CAH_METS4
ID CAH_METS4 Reviewed; 369 AA.
AC B0UET5;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Cyanuric acid amidohydrolase {ECO:0000255|HAMAP-Rule:MF_01989};
DE Short=CAH {ECO:0000255|HAMAP-Rule:MF_01989};
DE EC=3.5.2.15 {ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:22730121};
GN OrderedLocusNames=M446_3816;
OS Methylobacterium sp. (strain 4-46).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4-46;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium sp. 4-46.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22730121; DOI=10.1128/jb.00791-12;
RA Seffernick J.L., Erickson J.S., Cameron S.M., Cho S., Dodge A.G.,
RA Richman J.E., Sadowsky M.J., Wackett L.P.;
RT "Defining sequence space and reaction products within the cyanuric acid
RT hydrolase (AtzD)/barbiturase protein family.";
RL J. Bacteriol. 194:4579-4588(2012).
CC -!- FUNCTION: Responsible for the hydrolysis of cyanuric acid, an
CC intermediate formed during catabolism of s-triazine based compounds in
CC herbicides such as atrazine and polymers such as melamine. Catalyzes
CC the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-
CC trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which
CC spontaneously decarboxylates to biuret. {ECO:0000255|HAMAP-
CC Rule:MF_01989, ECO:0000269|PubMed:22730121}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyanurate + H2O = 1-carboxybiuret + H(+);
CC Xref=Rhea:RHEA:70363, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:38028, ChEBI:CHEBI:142864; EC=3.5.2.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01989,
CC ECO:0000269|PubMed:22730121};
CC -!- ACTIVITY REGULATION: Inhibited by barbituric acid.
CC {ECO:0000250|UniProtKB:P58329, ECO:0000255|HAMAP-Rule:MF_01989}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=69 uM for cyanuric acid {ECO:0000269|PubMed:22730121};
CC Note=kcat is 17 sec(-1) with cyanuric acid as substrate.
CC {ECO:0000269|PubMed:22730121};
CC -!- PATHWAY: Xenobiotic degradation; atrazine degradation; biuret from
CC cyanurate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01989}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P58329,
CC ECO:0000255|HAMAP-Rule:MF_01989}.
CC -!- DOMAIN: The monomer structure is formed from three repeating units
CC (RUs) that share the same structure as one another. The monomer, the
CC active site and substrate all possess threefold rotational symmetry, to
CC the extent that the active site possesses three potential Ser-Lys
CC catalytic dyads. It is possible that any or all of the three active-
CC site serines may act as nucleophile (albeit only one can do so per
CC catalytic cycle). {ECO:0000255|HAMAP-Rule:MF_01989}.
CC -!- SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family.
CC {ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000305}.
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DR EMBL; CP000943; ACA18193.1; -; Genomic_DNA.
DR RefSeq; WP_012333591.1; NC_010511.1.
DR AlphaFoldDB; B0UET5; -.
DR SMR; B0UET5; -.
DR STRING; 426117.M446_3816; -.
DR EnsemblBacteria; ACA18193; ACA18193; M446_3816.
DR KEGG; met:M446_3816; -.
DR eggNOG; ENOG502Z8BS; Bacteria.
DR HOGENOM; CLU_808206_0_0_5; -.
DR OMA; GRYRIGH; -.
DR OrthoDB; 984718at2; -.
DR UniPathway; UPA00008; UER00502.
DR GO; GO:0018753; F:cyanuric acid amidohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019381; P:atrazine catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1330.160; -; 1.
DR Gene3D; 3.30.1330.170; -; 1.
DR Gene3D; 3.30.1330.180; -; 1.
DR HAMAP; MF_01989; Cyc_amidohydrol; 1.
DR InterPro; IPR014086; AtzD/Barbiturase.
DR InterPro; IPR043008; AtzD/Barbiturase_RUA.
DR InterPro; IPR043006; AtzD/Barbiturase_RUB.
DR InterPro; IPR043007; AtzD/Barbiturase_RUC.
DR Pfam; PF09663; Amido_AtzD_TrzD; 1.
DR TIGRFAMs; TIGR02714; amido_AtzD_TrzD; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..369
FT /note="Cyanuric acid amidohydrolase"
FT /id="PRO_0000439914"
FT REGION 1..100
FT /note="RU A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 106..242
FT /note="RU B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 248..369
FT /note="RU C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 155
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 225
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 81..82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 225..226
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 342..343
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 350
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT SITE 319
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
SQ SEQUENCE 369 AA; 37174 MW; 4DA30CC5D9DD58E6 CRC64;
MPRRAEILRL PMAAPDDVSA IAASLRDGRL DPGDVVAVFA KTEGNGCVND FTRPLAVQAL
RGLFGPLIGE AALGRIAMVM SGGTEGGLSP HWLVIAAREA AGPGPALAVG QARTPPLAAE
DLGRRAQVEM VAAGVRAAMR EAGLDAGQVH YVQVKCPLLT SERIGAALAR GAAPATRDTL
KSMGLSRAAA ALGAALALGE VPAAAIGETV AETDPGRHAR RCGASAGVEL LDHEVVVMGM
SPDWTGPLVI DHAVMADAID LRPVAACLGR LGLLGPDGFV DEAGRARLAA LLAKAEASAD
GAIRGRRHTM LTDSDIAPTR HARGFVAGAL AGLVGATDLF VSGGAEFQGP DGGGPVAVIA
RRSGAAGPA
