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Cyanuric acid amidohydrolase (CAH) (EC 3.5.2.15) (Cyanuric acid hydrolase)

 CAH_SARSX               Reviewed;         341 AA.
U3N9N6;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
11-DEC-2013, sequence version 1.
30-AUG-2017, entry version 10.
RecName: Full=Cyanuric acid amidohydrolase {ECO:0000255|HAMAP-Rule:MF_01989};
Short=CAH {ECO:0000255|HAMAP-Rule:MF_01989};
EC=3.5.2.15 {ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:24039269};
AltName: Full=Cyanuric acid hydrolase {ECO:0000303|PubMed:24039269};
Sarocladium sp.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales;
Hypocreales incertae sedis; Sarocladium.
NCBI_TaxID=1707703;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 162-174,
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=CA;
PubMed=24039269; DOI=10.1128/JB.00965-13;
Dodge A.G., Preiner C.S., Wackett L.P.;
"Expanding the cyanuric acid hydrolase protein family to the fungal
kingdom.";
J. Bacteriol. 195:5233-5241(2013).
-!- FUNCTION: 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. Only active on cyanuric acid and N-methylisocyanuric acid.
{ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:24039269}.
-!- CATALYTIC ACTIVITY: Cyanuric acid + H(2)O = biuret + CO(2).
{ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:24039269}.
-!- ENZYME REGULATION: Inhibited by barbituric acid.
{ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:24039269}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=400 uM for cyanuric acid {ECO:0000269|PubMed:24039269};
Note=kcat is 3.4 sec(-1) with cyanuric acid as substrate.
{ECO:0000269|PubMed:24039269};
-!- PATHWAY: Xenobiotic degradation; atrazine degradation; biuret from
cyanurate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01989}.
-!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P58329,
ECO:0000255|HAMAP-Rule:MF_01989}.
-!- DOMAIN: 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). {ECO:0000255|HAMAP-
Rule:MF_01989}.
-!- SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family.
{ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000305}.
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EMBL; KF537246; AGW27430.1; -; Genomic_DNA.
SMR; U3N9N6; -.
UniPathway; UPA00008; UER00502.
GO; GO:0018753; F:cyanuric acid amidohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019381; P:atrazine catabolic process; IEA:UniProtKB-UniPathway.
HAMAP; MF_01989; Cyc_amidohydrol; 1.
InterPro; IPR014086; AtzD/Barbiturase.
Pfam; PF09663; Amido_AtzD_TrzD; 1.
TIGRFAMs; TIGR02714; amido_AtzD_TrzD; 1.
1: Evidence at protein level;
Direct protein sequencing; Hydrolase; Magnesium; Metal-binding.
CHAIN 1 341 Cyanuric acid amidohydrolase.
/FTId=PRO_0000439922.
REGION 1 90 RU A. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 71 72 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989}.
REGION 95 229 RU B. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 212 213 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989}.
REGION 235 341 RU C. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 319 320 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989}.
ACT_SITE 144 144 {ECO:0000255|HAMAP-Rule:MF_01989}.
ACT_SITE 212 212 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 273 273 Magnesium; structural.
{ECO:0000255|HAMAP-Rule:MF_01989}.
METAL 322 322 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 325 325 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 326 326 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 327 327 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 330 330 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989}.
BINDING 51 51 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989}.
BINDING 176 176 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989}.
BINDING 300 300 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989}.
SITE 296 296 Important for substrate specificity.
{ECO:0000255|HAMAP-Rule:MF_01989}.
SEQUENCE 341 AA; 35773 MW; 4FA0812A149342EA CRC64;
MAPIEILKFP ISSPGDISPL KKLQDAGYDP SNILAVVGKT EGNGCVNDFS RTLASAVWEP
RIPSDAVTIF SGGTEGVLSP HVTFFLRSPG DKETGLSAAV GHTRRFEPHE IGTDEQAQQV
ATTTSSLIEQ MGVTPDQVHM VLIKCPLLTS EKLETIRALG RVPVTTDTYE SMARSRYASA
VGIAAAVGEI QHTRIPEAVS KAGTWSAKAS CSSGAELEDC HILVLASTSA QGSRLHAVSR
PMADAMDAAS ILALMELAKK DGGKIVQVFA KAEADPSGHV REWRHTMNTD SDIHSTRHAR
AAVGGLIAGL VSDAEIYVSG GAEGQGPSGG GSLCLVYETS I


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