CAH_BRAS3
ID CAH_BRAS3 Reviewed; 372 AA.
AC H0SH23;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 28.
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:28235873};
GN ORFNames=BRAO375_2640015;
OS Bradyrhizobium sp. (strain ORS 375).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=566679;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS375;
RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA Smith A.A.T., Giraud E., Medigue C., Moulin L.;
RT "Comparative Genomics of Aeschynomene Symbionts: Insights into the
RT Ecological Lifestyle of Nod-Independent Photosynthetic Bradyrhizobia.";
RL Genes (Basel) 3:35-61(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=28235873; DOI=10.1128/aem.03365-16;
RA Peat T.S., Balotra S., Wilding M., Hartley C.J., Newman J., Scott C.;
RT "High resolution X-ray structures of two functionally distinct members of
RT the cyclic amide hydrolase (CyAH) family of Toblerone fold enzymes.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
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:28235873}.
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:28235873};
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 Note=kcat/KM is with cyanuric acid as substrate.
CC {ECO:0000269|PubMed:28235873};
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; CAFI01000184; CCD93500.1; -; Genomic_DNA.
DR RefSeq; WP_009028459.1; NZ_CAFI01000184.1.
DR AlphaFoldDB; H0SH23; -.
DR SMR; H0SH23; -.
DR EnsemblBacteria; CCD93500; CCD93500; BRAO375_2640015.
DR UniPathway; UPA00008; UER00502.
DR Proteomes; UP000003055; Unassembled WGS sequence.
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..372
FT /note="Cyanuric acid amidohydrolase"
FT /id="PRO_0000439913"
FT REGION 1..105
FT /note="RU A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 115..252
FT /note="RU B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 258..372
FT /note="RU C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 165
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 235
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 84..85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 235..236
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 351..352
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 358
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT SITE 328
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
SQ SEQUENCE 372 AA; 38930 MW; 1C303D8DDFEAD90D CRC64;
MPTTLRRAHV HRLPMRSPDD VAALEAAITQ GTIDPAGIVA ILGKTEGNGC VNDFTRAFAV
RSLEALLGRH LATEAVRQIA MVMSGGTEGA LSPHMIVFEA REVDEGHAPR AFAASLALGR
ARTPVLPSEH LGRMQQVAQV AAGVRAAMND AGITDAGDVH YVQVKCPLLT MERIEAAEAR
GVRTAVRDTL KSMGFSRGAS ALGVAVALGE LAMDELSDTE ICTDYARYSE RAATSGGVEL
LDHEIMVAGM SRDWTGPLAI DHGVMRDAID IEPARAALAR LGLDVPGQLP AAARGRIAAV
LAKAEAAQSG KVRDVRHTML DDSDVSSTRH ARAFVGGALA GLFGFTDLFV SGGAEHQGPD
GGGPVAIIVE RT
