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Cyanuric acid amidohydrolase (CAH) (EC 3.5.2.15)

 CAH_BRAS3               Reviewed;         372 AA.
H0SH23;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
22-FEB-2012, sequence version 1.
10-OCT-2018, entry version 19.
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:28235873};
ORFNames=BRAO375_2640015;
Bradyrhizobium sp. (strain ORS 375).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Bradyrhizobiaceae; Bradyrhizobium.
NCBI_TaxID=566679;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ORS375;
Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
Smith A.A.T., Giraud E., Medigue C., Moulin L.;
"Comparative Genomics of Aeschynomene Symbionts: Insights into the
Ecological Lifestyle of Nod-Independent Photosynthetic
Bradyrhizobia.";
Genes (Basel) 3:35-61(2012).
[2]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=28235873; DOI=10.1128/AEM.03365-16;
Peat T.S., Balotra S., Wilding M., Hartley C.J., Newman J., Scott C.;
"High resolution X-ray structures of two functionally distinct members
of the cyclic amide hydrolase (CyAH) family of Toblerone fold
enzymes.";
Appl. Environ. Microbiol. 0:0-0(2017).
-!- 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. {ECO:0000255|HAMAP-Rule:MF_01989,
ECO:0000269|PubMed:28235873}.
-!- CATALYTIC ACTIVITY: Cyanuric acid + H(2)O = biuret + CO(2).
{ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:28235873}.
-!- ACTIVITY REGULATION: Inhibited by barbituric acid.
{ECO:0000250|UniProtKB:P58329, ECO:0000255|HAMAP-Rule:MF_01989}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=kcat/KM is with cyanuric acid as substrate.
{ECO:0000269|PubMed:28235873};
-!- 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; CAFI01000184; CCD93500.1; -; Genomic_DNA.
RefSeq; WP_009028459.1; NZ_CAFI01000184.1.
SMR; H0SH23; -.
EnsemblBacteria; CCD93500; CCD93500; BRAO375_2640015.
OrthoDB; POG091H115Q; -.
UniPathway; UPA00008; UER00502.
Proteomes; UP000003055; Unassembled WGS sequence.
GO; GO:0018753; F:cyanuric acid amidohydrolase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0019381; P:atrazine catabolic process; IEA:UniProtKB-UniRule.
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;
Complete proteome; Hydrolase; Magnesium; Metal-binding.
CHAIN 1 372 Cyanuric acid amidohydrolase.
/FTId=PRO_0000439913.
REGION 1 105 RU A. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 84 85 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989}.
REGION 115 252 RU B. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 235 236 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989}.
REGION 258 372 RU C. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 351 352 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989}.
ACT_SITE 165 165 {ECO:0000255|HAMAP-Rule:MF_01989}.
ACT_SITE 235 235 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 305 305 Magnesium; structural.
{ECO:0000255|HAMAP-Rule:MF_01989}.
METAL 354 354 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 357 357 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 358 358 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 359 359 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 362 362 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989}.
BINDING 56 56 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989}.
BINDING 197 197 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989}.
BINDING 332 332 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989}.
SITE 328 328 Important for substrate specificity.
{ECO:0000255|HAMAP-Rule:MF_01989}.
SEQUENCE 372 AA; 38930 MW; 1C303D8DDFEAD90D CRC64;
MPTTLRRAHV HRLPMRSPDD VAALEAAITQ GTIDPAGIVA ILGKTEGNGC VNDFTRAFAV
RSLEALLGRH LATEAVRQIA MVMSGGTEGA LSPHMIVFEA REVDEGHAPR AFAASLALGR
ARTPVLPSEH LGRMQQVAQV AAGVRAAMND AGITDAGDVH YVQVKCPLLT MERIEAAEAR
GVRTAVRDTL KSMGFSRGAS ALGVAVALGE LAMDELSDTE ICTDYARYSE RAATSGGVEL
LDHEIMVAGM SRDWTGPLAI DHGVMRDAID IEPARAALAR LGLDVPGQLP AAARGRIAAV
LAKAEAAQSG KVRDVRHTML DDSDVSSTRH ARAFVGGALA GLFGFTDLFV SGGAEHQGPD
GGGPVAIIVE RT


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