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Q2FF63

- ILVA_STAA3

UniProt

Q2FF63 - ILVA_STAA3

Protein

L-threonine dehydratase biosynthetic IlvA

Gene

ilvA

Organism
Staphylococcus aureus (strain USA300)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (21 Mar 2006)
      Previous versions | rss
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    Functioni

    Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA By similarity.By similarity

    Catalytic activityi

    L-threonine = 2-oxobutanoate + NH3.

    Cofactori

    Pyridoxal phosphate.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei83 – 831Pyridoxal phosphateBy similarity
    Binding sitei315 – 3151Pyridoxal phosphateBy similarity

    GO - Molecular functioni

    1. L-threonine ammonia-lyase activity Source: UniProtKB-EC
    2. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. isoleucine biosynthetic process Source: UniProtKB-UniPathway
    2. threonine metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Isoleucine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciSAUR451515:GH3C-2014-MONOMER.
    UniPathwayiUPA00047; UER00054.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-threonine dehydratase biosynthetic IlvA (EC:4.3.1.19)
    Alternative name(s):
    Threonine deaminase
    Gene namesi
    Name:ilvA
    Ordered Locus Names:SAUSA300_2014
    OrganismiStaphylococcus aureus (strain USA300)
    Taxonomic identifieri367830 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000001939: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 422422L-threonine dehydratase biosynthetic IlvAPRO_0000234304Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei56 – 561N6-(pyridoxal phosphate)lysineBy similarity

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi451515.SAUSA300_2014.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2FF63.
    SMRiQ2FF63. Positions 11-329.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini339 – 41375ACT-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni190 – 1934Pyridoxal phosphate bindingBy similarity

    Sequence similaritiesi

    Contains 1 ACT-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1171.
    HOGENOMiHOG000046973.
    KOiK01754.
    OMAiEMLANFV.
    OrthoDBiEOG6ZSP7D.

    Family and domain databases

    InterProiIPR001721. ACT-like_dom.
    IPR011820. IlvA.
    IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    PF00585. Thr_dehydrat_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 1 hit.
    TIGRFAMsiTIGR02079. THD1. 1 hit.
    PROSITEiPS51672. ACT_LIKE. 1 hit.
    PS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q2FF63-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTVKTTVSTK DIDEAFLRLK DIVKETPLQL DHYLSQKYDC KVYLKREDLQ    50
    WVRSFKLRGA YNAISVLSDE AKSKGITCAS AGNHAQGVAY TAKKLNLNAV 100
    IFMPVTTPLQ KVNQVKFFGN SNVEVVLTGD TFDHCLAEAL TYTSEHQMNF 150
    IDPFNNVHTI SGQGTLAKEM LEQAKSDNVN FDYLFAAIGG GGLISGISTY 200
    FKTYSPTTKI IGVEPSGASS MYESVVVNNQ VVTLPNIDKF VDGASVARVG 250
    DITFEIAKEN VDDYVQVDEG AVCSTILDMY SKQAIVAEPA GALSVSALEN 300
    YKDHIKGKTV VCVISGGNND INRMKEIEER SLLYEEMKHY FILNFPQRPG 350
    ALREFVNDVL GPQDDITKFE YLKKSSQNTG TVIIGIQLKD HDDLIQLKQR 400
    VNHFDPSNIY INENKMLYSL LI 422
    Length:422
    Mass (Da):46,937
    Last modified:March 21, 2006 - v1
    Checksum:iA1A085175DA56D90
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000255 Genomic DNA. Translation: ABD20804.1.
    RefSeqiYP_494665.1. NC_007793.1.

    Genome annotation databases

    EnsemblBacteriaiABD20804; ABD20804; SAUSA300_2014.
    GeneIDi3915391.
    KEGGisaa:SAUSA300_2014.
    PATRICi19593533. VBIStaAur129981_2157.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000255 Genomic DNA. Translation: ABD20804.1 .
    RefSeqi YP_494665.1. NC_007793.1.

    3D structure databases

    ProteinModelPortali Q2FF63.
    SMRi Q2FF63. Positions 11-329.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 451515.SAUSA300_2014.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABD20804 ; ABD20804 ; SAUSA300_2014 .
    GeneIDi 3915391.
    KEGGi saa:SAUSA300_2014.
    PATRICi 19593533. VBIStaAur129981_2157.

    Phylogenomic databases

    eggNOGi COG1171.
    HOGENOMi HOG000046973.
    KOi K01754.
    OMAi EMLANFV.
    OrthoDBi EOG6ZSP7D.

    Enzyme and pathway databases

    UniPathwayi UPA00047 ; UER00054 .
    BioCyci SAUR451515:GH3C-2014-MONOMER.

    Family and domain databases

    InterProi IPR001721. ACT-like_dom.
    IPR011820. IlvA.
    IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view ]
    Pfami PF00291. PALP. 1 hit.
    PF00585. Thr_dehydrat_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53686. SSF53686. 1 hit.
    TIGRFAMsi TIGR02079. THD1. 1 hit.
    PROSITEi PS51672. ACT_LIKE. 1 hit.
    PS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete genome sequence of USA300, an epidemic clone of community-acquired meticillin-resistant Staphylococcus aureus."
      Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., Perdreau-Remington F.
      Lancet 367:731-739(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: USA300.

    Entry informationi

    Entry nameiILVA_STAA3
    AccessioniPrimary (citable) accession number: Q2FF63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2006
    Last sequence update: March 21, 2006
    Last modified: October 1, 2014
    This is version 56 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

    Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3