Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cyanuric acid amidohydrolase

Gene

atzD

Organism
Pseudomonas sp. (strain ADP)
Status
Reviewed-Annotation score: Annotation score: 5 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 annotation2 Publications

Enzyme regulationi

Inhibited by barbituric acid.UniRule annotation1 Publication

Kineticsi

kcat is 73 sec(-1) with cyanuric acid as substrate (PubMed:22730121). kcat is 6.8 sec(-1) with cyanuric acid as substrate and 3.1 sec(-1) with N-methylisocyanuric acid as substrate (PubMed:12788776).2 Publications
  1. KM=23 µM for cyanuric acid1 Publication
  2. KM=57 µM for cyanuric acid1 Publication
  3. KM=71 µM for N-methylisocyanuric acid1 Publication

    pH dependencei

    Optimum pH is 8.2.1 Publication

    Pathwayi: atrazine degradation

    This protein is involved in step 1 of the subpathway that synthesizes biuret from cyanurate.UniRule annotation1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Cyanuric acid amidohydrolase (atzD)
    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 sitei52SubstrateUniRule annotation1 Publication1
    Active sitei162UniRule annotation1
    Binding sitei194SubstrateUniRule annotation1 Publication1
    Active sitei232NucleophileUniRule annotation1
    Metal bindingi297Magnesium; structuralUniRule annotation1 Publication1
    Sitei320Important for substrate specificityUniRule annotation1 Publication1
    Binding sitei324SubstrateUniRule annotation1 Publication1
    Metal bindingi346Magnesium; via carbonyl oxygen; structuralUniRule annotation1 Publication1
    Metal bindingi349Magnesium; via carbonyl oxygen; structuralUniRule annotation1 Publication1
    Metal bindingi350Magnesium; via carbonyl oxygen; structuralUniRule annotation1 Publication1
    Metal bindingi351Magnesium; via carbonyl oxygen; structuralUniRule annotation1 Publication1
    Metal bindingi354Magnesium; via carbonyl oxygen; structuralUniRule annotation1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionHydrolase
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13543.
    BRENDAi3.5.2.15. 5085.
    UniPathwayiUPA00008; UER00502.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyanuric acid amidohydrolaseUniRule annotation (EC:3.5.2.15UniRule annotation2 Publications)
    Short name:
    CAHUniRule annotation
    Gene namesi
    Name:atzD
    ORF Names:AOX63_31675
    Encoded oniPlasmid pADP-10 Publication
    OrganismiPseudomonas sp. (strain ADP)
    Taxonomic identifieri47660 [NCBI]
    Taxonomic lineageiBacteriaProteobacteria
    Proteomesi
    • UP000054734 Componentsi: Plasmid padp1, Unassembled WGS sequence

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000647611 – 363Cyanuric acid amidohydrolaseAdd BLAST363

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation1 Publication

    Structurei

    Secondary structure

    1363
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 10Combined sources9
    Helixi18 – 25Combined sources8
    Helixi31 – 33Combined sources3
    Beta strandi34 – 43Combined sources10
    Helixi51 – 67Combined sources17
    Helixi71 – 77Combined sources7
    Beta strandi78 – 84Combined sources7
    Beta strandi93 – 101Combined sources9
    Beta strandi112 – 119Combined sources8
    Helixi125 – 127Combined sources3
    Helixi131 – 148Combined sources18
    Helixi153 – 155Combined sources3
    Beta strandi156 – 163Combined sources8
    Helixi168 – 176Combined sources9
    Helixi186 – 204Combined sources19
    Helixi210 – 212Combined sources3
    Helixi215 – 217Combined sources3
    Turni218 – 220Combined sources3
    Beta strandi226 – 233Combined sources8
    Beta strandi241 – 248Combined sources8
    Beta strandi254 – 264Combined sources11
    Helixi268 – 277Combined sources10
    Helixi283 – 288Combined sources6
    Beta strandi289 – 296Combined sources8
    Beta strandi302 – 304Combined sources3
    Turni311 – 313Combined sources3
    Beta strandi315 – 317Combined sources3
    Helixi319 – 335Combined sources17
    Beta strandi336 – 338Combined sources3
    Beta strandi340 – 344Combined sources5
    Beta strandi349 – 351Combined sources3
    Beta strandi355 – 362Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4BVQX-ray1.90A/B1-363[»]
    4BVRX-ray2.58A/B1-363[»]
    4BVSX-ray2.60A/B1-363[»]
    4BVTX-ray3.10A/B1-363[»]
    SMRiP58329.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1 – 104RU AUniRule annotationAdd BLAST104
    Regioni83 – 84Substrate bindingUniRule annotation1 Publication2
    Regioni112 – 249RU BUniRule annotationAdd BLAST138
    Regioni232 – 233Substrate bindingUniRule annotation1 Publication2
    Regioni255 – 363RU CUniRule annotationAdd BLAST109
    Regioni343 – 344Substrate bindingUniRule annotation1 Publication2

    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 annotation1 Publication

    Sequence similaritiesi

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

    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.

    P58329-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MYHIDVFRIP CHSPGDTSGL EDLIETGRVA PADIVAVMGK TEGNGCVNDY
    60 70 80 90 100
    TREYATAMLA ACLGRHLQLP PHEVEKRVAF VMSGGTEGVL SPHHTVFARR
    110 120 130 140 150
    PAIDAHRPAG KRLTLGIAFT RDFLPEEIGR HAQITETAGA VKRAMRDAGI
    160 170 180 190 200
    ASIDDLHFVQ VKCPLLTPAK IASARSRGCA PVTTDTYESM GYSRGASALG
    210 220 230 240 250
    IALATEEVPS SMLVDESVLN DWSLSSSLAS ASAGIELEHN VVIAIGMSEQ
    260 270 280 290 300
    ATSELVIAHG VMSDAIDAAS VRRTIESLGI RSDDEMDRIV NVFAKAEASP
    310 320 330 340 350
    DGVVRGMRHT MLSDSDINST RHARAVTGAA IASVVGHGMV YVSGGAEHQG
    360
    PAGGGPFAVI ARA
    Length:363
    Mass (Da):38,200
    Last modified:October 24, 2001 - v1
    Checksum:i140256C30D82FF83
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U66917 Genomic DNA. Translation: AAK50331.1.
    JN607164 Genomic DNA. Translation: AET43038.1.
    LKAX01000023 Genomic DNA. Translation: KSW21436.1.
    RefSeqiNP_862537.1. NC_004956.1.
    WP_011117191.1. NZ_CM003636.1.

    Genome annotation databases

    EnsemblBacteriaiKSW21436; KSW21436; AOX63_31675.
    GeneIDi1440634.

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

    Entry informationi

    Entry nameiCAH_PSESD
    AccessioniPrimary (citable) accession number: P58329
    Secondary accession number(s): G8HMW5
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 24, 2001
    Last sequence update: October 24, 2001
    Last modified: June 7, 2017
    This is version 48 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

    3D-structure, Complete proteome, Plasmid

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families