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C8TG88

- C8TG88_ECO26

UniProt

C8TG88 - C8TG88_ECO26

Protein

Diaminopimelate decarboxylase

Gene

lysA

Organism
Escherichia coli O26:H11 (strain 11368 / EHEC)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 35 (01 Oct 2014)
      Sequence version 1 (03 Nov 2009)
      Previous versions | rss
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    Functioni

    Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.UniRule annotation

    Catalytic activityi

    Meso-2,6-diaminoheptanedioate = L-lysine + CO2.UniRule annotation

    Cofactori

    Pyridoxal phosphate.UniRule annotationSAAS annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei227 – 2271Pyridoxal phosphate; via amide nitrogenUniRule annotation
    Binding sitei271 – 2711SubstrateUniRule annotation
    Binding sitei307 – 3071SubstrateUniRule annotation
    Binding sitei311 – 3111SubstrateUniRule annotation
    Binding sitei343 – 3431SubstrateUniRule annotation
    Binding sitei378 – 3781Pyridoxal phosphateUniRule annotation
    Binding sitei378 – 3781SubstrateUniRule annotation

    GO - Molecular functioni

    1. diaminopimelate decarboxylase activity Source: UniProtKB-HAMAP
    2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. lysine biosynthetic process via diaminopimelate Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    DecarboxylaseUniRule annotationSAAS annotation, Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Lysine biosynthesisUniRule annotation

    Keywords - Ligandi

    Pyridoxal phosphateUniRule annotationSAAS annotation

    Enzyme and pathway databases

    BioCyciECOL573235:GCY7-4034-MONOMER.
    UniPathwayiUPA00034; UER00027.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Diaminopimelate decarboxylaseUniRule annotation (EC:4.1.1.20UniRule annotation)
    Short name:
    DAP decarboxylaseUniRule annotation
    Short name:
    DAPDCUniRule annotation
    Gene namesi
    Name:lysAUniRule annotationImported
    Ordered Locus Names:ECO26_3911Imported
    OrganismiEscherichia coli O26:H11 (strain 11368 / EHEC)Imported
    Taxonomic identifieri573235 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000001617: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei54 – 541N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi573235.ECO26_3911.

    Structurei

    3D structure databases

    ProteinModelPortaliC8TG88.
    SMRiC8TG88. Positions 2-411.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni268 – 2714Pyridoxal phosphate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0019.
    HOGENOMiHOG000045070.
    KOiK01586.
    OrthoDBiEOG6Z9B18.

    Family and domain databases

    Gene3Di2.40.37.10. 1 hit.
    3.20.20.10. 1 hit.
    HAMAPiMF_02120. LysA.
    InterProiIPR009006. Ala_racemase/Decarboxylase_C.
    IPR002986. DAP_deCOOHase_LysA.
    IPR022643. De-COase2_C.
    IPR022657. De-COase2_CS.
    IPR022644. De-COase2_N.
    IPR022653. De-COase2_pyr-phos_BS.
    IPR000183. Orn/DAP/Arg_de-COase.
    IPR029066. PLP-binding_barrel.
    [Graphical view]
    PfamiPF02784. Orn_Arg_deC_N. 1 hit.
    PF00278. Orn_DAP_Arg_deC. 1 hit.
    [Graphical view]
    PRINTSiPR01181. DAPDCRBXLASE.
    PR01179. ODADCRBXLASE.
    SUPFAMiSSF50621. SSF50621. 1 hit.
    SSF51419. SSF51419. 1 hit.
    TIGRFAMsiTIGR01048. lysA. 1 hit.
    PROSITEiPS00878. ODR_DC_2_1. 1 hit.
    PS00879. ODR_DC_2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    C8TG88-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPHSLFSTDT DLTAENLLRL PAEFGCPVWV YDAQIIRRQI AALKQFDVVR    50
    FAQKACSNIH ILRLMREQGV KVDSVSLGEI ERALAAGYNP QTHPDDIVFT 100
    ADVIDQATLE RVSELQIPVN AGSVDMLDQL GQVSPGHRVW LRVNPGFGHG 150
    HSQKTNTGGE NSKHGIWYTD LPAALDVIQR HHLQLVGIHM HIGSGVDYAH 200
    LEQVCGAMVR QVIEFGQDLQ AISAGGGLSI PYQQGEEAVD TEHYYGLWNA 250
    AREQIARHLG HPVKLEIEPG RFLVAQSGVL ITQVRSVKQM GSRHFVLVDA 300
    GFNDLMRPAM YGSYHHISAL AADGRSLEHA PTVETVVAGP LCESGDVFTQ 350
    QEGGNVETRA LPEVKAGDYL VLHDTGAYGA SMSSNYNSRP LLPEVLFDNG 400
    QARLIRRRQT IEELLALELL 420
    Length:420
    Mass (Da):46,191
    Last modified:November 3, 2009 - v1
    Checksum:i000D02EE3F96FF3A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP010953 Genomic DNA. Translation: BAI27102.1.
    RefSeqiYP_003230842.1. NC_013361.1.

    Genome annotation databases

    EnsemblBacteriaiBAI27102; BAI27102; ECO26_3911.
    GeneIDi8481203.
    KEGGieoj:ECO26_3911.
    PATRICi18403575. VBIEscCol24965_4000.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP010953 Genomic DNA. Translation: BAI27102.1 .
    RefSeqi YP_003230842.1. NC_013361.1.

    3D structure databases

    ProteinModelPortali C8TG88.
    SMRi C8TG88. Positions 2-411.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 573235.ECO26_3911.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAI27102 ; BAI27102 ; ECO26_3911 .
    GeneIDi 8481203.
    KEGGi eoj:ECO26_3911.
    PATRICi 18403575. VBIEscCol24965_4000.

    Phylogenomic databases

    eggNOGi COG0019.
    HOGENOMi HOG000045070.
    KOi K01586.
    OrthoDBi EOG6Z9B18.

    Enzyme and pathway databases

    UniPathwayi UPA00034 ; UER00027 .
    BioCyci ECOL573235:GCY7-4034-MONOMER.

    Family and domain databases

    Gene3Di 2.40.37.10. 1 hit.
    3.20.20.10. 1 hit.
    HAMAPi MF_02120. LysA.
    InterProi IPR009006. Ala_racemase/Decarboxylase_C.
    IPR002986. DAP_deCOOHase_LysA.
    IPR022643. De-COase2_C.
    IPR022657. De-COase2_CS.
    IPR022644. De-COase2_N.
    IPR022653. De-COase2_pyr-phos_BS.
    IPR000183. Orn/DAP/Arg_de-COase.
    IPR029066. PLP-binding_barrel.
    [Graphical view ]
    Pfami PF02784. Orn_Arg_deC_N. 1 hit.
    PF00278. Orn_DAP_Arg_deC. 1 hit.
    [Graphical view ]
    PRINTSi PR01181. DAPDCRBXLASE.
    PR01179. ODADCRBXLASE.
    SUPFAMi SSF50621. SSF50621. 1 hit.
    SSF51419. SSF51419. 1 hit.
    TIGRFAMsi TIGR01048. lysA. 1 hit.
    PROSITEi PS00878. ODR_DC_2_1. 1 hit.
    PS00879. ODR_DC_2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
      Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
      Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 11368 / EHECImported.

    Entry informationi

    Entry nameiC8TG88_ECO26
    AccessioniPrimary (citable) accession number: C8TG88
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 3, 2009
    Last sequence update: November 3, 2009
    Last modified: October 1, 2014
    This is version 35 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteomeImported

    External Data

    Dasty 3