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Cyanuric acid amidohydrolase (CAH) (EC 3.5.2.15)

 CAH_ENTCL               Reviewed;         370 AA.
P0A3V4; O87589;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 1.
10-OCT-2018, entry version 37.
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};
Name=trzD;
Enterobacter cloacae.
Plasmid pPDL12.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
NCBI_TaxID=550;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=99;
PubMed=1991731; DOI=10.1128/jb.173.3.1363-1366.1991;
Eaton R.W., Karns J.S.;
"Cloning and comparison of the DNA encoding ammelide aminohydrolase
and cyanuric acid amidohydrolase from three s-triazine-degrading
bacterial strains.";
J. Bacteriol. 173:1363-1366(1991).
-!- 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}.
-!- CATALYTIC ACTIVITY: Cyanuric acid + H(2)O = biuret + CO(2).
{ECO:0000255|HAMAP-Rule:MF_01989}.
-!- ACTIVITY REGULATION: Inhibited by barbituric acid.
{ECO:0000255|HAMAP-Rule:MF_01989}.
-!- PATHWAY: Xenobiotic degradation; atrazine degradation; biuret from
cyanurate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01989}.
-!- SUBUNIT: Homotetramer. {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; AF342826; AAK11688.1; -; Genomic_DNA.
RefSeq; WP_031302833.1; NZ_FKBF01000014.1.
PDB; 5T13; X-ray; 2.19 A; A=1-370.
PDBsum; 5T13; -.
SMR; P0A3V4; -.
PRIDE; P0A3V4; -.
UniPathway; UPA00008; UER00502.
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;
3D-structure; Hydrolase; Magnesium; Metal-binding; Plasmid.
CHAIN 1 370 Cyanuric acid amidohydrolase.
/FTId=PRO_0000065648.
REGION 1 103 RU A. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 82 83 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989}.
REGION 113 250 RU B. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 233 234 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989}.
REGION 256 370 RU C. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 349 350 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989}.
ACT_SITE 163 163 {ECO:0000255|HAMAP-Rule:MF_01989}.
ACT_SITE 233 233 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 303 303 Magnesium; structural.
{ECO:0000255|HAMAP-Rule:MF_01989}.
METAL 352 352 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 355 355 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 356 356 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 360 360 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989}.
BINDING 51 51 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989}.
BINDING 195 195 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989}.
BINDING 330 330 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989}.
SITE 326 326 Important for substrate specificity.
{ECO:0000255|HAMAP-Rule:MF_01989}.
STRAND 1 9 {ECO:0000244|PDB:5T13}.
HELIX 17 24 {ECO:0000244|PDB:5T13}.
HELIX 30 32 {ECO:0000244|PDB:5T13}.
STRAND 33 42 {ECO:0000244|PDB:5T13}.
HELIX 50 66 {ECO:0000244|PDB:5T13}.
HELIX 70 76 {ECO:0000244|PDB:5T13}.
STRAND 77 83 {ECO:0000244|PDB:5T13}.
STRAND 92 106 {ECO:0000244|PDB:5T13}.
STRAND 113 120 {ECO:0000244|PDB:5T13}.
HELIX 126 128 {ECO:0000244|PDB:5T13}.
HELIX 132 148 {ECO:0000244|PDB:5T13}.
HELIX 154 156 {ECO:0000244|PDB:5T13}.
STRAND 157 164 {ECO:0000244|PDB:5T13}.
HELIX 169 177 {ECO:0000244|PDB:5T13}.
HELIX 187 205 {ECO:0000244|PDB:5T13}.
HELIX 211 213 {ECO:0000244|PDB:5T13}.
HELIX 216 218 {ECO:0000244|PDB:5T13}.
TURN 219 221 {ECO:0000244|PDB:5T13}.
STRAND 227 234 {ECO:0000244|PDB:5T13}.
STRAND 242 249 {ECO:0000244|PDB:5T13}.
STRAND 252 265 {ECO:0000244|PDB:5T13}.
HELIX 269 278 {ECO:0000244|PDB:5T13}.
STRAND 283 286 {ECO:0000244|PDB:5T13}.
HELIX 289 293 {ECO:0000244|PDB:5T13}.
STRAND 295 302 {ECO:0000244|PDB:5T13}.
STRAND 308 310 {ECO:0000244|PDB:5T13}.
STRAND 321 323 {ECO:0000244|PDB:5T13}.
HELIX 325 341 {ECO:0000244|PDB:5T13}.
STRAND 347 350 {ECO:0000244|PDB:5T13}.
STRAND 355 357 {ECO:0000244|PDB:5T13}.
STRAND 361 368 {ECO:0000244|PDB:5T13}.
SEQUENCE 370 AA; 39420 MW; E02B447694802035 CRC64;
MQAQVFRVPM SNPADVSGVA KLIDEGVIRA EEVVCVLGKT EGNGCVNDFT RGYTTLAFKV
YFSEKLGVSR QEVGERIAFI MSGGTEGVMA PHCTIFTVQK TDNKQKTAAE GKRLAVQQIF
TREFLPEEIG RMPQVTETAD AVRRAMREAG IADASDVHFV QVKCPLLTAG RMHDAVERGH
TVATEDTYES MGYSRGASAL GIALALGEVE KANLSDEVIT ADYSLYSSVA STSAGIELMN
NEIIVMGNSR AWGGDLVIGH AEMKDAIDGA AVRQALRDVG CCENDLPTVD ELGRVVNVFA
KAEASPDGEV RNRRHTMLDD SDINSTRHAR AVVNAVIASI VGDPMVYVSG GSEHQGPAGG
GPVAVIARTA


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