNA thus repressing its own translation.

    Catalytic activityi

    5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei146 – 1461

    GO - Molecular functioni

    1. RNA binding Source: UniProtKB-KW
    2. thymidylate synthase activity Source: EcoCyc

    GO - Biological processi

    1. dTMP biosynthetic process Source: UniProtKB-HAMAP
    2. dTTP biosynthetic process Source: UniProtKB-UniPathway
    3. regulation of translation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Methyltransferase, Repressor, Transferase

    Keywords - Biological processi

    Nucleotide biosynthesis, Translation regulation

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:THYMIDYLATESYN-MONOMER.
    ECOL316407:JW2795-MONOMER.
    MetaCyc:THYMIDYLATESYN-MONOMER.
    SABIO-RKP0A884.
    UniPathwayiUPA00575.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thymidylate synthaseUniRule annotation (EC:2.1.1.45UniRule annotation)
    Short name:
    TSUniRule annotation
    Short name:
    TSaseUniRule annotation
    Gene namesi
    Name:thyAUniRule annotation
    Ordered Locus Names:b2827, JW2795
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11002. thyA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 264264Thymidylate synthasePRO_0000140954Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-formylmethionineCurated

    Post-translational modificationi

    Although not discussed in the published references, Met-1 is represented in the submitted PDB entries as being modified by either a formyl, or a carboxyl group. The N-terminal is probably N-(dihydroxymethyl)methionine, the hydrated form of N-formylmethionine.

    Keywords - PTMi

    Formylation

    Proteomic databases

    PaxDbiP0A884.
    PRIDEiP0A884.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A884.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    DIPiDIP-48261N.
    IntActiP0A884. 5 interactions.
    MINTiMINT-1265510.
    STRINGi511145.b2827.

    Structurei

    Secondary structure

    1
    264
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 1413
    Beta strandi16 – 183
    Beta strandi21 – 233
    Beta strandi26 – 3712
    Helixi38 – 403
    Beta strandi46 – 483
    Helixi52 – 6413
    Helixi70 – 745
    Helixi81 – 833
    Helixi94 – 1007
    Beta strandi101 – 1033
    Turni104 – 1063
    Beta strandi107 – 1093
    Helixi111 – 12111
    Beta strandi129 – 1313
    Helixi135 – 1406
    Beta strandi141 – 1433
    Beta strandi146 – 15510
    Beta strandi158 – 16912
    Turni170 – 1734
    Helixi174 – 19118
    Beta strandi195 – 20915
    Helixi210 – 2123
    Helixi213 – 2208
    Beta strandi229 – 2324
    Helixi239 – 2413
    Helixi244 – 2463
    Beta strandi247 – 2515

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AIQX-ray2.20A/B1-264[»]
    1AJMX-ray2.40A1-264[»]
    1AN5X-ray2.60A/B1-264[»]
    1AOBX-ray2.10A1-264[»]
    1AXWX-ray1.70A/B1-264[»]
    1BDUX-ray2.10A1-264[»]
    1BIDX-ray2.20A1-264[»]
    1BJGX-ray2.30A1-264[»]
    1BQ1X-ray2.50A/B1-264[»]
    1BQ2X-ray2.20A1-264[»]
    1DDUX-ray2.10A/B1-264[»]
    1DNAX-ray2.20A/B1-264[»]
    1EV5X-ray1.70A1-264[»]
    1EV8X-ray2.60A1-264[»]
    1EVFX-ray1.70A1-264[»]
    1EVGX-ray2.00A1-264[»]
    1F4BX-ray1.75A1-264[»]
    1F4CX-ray2.00A/B1-264[»]
    1F4DX-ray2.15A/B1-264[»]
    1F4EX-ray1.90A1-264[»]
    1F4FX-ray2.00A/B1-264[»]
    1F4GX-ray1.75A/B1-264[»]
    1FFLX-ray2.94A1-264[»]
    1FWMX-ray2.20A/B1-264[»]
    1JG0X-ray2.00A/B1-264[»]
    1JTQX-ray2.50A/B1-264[»]
    1JTUX-ray2.20A/B1-264[»]
    1JUTX-ray2.70A/B1-264[»]
    1KCEX-ray2.00A/B1-264[»]
    1KZIX-ray1.75A/B1-264[»]
    1KZJX-ray2.60A/B/C/D/E/F1-264[»]
    1NCEX-ray2.40A/B1-264[»]
    1QQQX-ray1.50A1-264[»]
    1SYNX-ray2.00A/B1-264[»]
    1TDUX-ray2.10A/B1-264[»]
    1TJSX-ray2.20A1-264[»]
    1TLCX-ray2.10A/B1-264[»]
    1TLSX-ray2.60A/B1-264[»]
    1TRGX-ray1.90A1-264[»]
    1TSDX-ray1.95A/B1-264[»]
    1TSNX-ray2.20A1-264[»]
    1TYSX-ray1.80A1-264[»]
    1ZPRX-ray2.50A/B1-264[»]
    2A9WX-ray1.65A/B/C/D1-264[»]
    2BBQX-ray2.30A/B1-264[»]
    2FTNX-ray1.60A1-264[»]
    2FTOX-ray2.00X1-264[»]
    2FTQX-ray1.81A1-264[»]
    2G8XX-ray1.83A/B1-264[»]
    2KCEX-ray2.20A/B1-264[»]
    2TSCX-ray1.97A/B1-264[»]
    2VETX-ray2.20A1-264[»]
    2VF0X-ray3.00A/B1-264[»]
    3B5BX-ray2.70A/B1-264[»]
    3B9HX-ray2.49A1-264[»]
    3BFIX-ray2.20A1-264[»]
    3BGXX-ray1.93A1-264[»]
    3BHLX-ray1.40A/B1-264[»]
    3BHRX-ray1.90A1-264[»]
    3TMSX-ray2.10A1-264[»]
    4F2VX-ray2.49A/B1-264[»]
    4GEVX-ray1.30A/B1-264[»]
    4ISKX-ray1.75A/B/C/D/E/F/G/H2-264[»]
    4KNZX-ray1.30A/B1-264[»]
    ProteinModelPortaliP0A884.
    SMRiP0A884. Positions 2-264.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A884.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0207.
    HOGENOMiHOG000257900.
    KOiK00560.
    OMAiDVHLYSN.
    OrthoDBiEOG6K6V53.
    PhylomeDBiP0A884.

    Family and domain databases

    Gene3Di3.30.572.10. 1 hit.
    HAMAPiMF_00008. Thymidy_synth_bact.
    InterProiIPR023451. Thymidate_synth/dCMP_Mease.
    IPR000398. Thymidylate_synthase.
    IPR020940. Thymidylate_synthase_AS.
    [Graphical view]
    PfamiPF00303. Thymidylat_synt. 1 hit.
    [Graphical view]
    PRINTSiPR00108. THYMDSNTHASE.
    SUPFAMiSSF55831. SSF55831. 1 hit.
    TIGRFAMsiTIGR03284. thym_sym. 2 hits.
    PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A884-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKQYLELMQK VLDEGTQKND RTGTGTLSIF GHQMRFNLQD GFPLVTTKRC    50
    HLRSIIHELL WFLQGDTNIA YLHENNVTIW DEWADENGDL GPVYGKQWRA 100
    WPTPDGRHID QITTVLNQLK NDPDSRRIIV SAWNVGELDK MALAPCHAFF 150
    QFYVADGKLS CQLYQRSCDV FLGLPFNIAS YALLVHMMAQ QCDLEVGDFV 200
    WTGGDTHLYS NHMDQTHLQL SREPRPLPKL IIKRKPESIF DYRFEDFEIE 250
    GYDPHPGIKA PVAI 264
    Length:264
    Mass (Da):30,480
    Last modified:July 21, 1986 - v1
    Checksum:i0E6D88ED98D24D22
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01710 Genomic DNA. Translation: AAA24675.1.
    U29581 Genomic DNA. Translation: AAB40474.1.
    U00096 Genomic DNA. Translation: AAC75866.1.
    AP009048 Genomic DNA. Translation: BAE76896.1.
    X03966 Genomic DNA. Translation: CAA27600.1.
    PIRiA00549. SYECT.
    RefSeqiNP_417304.1. NC_000913.3.
    YP_491032.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75866; AAC75866; b2827.
    BAE76896; BAE76896; BAE76896.
    GeneIDi12933064.
    949035.
    KEGGiecj:Y75_p2761.
    eco:b2827.
    PATRICi32121072. VBIEscCol129921_2925.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01710 Genomic DNA. Translation: AAA24675.1 .
    U29581 Genomic DNA. Translation: AAB40474.1 .
    U00096 Genomic DNA. Translation: AAC75866.1 .
    AP009048 Genomic DNA. Translation: BAE76896.1 .
    X03966 Genomic DNA. Translation: CAA27600.1 .
    PIRi A00549. SYECT.
    RefSeqi NP_417304.1. NC_000913.3.
    YP_491032.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AIQ X-ray 2.20 A/B 1-264 [» ]
    1AJM X-ray 2.40 A 1-264 [» ]
    1AN5 X-ray 2.60 A/B 1-264 [» ]
    1AOB X-ray 2.10 A 1-264 [» ]
    1AXW X-ray 1.70 A/B 1-264 [» ]
    1BDU X-ray 2.10 A 1-264 [» ]
    1BID X-ray 2.20 A 1-264 [» ]
    1BJG X-ray 2.30 A 1-264 [» ]
    1BQ1 X-ray 2.50 A/B 1-264 [» ]
    1BQ2 X-ray 2.20 A 1-264 [» ]
    1DDU X-ray 2.10 A/B 1-264 [» ]
    1DNA X-ray 2.20 A/B 1-264 [» ]
    1EV5 X-ray 1.70 A 1-264 [» ]
    1EV8 X-ray 2.60 A 1-264 [» ]
    1EVF X-ray 1.70 A 1-264 [» ]
    1EVG X-ray 2.00 A 1-264 [» ]
    1F4B X-ray 1.75 A 1-264 [» ]
    1F4C X-ray 2.00 A/B 1-264 [» ]
    1F4D X-ray 2.15 A/B 1-264 [» ]
    1F4E X-ray 1.90 A 1-264 [» ]
    1F4F X-ray 2.00 A/B 1-264 [» ]
    1F4G X-ray 1.75 A/B 1-264 [» ]
    1FFL X-ray 2.94 A 1-264 [» ]
    1FWM X-ray 2.20 A/B 1-264 [» ]
    1JG0 X-ray 2.00 A/B 1-264 [» ]
    1JTQ X-ray 2.50 A/B 1-264 [» ]
    1JTU X-ray 2.20 A/B 1-264 [» ]
    1JUT X-ray 2.70 A/B 1-264 [» ]
    1KCE X-ray 2.00 A/B 1-264 [» ]
    1KZI X-ray 1.75 A/B 1-264 [» ]
    1KZJ X-ray 2.60 A/B/C/D/E/F 1-264 [» ]
    1NCE X-ray 2.40 A/B 1-264 [» ]
    1QQQ X-ray 1.50 A 1-264 [» ]
    1SYN X-ray 2.00 A/B 1-264 [» ]
    1TDU X-ray 2.10 A/B 1-264 [» ]
    1TJS X-ray 2.20 A 1-264 [» ]
    1TLC X-ray 2.10 A/B 1-264 [» ]
    1TLS X-ray 2.60 A/B 1-264 [» ]
    1TRG X-ray 1.90 A 1-264 [» ]
    1TSD X-ray 1.95 A/B 1-264 [» ]
    1TSN X-ray 2.20 A 1-264 [» ]
    1TYS X-ray 1.80 A 1-264 [» ]
    1ZPR X-ray 2.50 A/B 1-264 [» ]
    2A9W X-ray 1.65 A/B/C/D 1-264 [» ]
    2BBQ X-ray 2.30 A/B 1-264 [» ]
    2FTN X-ray 1.60 A 1-264 [» ]
    2FTO X-ray 2.00 X 1-264 [» ]
    2FTQ X-ray 1.81 A 1-264 [» ]
    2G8X X-ray 1.83 A/B 1-264 [» ]
    2KCE X-ray 2.20 A/B 1-264 [» ]
    2TSC X-ray 1.97 A/B 1-264 [» ]
    2VET X-ray 2.20 A 1-264 [» ]
    2VF0 X-ray 3.00 A/B 1-264 [» ]
    3B5B X-ray 2.70 A/B 1-264 [» ]
    3B9H X-ray 2.49 A 1-264 [» ]
    3BFI X-ray 2.20 A 1-264 [» ]
    3BGX X-ray 1.93 A 1-264 [» ]
    3BHL X-ray 1.40 A/B 1-264 [» ]
    3BHR X-ray 1.90 A 1-264 [» ]
    3TMS X-ray 2.10 A 1-264 [» ]
    4F2V X-ray 2.49 A/B 1-264 [» ]
    4GEV X-ray 1.30 A/B 1-264 [» ]
    4ISK X-ray 1.75 A/B/C/D/E/F/G/H 2-264 [» ]
    4KNZ X-ray 1.30 A/B 1-264 [» ]
    ProteinModelPortali P0A884.
    SMRi P0A884. Positions 2-264.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48261N.
    IntActi P0A884. 5 interactions.
    MINTi MINT-1265510.
    STRINGi 511145.b2827.

    Chemistry

    BindingDBi P0A884.
    ChEMBLi CHEMBL2555.

    Proteomic databases

    PaxDbi P0A884.
    PRIDEi P0A884.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75866 ; AAC75866 ; b2827 .
    BAE76896 ; BAE76896 ; BAE76896 .
    GeneIDi 12933064.
    949035.
    KEGGi ecj:Y75_p2761.
    eco:b2827.
    PATRICi 32121072. VBIEscCol129921_2925.

    Organism-specific databases

    EchoBASEi EB0995.
    EcoGenei EG11002. thyA.

    Phylogenomic databases

    eggNOGi COG0207.
    HOGENOMi HOG000257900.
    KOi K00560.
    OMAi DVHLYSN.
    OrthoDBi EOG6K6V53.
    PhylomeDBi P0A884.

    Enzyme and pathway databases

    UniPathwayi UPA00575 .
    BioCyci EcoCyc:THYMIDYLATESYN-MONOMER.
    ECOL316407:JW2795-MONOMER.
    MetaCyc:THYMIDYLATESYN-MONOMER.
    SABIO-RK P0A884.

    Miscellaneous databases

    EvolutionaryTracei P0A884.
    PROi P0A884.

    Gene expression databases

    Genevestigatori P0A884.

    Family and domain databases

    Gene3Di 3.30.572.10. 1 hit.
    HAMAPi MF_00008. Thymidy_synth_bact.
    InterProi IPR023451. Thymidate_synth/dCMP_Mease.
    IPR000398. Thymidylate_synthase.
    IPR020940. Thymidylate_synthase_AS.
    [Graphical view ]
    Pfami PF00303. Thymidylat_synt. 1 hit.
    [Graphical view ]
    PRINTSi PR00108. THYMDSNTHASE.
    SUPFAMi SSF55831. SSF55831. 1 hit.
    TIGRFAMsi TIGR03284. thym_sym. 2 hits.
    PROSITEi PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the Escherichia coli thyA gene and its thymidylate synthase product."
      Belfort M., Maley G.F., Pedersen-Lane J., Maley F.
      Proc. Natl. Acad. Sci. U.S.A. 80:4914-4918(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: K12 / JM103 / ATCC 39403 / DSM 2829 / NCIMB 12044.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Complete nucleotide sequence of the Escherichia coli recC gene and of the thyA-recC intergenic region."
      Finch P.W., Wilson R.E., Brown K., Hickson I.D., Tomkinson A.E., Emmerson P.T.
      Nucleic Acids Res. 14:4437-4451(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 63-264.
    5. "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.
    6. "Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate."
      Montfort W.R., Perry K.M., Fauman E.B., Finer-Moore J.S., Maley G.F., Hardy L., Maley F., Stroud R.M.
      Biochemistry 29:6964-6977(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS).
    7. "Characterization of a specific interaction between Escherichia coli thymidylate synthase and Escherichia coli thymidylate synthase mRNA."
      Voeller D.M., Changchien L.-M., Maley G.F., Maley F., Takechi T., Turner R.E., Montfort W.R., Allegra C.J., Chu E.
      Nucleic Acids Res. 23:869-875(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MECHANISM OF TRANSLATION REGULATION.
    8. "Amino acid substitution analysis of E. coli thymidylate synthase: the study of a highly conserved region at the N-terminus."
      Kim C.W., Michaels M.L., Miller J.F.
      Proteins 13:352-363(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    9. "Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases."
      Perry K.M., Fauman E.B., Finer-Moore J.S., Montfort W.R., Maley G.F., Maley F., Stroud R.M.
      Proteins 8:315-333(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    10. "Water-mediated substrate/product discrimination: the product complex of thymidylate synthase at 1.83 A."
      Fauman E.B., Rutenber E.E., Maley G.F., Maley F., Stroud R.M.
      Biochemistry 33:1502-1511(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
    11. "An essential role for water in an enzyme reaction mechanism: the crystal structure of the thymidylate synthase mutant E58Q."
      Sage C.R., Rutenber E.E., Stout T.J., Stroud R.M.
      Biochemistry 35:16270-16281(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLN-58.
    12. "Crystal structures of a marginally active thymidylate synthase mutant, Arg 126-->Glu."
      Strop P., Changchien L., Maley F., Montfort W.R.
      Protein Sci. 6:2504-2511(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT GLU-126.
    13. "Inactivity of N229A thymidylate synthase due to water-mediated effects: isolating a late stage in methyl transfer."
      Reyes C.L., Sage C.R., Rutenber E.E., Nissen R.M., Finer-Moore J.S., Stroud R.M.
      J. Mol. Biol. 284:699-712(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT ALA-177.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).

    Entry informationi

    Entry nameiTYSY_ECOLI
    AccessioniPrimary (citable) accession number: P0A884
    Secondary accession number(s): P00470, Q2MA10
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 91 of the entry and version 1 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3