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Cyanuric acid amidohydrolase (CAH) (EC 3.5.2.15)

 CAH_AZOC5               Reviewed;         356 AA.
A8IKD2;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 1.
05-JUL-2017, entry version 51.
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:22730121};
OrderedLocusNames=AZC_3892;
Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 /
NBRC 14845 / NCIMB 13405 / ORS 571).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Xanthobacteraceae; Azorhizobium.
NCBI_TaxID=438753;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 /
ORS 571;
Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T.,
Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B.,
Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M.,
Oyaizu H.;
"Complete genome sequence of the nitrogen-fixing bacterium
Azorhizobium caulinodans ORS571.";
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION, CATALYTIC ACTIVITY, AND 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).
[3]
SUBUNIT.
PubMed=23908033; DOI=10.1107/S1744309113017077;
Cho S., Shi K., Wackett L.P., Aihara H.;
"Crystallization and preliminary X-ray diffraction studies of cyanuric
acid hydrolase from Azorhizobium caulinodans.";
Acta Crystallogr. F 69:880-883(2013).
[4]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
INHIBIOR, ACTIVE SITE, AND MUTAGENESIS OF LYS-40; SER-79; LYS-156;
SER-226; LYS-285 AND SER-333.
PubMed=24915109; DOI=10.1371/journal.pone.0099349;
Cho S., Shi K., Seffernick J.L., Dodge A.G., Wackett L.P., Aihara H.;
"Cyanuric acid hydrolase from Azorhizobium caulinodans ORS 571:
crystal structure and insights into a new class of Ser-Lys dyad
proteins.";
PLoS ONE 9:E99349-E99349(2014).
-!- 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:22730121}.
-!- CATALYTIC ACTIVITY: Cyanuric acid + H(2)O = biuret + CO(2).
{ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:22730121}.
-!- ENZYME REGULATION: Inhibited by barbituric acid.
{ECO:0000250|UniProtKB:P58329, ECO:0000255|HAMAP-Rule:MF_01989}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=370 uM for cyanuric acid {ECO:0000269|PubMed:22730121};
Note=kcat is 50 sec(-1) with cyanuric acid as substrate.
{ECO:0000269|PubMed:22730121};
-!- 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,
ECO:0000269|PubMed:23908033}.
-!- 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). Mutant, bioinformatic and
structural data propose one specific dyad being involved in
catalysis. {ECO:0000255|HAMAP-Rule:MF_01989,
ECO:0000305|PubMed:24915109}.
-!- SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family.
{ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000305}.
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EMBL; AP009384; BAF89890.1; -; Genomic_DNA.
RefSeq; WP_012172412.1; NC_009937.1.
PDB; 4NQ3; X-ray; 2.70 A; A/B=1-356.
PDBsum; 4NQ3; -.
SMR; A8IKD2; -.
STRING; 438753.AZC_3892; -.
EnsemblBacteria; BAF89890; BAF89890; AZC_3892.
KEGG; azc:AZC_3892; -.
eggNOG; ENOG4105CWN; Bacteria.
eggNOG; ENOG410XP9R; LUCA.
HOGENOM; HOG000223772; -.
KO; K03383; -.
OMA; GRYRIGH; -.
OrthoDB; POG091H115Q; -.
UniPathway; UPA00008; UER00502.
Proteomes; UP000000270; Chromosome.
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;
Reference proteome.
CHAIN 1 356 Cyanuric acid amidohydrolase.
/FTId=PRO_0000439909.
REGION 1 99 RU A. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 79 80 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
REGION 106 243 RU B. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 226 227 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
REGION 249 356 RU C. {ECO:0000255|HAMAP-Rule:MF_01989}.
REGION 333 334 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
ACT_SITE 156 156 {ECO:0000255|HAMAP-Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
ACT_SITE 226 226 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
METAL 287 287 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
METAL 336 336 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
METAL 339 339 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
METAL 340 340 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
METAL 341 341 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
METAL 344 344 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
BINDING 52 52 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
BINDING 188 188 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
BINDING 314 314 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01989,
ECO:0000269|PubMed:24915109}.
SITE 310 310 Important for substrate specificity.
{ECO:0000255|HAMAP-Rule:MF_01989}.
MUTAGEN 40 40 K->A: Reduces catalytic activity 1e4-
fold. {ECO:0000269|PubMed:24915109}.
MUTAGEN 79 79 S->A: Reduces catalytic activity 1e8-
fold. {ECO:0000269|PubMed:24915109}.
MUTAGEN 156 156 K->A: Reduces catalytic activity 1e4-
fold. {ECO:0000269|PubMed:24915109}.
MUTAGEN 226 226 S->A: Reduces catalytic activity 1e9-
fold. {ECO:0000269|PubMed:24915109}.
MUTAGEN 285 285 K->A: Reduces catalytic activity 1e4-
fold. {ECO:0000269|PubMed:24915109}.
MUTAGEN 333 333 S->A: Reduces catalytic activity 1e8-
fold. {ECO:0000269|PubMed:24915109}.
STRAND 2 10 {ECO:0000244|PDB:4NQ3}.
HELIX 18 25 {ECO:0000244|PDB:4NQ3}.
HELIX 31 33 {ECO:0000244|PDB:4NQ3}.
STRAND 34 43 {ECO:0000244|PDB:4NQ3}.
HELIX 51 67 {ECO:0000244|PDB:4NQ3}.
HELIX 68 73 {ECO:0000244|PDB:4NQ3}.
STRAND 74 80 {ECO:0000244|PDB:4NQ3}.
STRAND 89 97 {ECO:0000244|PDB:4NQ3}.
STRAND 106 113 {ECO:0000244|PDB:4NQ3}.
TURN 119 123 {ECO:0000244|PDB:4NQ3}.
HELIX 125 141 {ECO:0000244|PDB:4NQ3}.
HELIX 147 149 {ECO:0000244|PDB:4NQ3}.
STRAND 150 157 {ECO:0000244|PDB:4NQ3}.
HELIX 162 170 {ECO:0000244|PDB:4NQ3}.
HELIX 180 199 {ECO:0000244|PDB:4NQ3}.
HELIX 204 206 {ECO:0000244|PDB:4NQ3}.
TURN 209 214 {ECO:0000244|PDB:4NQ3}.
STRAND 220 227 {ECO:0000244|PDB:4NQ3}.
STRAND 235 242 {ECO:0000244|PDB:4NQ3}.
STRAND 246 258 {ECO:0000244|PDB:4NQ3}.
HELIX 263 271 {ECO:0000244|PDB:4NQ3}.
STRAND 281 286 {ECO:0000244|PDB:4NQ3}.
STRAND 292 294 {ECO:0000244|PDB:4NQ3}.
STRAND 305 307 {ECO:0000244|PDB:4NQ3}.
HELIX 309 325 {ECO:0000244|PDB:4NQ3}.
STRAND 331 334 {ECO:0000244|PDB:4NQ3}.
STRAND 339 341 {ECO:0000244|PDB:4NQ3}.
STRAND 345 352 {ECO:0000244|PDB:4NQ3}.
SEQUENCE 356 AA; 36040 MW; 231B48FE327A4E3C CRC64;
MPIAKVHRIA TASPDDVSGL AAAIATGAIA PAGILAIFGK TEGNGCVNDF SRGFAVQSLQ
MLLRGHMGAA ADEVCLVMSG GTEGGMSPHF LVFERAEGNA PEAAPALAIG RAHTPDLPFE
ALGRMGQVRM VAQAVRRAMA AAGITDPEDV HFVQVKCPLL TAMRVKEAEA RGATTATSDT
LKSMGLSRGA SALGIALALG EVAEDALSDA VICADYGLWS ARASCSSGIE LLGHEIVVLG
MSEGWSGPLA IAHGVMADAI DVTPVKAALS ALGAEAGEAT IVLAKAEPSR SGRIRGKRHT
MLDDSDISPT RHARAFVAGA LAGVVGHTEI YVSGGGEHQG PDGGGPVAVI AARTMG


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