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Protein

Cyanuric acid amidohydrolase

Gene

pRL100353

Organism
Rhizobium leguminosarum bv. viciae (strain 3841)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret.UniRule annotation1 Publication

Catalytic activityi

Cyanuric acid + H2O = biuret + CO2.UniRule annotation1 Publication

Enzyme regulationi

Inhibited by barbituric acid.UniRule annotationBy similarity

Kineticsi

kcat is 5 sec(-1) with cyanuric acid as substrate.1 Publication
  1. KM=130 µM for cyanuric acid1 Publication

    Pathwayi: atrazine degradation

    This protein is involved in step 1 of the subpathway that synthesizes biuret from cyanurate.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Cyanuric acid amidohydrolase (pRL100353)
    This subpathway is part of the pathway atrazine degradation, which is itself part of Xenobiotic degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes biuret from cyanurate, the pathway atrazine degradation and in Xenobiotic degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei53SubstrateUniRule annotation1
    Active sitei153UniRule annotation1
    Binding sitei185SubstrateUniRule annotation1
    Active sitei223NucleophileUniRule annotation1
    Metal bindingi283Magnesium; structuralUniRule annotation1
    Sitei306Important for substrate specificityUniRule annotation1
    Binding sitei310SubstrateUniRule annotation1
    Metal bindingi332Magnesium; via carbonyl oxygen; structuralUniRule annotation1
    Metal bindingi335Magnesium; via carbonyl oxygen; structuralUniRule annotation1
    Metal bindingi336Magnesium; via carbonyl oxygen; structuralUniRule annotation1
    Metal bindingi337Magnesium; via carbonyl oxygen; structuralUniRule annotation1
    Metal bindingi340Magnesium; via carbonyl oxygen; structuralUniRule annotation1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionHydrolase
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00008; UER00502.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyanuric acid amidohydrolaseUniRule annotation (EC:3.5.2.15UniRule annotation1 Publication)
    Short name:
    CAHUniRule annotation
    Gene namesi
    Ordered Locus Names:pRL100353
    Encoded oniPlasmid pRL100 Publication
    OrganismiRhizobium leguminosarum bv. viciae (strain 3841)
    Taxonomic identifieri216596 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium
    Proteomesi
    • UP000006575 Componenti: Plasmid pRL10

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004399181 – 351Cyanuric acid amidohydrolaseAdd BLAST351

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotationBy similarity

    Structurei

    3D structure databases

    SMRiQ1M7F3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1 – 96RU AUniRule annotationAdd BLAST96
    Regioni77 – 78Substrate bindingUniRule annotation2
    Regioni103 – 240RU BUniRule annotationAdd BLAST138
    Regioni223 – 224Substrate bindingUniRule annotation2
    Regioni246 – 351RU CUniRule annotationAdd BLAST106
    Regioni329 – 330Substrate bindingUniRule annotation2

    Domaini

    The monomer structure is formed from three repeating units (RUs) that share the same structure as one another. The monomer, the active site and substrate all possess threefold rotational symmetry, to the extent that the active site possesses three potential Ser-Lys catalytic dyads. It is possible that any or all of the three active-site serines may act as nucleophile (albeit only one can do so per catalytic cycle).UniRule annotation

    Sequence similaritiesi

    Belongs to the cyclic amide hydrolase (CyAH) family.UniRule annotationCurated

    Phylogenomic databases

    HOGENOMiHOG000223772.
    KOiK03383.
    OMAiGRYRIGH.
    OrthoDBiPOG091H115Q.

    Family and domain databases

    HAMAPiMF_01989. Cyc_amidohydrol. 1 hit.
    InterProiView protein in InterPro
    IPR014086. AtzD/Barbiturase.
    PfamiView protein in Pfam
    PF09663. Amido_AtzD_TrzD. 1 hit.
    TIGRFAMsiTIGR02714. amido_AtzD_TrzD. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q1M7F3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPSLRAHVFR VPADGPDDVA GVEALFASGL QANNIVAVLG KTEGNGCVND
    60 70 80 90 100
    FTRGYATRSF ETLFSRYGVD GVSIIMSGGT EGALSPHWTV FARETVETPG
    110 120 130 140 150
    ERALAIGVSR TPALSPEHLG RREQILLVAE GVKSAMRDAG IDDPADAHFV
    160 170 180 190 200
    QIKCPLLTSR RIAEAEAAGR TVATHDTLKS MGLSRGASAL GVAVALGEID
    210 220 230 240 250
    ATSINDADIC TRFDLFSRCA STSSGVELTD HEIIVLGMSA KWSGPLSIDH
    260 270 280 290 300
    AVMRDAIDAH SVRKARERLP ENSRLAAVLA KAEPDPSGEI DGRRHTMLDD
    310 320 330 340 350
    SDIAGTRHAR AFVGGVLAGI FGITDLYVSG GAEHQGPPGG GPVAIIVEKE

    Q
    Length:351
    Mass (Da):36,854
    Last modified:May 30, 2006 - v1
    Checksum:iAA90284C62B6EC42
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AM236084 Genomic DNA. Translation: CAK10579.1.
    RefSeqiWP_011654380.1. NC_008381.1.

    Genome annotation databases

    EnsemblBacteriaiCAK10579; CAK10579; pRL100353.
    KEGGirle:pRL100353.

    Similar proteinsi

    Entry informationi

    Entry nameiCAH_RHIL3
    AccessioniPrimary (citable) accession number: Q1M7F3
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2017
    Last sequence update: May 30, 2006
    Last modified: January 31, 2018
    This is version 62 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Plasmid, Reference proteome

    Documents

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