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Cyanuric acid amidohydrolase (CAH) (EC 3.5.2.15)

 A0A1D7XDV5_MOOTH        Unreviewed;       367 AA.
A0A1D7XDV5;
18-JAN-2017, integrated into UniProtKB/TrEMBL.
18-JAN-2017, sequence version 1.
12-SEP-2018, entry version 7.
RecName: Full=Cyanuric acid amidohydrolase {ECO:0000256|HAMAP-Rule:MF_01989};
Short=CAH {ECO:0000256|HAMAP-Rule:MF_01989};
EC=3.5.2.15 {ECO:0000256|HAMAP-Rule:MF_01989};
Name=trzD {ECO:0000313|EMBL:AOQ25085.1};
ORFNames=Maut_02669 {ECO:0000313|EMBL:AOQ25085.1};
Moorella thermoacetica (Clostridium thermoaceticum).
Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
Thermoanaerobacteraceae; Moorella group; Moorella.
NCBI_TaxID=1525 {ECO:0000313|EMBL:AOQ25085.1, ECO:0000313|Proteomes:UP000094598};
[1] {ECO:0000313|EMBL:AOQ25085.1, ECO:0000313|Proteomes:UP000094598}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 103132 {ECO:0000313|EMBL:AOQ25085.1,
ECO:0000313|Proteomes:UP000094598};
Jendresen C.B., Redl S.M., Jensen T.O., Nielsen A.T.;
"Moorella thermoacetica DSM 103132.";
Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
-!- 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:0000256|HAMAP-Rule:MF_01989}.
-!- CATALYTIC ACTIVITY: Cyanuric acid + H(2)O = biuret + CO(2).
{ECO:0000256|HAMAP-Rule:MF_01989}.
-!- ACTIVITY REGULATION: Inhibited by barbituric acid.
{ECO:0000256|HAMAP-Rule:MF_01989}.
-!- PATHWAY: Xenobiotic degradation; atrazine degradation; biuret from
cyanurate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01989}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|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:0000256|HAMAP-
Rule:MF_01989}.
-!- SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family.
{ECO:0000256|HAMAP-Rule:MF_01989}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01989}.
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EMBL; CP017019; AOQ25085.1; -; Genomic_DNA.
RefSeq; WP_069590999.1; NZ_CP017019.1.
EnsemblBacteria; AOQ25085; AOQ25085; Maut_02669.
PATRIC; fig|1525.5.peg.2856; -.
UniPathway; UPA00008; UER00502.
Proteomes; UP000094598; Chromosome.
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.
3: Inferred from homology;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000094598};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01989,
ECO:0000313|EMBL:AOQ25085.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01989};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01989}.
REGION 1 103 RU A. {ECO:0000256|HAMAP-Rule:MF_01989}.
REGION 83 84 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01989}.
REGION 111 248 RU B. {ECO:0000256|HAMAP-Rule:MF_01989}.
REGION 231 232 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01989}.
REGION 254 367 RU C. {ECO:0000256|HAMAP-Rule:MF_01989}.
REGION 347 348 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01989}.
COILED 130 150 {ECO:0000256|SAM:Coils}.
ACT_SITE 161 161 {ECO:0000256|HAMAP-Rule:MF_01989}.
ACT_SITE 231 231 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_01989}.
METAL 301 301 Magnesium; structural.
{ECO:0000256|HAMAP-Rule:MF_01989}.
METAL 350 350 Magnesium; via carbonyl oxygen;
structural. {ECO:0000256|HAMAP-
Rule:MF_01989}.
METAL 353 353 Magnesium; via carbonyl oxygen;
structural. {ECO:0000256|HAMAP-
Rule:MF_01989}.
METAL 354 354 Magnesium; via carbonyl oxygen;
structural. {ECO:0000256|HAMAP-
Rule:MF_01989}.
METAL 355 355 Magnesium; via carbonyl oxygen;
structural. {ECO:0000256|HAMAP-
Rule:MF_01989}.
METAL 358 358 Magnesium; via carbonyl oxygen;
structural. {ECO:0000256|HAMAP-
Rule:MF_01989}.
BINDING 52 52 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01989}.
BINDING 193 193 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01989}.
BINDING 328 328 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01989}.
SITE 324 324 Important for substrate specificity.
{ECO:0000256|HAMAP-Rule:MF_01989}.
SEQUENCE 367 AA; 38872 MW; 6F1542BFDC00B579 CRC64;
MQKVEVFRIP TASPDDISGL ATLIDSGKIN PAEIVAILGK TEGNGCVNDF TRGFATQSLA
MYLAEKLGIS REEVVKKVAF IMSGGTEGVM TPHITVFVRK DVQEPAKPGK RLAVGVAFTR
DFLPEELGRM EQVNEVARAV KEAMKDAQID DPRDVHFVQI KCPLLTAERI EDAKRRGKDV
VVNDTYKSMA YSRGASALGV ALALGEISAD KISNEAICHD WNLYSSVAST SAGVELLNDE
IIVVGNSTNS ASDLVIGHSV MKDAIDADAV RAALKDAGLK FDCCPPAEEL AKIVNVLAKA
EAASSGTVRG RRNTMLDDSD INHTRSARAV VNAVIASVVG DPMVYVSGGA EHQGPDGGGP
IAVIAKV


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