CAH_PSEUX
ID CAH_PSEUX Reviewed; 344 AA.
AC F4CUJ4;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
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 OrderedLocusNames=Psed_3188;
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Pseudonocardia.
OX NCBI_TaxID=675635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190;
RX PubMed=21725009; DOI=10.1128/jb.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
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=176 uM for cyanuric acid {ECO:0000269|PubMed:28235873};
CC Note=kcat is 56.3 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; CP002593; AEA25384.1; -; Genomic_DNA.
DR RefSeq; WP_013675305.1; NC_015312.1.
DR AlphaFoldDB; F4CUJ4; -.
DR SMR; F4CUJ4; -.
DR STRING; 675635.Psed_3188; -.
DR EnsemblBacteria; AEA25384; AEA25384; Psed_3188.
DR KEGG; pdx:Psed_3188; -.
DR eggNOG; ENOG502Z8BS; Bacteria.
DR HOGENOM; CLU_808206_0_0_11; -.
DR OMA; GRYRIGH; -.
DR OrthoDB; 984718at2; -.
DR UniPathway; UPA00008; UER00502.
DR Proteomes; UP000007809; 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; Reference proteome.
FT CHAIN 1..344
FT /note="Cyanuric acid amidohydrolase"
FT /id="PRO_0000439917"
FT REGION 1..91
FT /note="RU A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 97..232
FT /note="RU B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 238..344
FT /note="RU C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 146
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 215
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 71..72
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 215..216
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 322..323
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT SITE 299
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
SQ SEQUENCE 344 AA; 34847 MW; DF0BEFF8B6915ADD CRC64;
MTVVDIVKRT TSSPDDTALV KTLADAGYST ADVVALVAKT EGNGCVNDFS RTLADHTWDA
VLPADAVTVF SGGTEGVLSP HASAFVGTDR PAAPEGALVA AVGRTASIPI ADLGRAGQVR
AVAARVRELC ADAALEPGDV HLVLVKCPLL TTESISRCLA DGVEPATRDT LRSMAMSRAA
SALGVAVALG EISEPDAAAA LRGEADVWSS VASISSGAEL DDCHILVLGN SPAAHGPLRA
VHGVMRDAMD ARTVLDLLDR VSADGGEVVQ VLAKAEADPS GSIRGRRHTM LTDSDLSSTR
HARAAVGGLL AGLVGDSAIY VSGGAEHQGP PGGGPVTVVY RVAS
