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Cyanuric acid amidohydrolase (CAH) (EC 3.5.2.15)

 CAH_PSESD               Reviewed;         363 AA.
P58329; G8HMW5;
24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
24-OCT-2001, sequence version 1.
23-MAY-2018, entry version 49.
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:11544232, ECO:0000269|PubMed:12788776};
Name=atzD; ORFNames=AOX63_31675;
Pseudomonas sp. (strain ADP).
Plasmid pADP-1.
Bacteria; Proteobacteria.
NCBI_TaxID=47660;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
PATHWAY.
STRAIN=ADP;
PubMed=11544232; DOI=10.1128/JB.183.19.5684-5697.2001;
Martinez B., Tomkins J., Wackett L.P., Wing R., Sadowsky M.J.;
"Complete nucleotide sequence and organization of the atrazine
catabolic plasmid pADP-1 from Pseudomonas sp. strain ADP.";
J. Bacteriol. 183:5684-5697(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ADPE;
PubMed=21959051; DOI=10.1016/j.gene.2011.09.005;
Changey F., Devers-Lamrani M., Rouard N., Martin-Laurent F.;
"In vitro evolution of an atrazine-degrading population under cyanuric
acid selection pressure: Evidence for the selective loss of a 47kb
region on the plasmid ADP1 containing the atzA, B and C genes.";
Gene 490:18-25(2011).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ADP;
Devers-Lamrani M., Spor A., Mounier A., Martin-Laurent F.;
"Draft genome of the atrazine degrading bacteria Pseudomonas sp.
ADP.";
Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
STRAIN=ADP;
PubMed=12788776; DOI=10.1128/AEM.69.6.3653-3657.2003;
Fruchey I., Shapir N., Sadowsky M.J., Wackett L.P.;
"On the origins of cyanuric acid hydrolase: purification, substrates,
and prevalence of AtzD from Pseudomonas sp. strain ADP.";
Appl. Environ. Microbiol. 69:3653-3657(2003).
[5]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=22730121; DOI=10.1128/JB.00791-12;
Seffernick J.L., Erickson J.S., Cameron S.M., Cho S., Dodge A.G.,
Richman J.E., Sadowsky M.J., Wackett L.P.;
"Defining sequence space and reaction products within the cyanuric
acid hydrolase (AtzD)/barbiturase protein family.";
J. Bacteriol. 194:4579-4588(2012).
[6]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH METAL ION;
SUBSTRATE AND INHIBITOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=23651355; DOI=10.1111/mmi.12249;
Peat T.S., Balotra S., Wilding M., French N.G., Briggs L.J.,
Panjikar S., Cowieson N., Newman J., Scott C.;
"Cyanuric acid hydrolase: evolutionary innovation by structural
concatenation.";
Mol. Microbiol. 88:1149-1163(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. {ECO:0000255|HAMAP-Rule:MF_01989,
ECO:0000269|PubMed:11544232}.
-!- CATALYTIC ACTIVITY: Cyanuric acid + H(2)O = biuret + CO(2).
{ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:11544232,
ECO:0000269|PubMed:12788776}.
-!- ENZYME REGULATION: Inhibited by barbituric acid.
{ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:12788776}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=23 uM for cyanuric acid {ECO:0000269|PubMed:22730121};
KM=57 uM for cyanuric acid {ECO:0000269|PubMed:12788776};
KM=71 uM for N-methylisocyanuric acid
{ECO:0000269|PubMed:12788776};
Note=kcat is 73 sec(-1) with cyanuric acid as substrate
(PubMed:22730121). kcat is 6.8 sec(-1) with cyanuric acid as
substrate and 3.1 sec(-1) with N-methylisocyanuric acid as
substrate (PubMed:12788776). {ECO:0000269|PubMed:12788776,
ECO:0000269|PubMed:22730121};
pH dependence:
Optimum pH is 8.2. {ECO:0000269|PubMed:12788776};
-!- PATHWAY: Xenobiotic degradation; atrazine degradation; biuret from
cyanurate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01989,
ECO:0000269|PubMed:11544232}.
-!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01989,
ECO:0000269|PubMed:23651355}.
-!- 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, ECO:0000305|PubMed:23651355}.
-!- SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family.
{ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000305}.
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EMBL; U66917; AAK50331.1; -; Genomic_DNA.
EMBL; JN607164; AET43038.1; -; Genomic_DNA.
EMBL; LKAX01000023; KSW21436.1; -; Genomic_DNA.
RefSeq; NP_862537.1; NC_004956.1.
RefSeq; WP_011117191.1; NZ_CM003636.1.
PDB; 4BVQ; X-ray; 1.90 A; A/B=1-363.
PDB; 4BVR; X-ray; 2.58 A; A/B=1-363.
PDB; 4BVS; X-ray; 2.60 A; A/B=1-363.
PDB; 4BVT; X-ray; 3.10 A; A/B=1-363.
PDBsum; 4BVQ; -.
PDBsum; 4BVR; -.
PDBsum; 4BVS; -.
PDBsum; 4BVT; -.
SMR; P58329; -.
PRIDE; P58329; -.
EnsemblBacteria; KSW21436; KSW21436; AOX63_31675.
GeneID; 1440634; -.
BioCyc; MetaCyc:MONOMER-13543; -.
BRENDA; 3.5.2.15; 5085.
UniPathway; UPA00008; UER00502.
Proteomes; UP000054734; Plasmid padp1.
Proteomes; UP000054734; Unassembled WGS sequence.
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;
3D-structure; Complete proteome; Hydrolase; Magnesium; Metal-binding;
Plasmid.
CHAIN 1 363 Cyanuric acid amidohydrolase.
/FTId=PRO_0000064761.
REGION 1 104 RU A. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 83 84 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:23651355}.
REGION 112 249 RU B. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 232 233 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:23651355}.
REGION 255 363 RU C. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 343 344 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:23651355}.
ACT_SITE 162 162 {ECO:0000255|HAMAP-Rule:MF_01989}.
ACT_SITE 232 232 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_01989}.
METAL 297 297 Magnesium; structural.
{ECO:0000255|HAMAP-Rule:MF_01989,
ECO:0000269|PubMed:23651355}.
METAL 346 346 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:23651355}.
METAL 349 349 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:23651355}.
METAL 350 350 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:23651355}.
METAL 351 351 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:23651355}.
METAL 354 354 Magnesium; via carbonyl oxygen;
structural. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:23651355}.
BINDING 52 52 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:23651355}.
BINDING 194 194 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:23651355}.
BINDING 324 324 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:23651355}.
SITE 320 320 Important for substrate specificity.
{ECO:0000255|HAMAP-Rule:MF_01989,
ECO:0000305|PubMed:23651355}.
STRAND 2 10 {ECO:0000244|PDB:4BVQ}.
HELIX 18 25 {ECO:0000244|PDB:4BVQ}.
HELIX 31 33 {ECO:0000244|PDB:4BVQ}.
STRAND 34 43 {ECO:0000244|PDB:4BVQ}.
HELIX 51 67 {ECO:0000244|PDB:4BVQ}.
HELIX 71 77 {ECO:0000244|PDB:4BVQ}.
STRAND 78 84 {ECO:0000244|PDB:4BVQ}.
STRAND 93 101 {ECO:0000244|PDB:4BVQ}.
STRAND 112 119 {ECO:0000244|PDB:4BVQ}.
HELIX 125 127 {ECO:0000244|PDB:4BVQ}.
HELIX 131 148 {ECO:0000244|PDB:4BVQ}.
HELIX 153 155 {ECO:0000244|PDB:4BVQ}.
STRAND 156 163 {ECO:0000244|PDB:4BVQ}.
HELIX 168 176 {ECO:0000244|PDB:4BVQ}.
HELIX 186 204 {ECO:0000244|PDB:4BVQ}.
HELIX 210 212 {ECO:0000244|PDB:4BVQ}.
HELIX 215 217 {ECO:0000244|PDB:4BVQ}.
TURN 218 220 {ECO:0000244|PDB:4BVQ}.
STRAND 226 233 {ECO:0000244|PDB:4BVQ}.
STRAND 241 248 {ECO:0000244|PDB:4BVQ}.
STRAND 254 264 {ECO:0000244|PDB:4BVQ}.
HELIX 268 277 {ECO:0000244|PDB:4BVQ}.
HELIX 283 288 {ECO:0000244|PDB:4BVQ}.
STRAND 289 296 {ECO:0000244|PDB:4BVQ}.
STRAND 302 304 {ECO:0000244|PDB:4BVQ}.
TURN 311 313 {ECO:0000244|PDB:4BVQ}.
STRAND 315 317 {ECO:0000244|PDB:4BVQ}.
HELIX 319 335 {ECO:0000244|PDB:4BVQ}.
STRAND 336 338 {ECO:0000244|PDB:4BVQ}.
STRAND 340 344 {ECO:0000244|PDB:4BVQ}.
STRAND 349 351 {ECO:0000244|PDB:4BVQ}.
STRAND 355 362 {ECO:0000244|PDB:4BVQ}.
SEQUENCE 363 AA; 38200 MW; 140256C30D82FF83 CRC64;
MYHIDVFRIP CHSPGDTSGL EDLIETGRVA PADIVAVMGK TEGNGCVNDY TREYATAMLA
ACLGRHLQLP PHEVEKRVAF VMSGGTEGVL SPHHTVFARR PAIDAHRPAG KRLTLGIAFT
RDFLPEEIGR HAQITETAGA VKRAMRDAGI ASIDDLHFVQ VKCPLLTPAK IASARSRGCA
PVTTDTYESM GYSRGASALG IALATEEVPS SMLVDESVLN DWSLSSSLAS ASAGIELEHN
VVIAIGMSEQ ATSELVIAHG VMSDAIDAAS VRRTIESLGI RSDDEMDRIV NVFAKAEASP
DGVVRGMRHT MLSDSDINST RHARAVTGAA IASVVGHGMV YVSGGAEHQG PAGGGPFAVI
ARA


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