CAH_PSEP5
ID CAH_PSEP5 Reviewed; 363 AA.
AC W6RJ11;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Cyanuric acid amidohydrolase {ECO:0000255|HAMAP-Rule:MF_01989};
DE Short=CAH {ECO:0000255|HAMAP-Rule:MF_01989};
DE EC=3.5.2.15 {ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:28235873};
GN ORFNames=BN5_3198;
OS Pseudomonas pseudoalcaligenes (strain CECT 5344).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas;
OC Pseudomonas oleovorans/pseudoalcaligenes group.
OX NCBI_TaxID=1182590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5344;
RA Wibberg D., Puehler A., Schlueter A.;
RT "Complete genome sequence of the cyanide-degrading bacterium Pseudomonas
RT pseudoalcaligenes CECT 5344.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=28235873; DOI=10.1128/aem.03365-16;
RA Peat T.S., Balotra S., Wilding M., Hartley C.J., Newman J., Scott C.;
RT "High resolution X-ray structures of two functionally distinct members of
RT the cyclic amide hydrolase (CyAH) family of Toblerone fold enzymes.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
CC -!- FUNCTION: Responsible for the hydrolysis of cyanuric acid, an
CC intermediate formed during catabolism of s-triazine based compounds in
CC herbicides such as atrazine and polymers such as melamine. Catalyzes
CC the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-
CC trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which
CC spontaneously decarboxylates to biuret. {ECO:0000255|HAMAP-
CC Rule:MF_01989, ECO:0000269|PubMed:28235873}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyanurate + H2O = 1-carboxybiuret + H(+);
CC Xref=Rhea:RHEA:70363, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:38028, ChEBI:CHEBI:142864; EC=3.5.2.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01989,
CC ECO:0000269|PubMed:28235873};
CC -!- ACTIVITY REGULATION: Inhibited by barbituric acid.
CC {ECO:0000250|UniProtKB:P58329, ECO:0000255|HAMAP-Rule:MF_01989}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=79 uM for cyanuric acid {ECO:0000269|PubMed:28235873};
CC Note=kcat is 2.2 sec(-1) with cyanuric acid as substrate.
CC {ECO:0000269|PubMed:28235873};
CC -!- PATHWAY: Xenobiotic degradation; atrazine degradation; biuret from
CC cyanurate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01989}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P58329,
CC ECO:0000255|HAMAP-Rule:MF_01989}.
CC -!- DOMAIN: The monomer structure is formed from three repeating units
CC (RUs) that share the same structure as one another. The monomer, the
CC active site and substrate all possess threefold rotational symmetry, to
CC the extent that the active site possesses three potential Ser-Lys
CC catalytic dyads. It is possible that any or all of the three active-
CC site serines may act as nucleophile (albeit only one can do so per
CC catalytic cycle). {ECO:0000255|HAMAP-Rule:MF_01989}.
CC -!- SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family.
CC {ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000305}.
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DR EMBL; HG916826; CDM41754.1; -; Genomic_DNA.
DR RefSeq; WP_003459769.1; NZ_HG916826.1.
DR AlphaFoldDB; W6RJ11; -.
DR SMR; W6RJ11; -.
DR STRING; 1182590.BN5_00871; -.
DR EnsemblBacteria; CDM41754; CDM41754; BN5_3198.
DR GeneID; 61800832; -.
DR KEGG; ppse:BN5_3198; -.
DR eggNOG; ENOG502Z8BS; Bacteria.
DR HOGENOM; CLU_808206_0_0_6; -.
DR UniPathway; UPA00008; UER00502.
DR Proteomes; UP000032841; Chromosome.
DR GO; GO:0018753; F:cyanuric acid amidohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019381; P:atrazine catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1330.160; -; 1.
DR Gene3D; 3.30.1330.170; -; 1.
DR Gene3D; 3.30.1330.180; -; 1.
DR HAMAP; MF_01989; Cyc_amidohydrol; 1.
DR InterPro; IPR014086; AtzD/Barbiturase.
DR InterPro; IPR043008; AtzD/Barbiturase_RUA.
DR InterPro; IPR043006; AtzD/Barbiturase_RUB.
DR InterPro; IPR043007; AtzD/Barbiturase_RUC.
DR Pfam; PF09663; Amido_AtzD_TrzD; 1.
DR TIGRFAMs; TIGR02714; amido_AtzD_TrzD; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..363
FT /note="Cyanuric acid amidohydrolase"
FT /id="PRO_0000439916"
FT REGION 1..103
FT /note="RU A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 111..247
FT /note="RU B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 253..363
FT /note="RU C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 161
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 230
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 230..231
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 343..344
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 350
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT SITE 320
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
SQ SEQUENCE 363 AA; 38279 MW; CD49AFAFAD3BC16A CRC64;
MKTRVTRLTV AAPNDVSALA QAIESGEVDP TRVIAVLGKT EGNGCVNDFT RAFATSTLKR
FFAERLALNE TEVDERIAFV MSGGTEGGLS PHWLVFEVDD SAPSRDTTTP GLAAGVAFTR
DLRPEEIGRT SQVELTRDAV LRAMAAAGIQ RVEDVHFVQI KCPLLTAARI NEAAARGQSV
ACHDTYESMG YSRGASALGV AAALGDLPGD VRDEQICREW SLYSSRASSS AGIELLRNEV
LVLGNAPGWD PEYRIGHAVM EDALDAQAIE RALASVPGGD KIKLTPERLA GLLVKAEPSA
SGSIRGNRHV MSDDSDINGS RHARALVGGV LAGQLGDTRL FVSGGAEHQG PNGGGPLALI
VRS
