CAH_PSESD
ID CAH_PSESD Reviewed; 363 AA.
AC P58329; G8HMW5;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 61.
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:11544232, ECO:0000269|PubMed:12788776};
GN Name=atzD; ORFNames=AOX63_31675;
OS Pseudomonas sp. (strain ADP).
OG Plasmid pADP-1.
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=47660;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=ADP;
RX PubMed=11544232; DOI=10.1128/jb.183.19.5684-5697.2001;
RA Martinez B., Tomkins J., Wackett L.P., Wing R., Sadowsky M.J.;
RT "Complete nucleotide sequence and organization of the atrazine catabolic
RT plasmid pADP-1 from Pseudomonas sp. strain ADP.";
RL J. Bacteriol. 183:5684-5697(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ADPE;
RX PubMed=21959051; DOI=10.1016/j.gene.2011.09.005;
RA Changey F., Devers-Lamrani M., Rouard N., Martin-Laurent F.;
RT "In vitro evolution of an atrazine-degrading population under cyanuric acid
RT selection pressure: Evidence for the selective loss of a 47kb region on the
RT plasmid ADP1 containing the atzA, B and C genes.";
RL Gene 490:18-25(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADP;
RA Devers-Lamrani M., Spor A., Mounier A., Martin-Laurent F.;
RT "Draft genome of the atrazine degrading bacteria Pseudomonas sp. ADP.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=ADP;
RX PubMed=12788776; DOI=10.1128/aem.69.6.3653-3657.2003;
RA Fruchey I., Shapir N., Sadowsky M.J., Wackett L.P.;
RT "On the origins of cyanuric acid hydrolase: purification, substrates, and
RT prevalence of AtzD from Pseudomonas sp. strain ADP.";
RL Appl. Environ. Microbiol. 69:3653-3657(2003).
RN [5]
RP 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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH METAL ION; SUBSTRATE
RP AND INHIBITOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=23651355; DOI=10.1111/mmi.12249;
RA Peat T.S., Balotra S., Wilding M., French N.G., Briggs L.J., Panjikar S.,
RA Cowieson N., Newman J., Scott C.;
RT "Cyanuric acid hydrolase: evolutionary innovation by structural
RT concatenation.";
RL Mol. Microbiol. 88:1149-1163(2013).
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:11544232}.
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:11544232, ECO:0000269|PubMed:12788776};
CC -!- ACTIVITY REGULATION: Inhibited by barbituric acid. {ECO:0000255|HAMAP-
CC Rule:MF_01989, ECO:0000269|PubMed:12788776}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23 uM for cyanuric acid {ECO:0000269|PubMed:22730121};
CC KM=57 uM for cyanuric acid {ECO:0000269|PubMed:12788776};
CC KM=71 uM for N-methylisocyanuric acid {ECO:0000269|PubMed:12788776};
CC Note=kcat is 73 sec(-1) with cyanuric acid as substrate
CC (PubMed:22730121). kcat is 6.8 sec(-1) with cyanuric acid as
CC substrate and 3.1 sec(-1) with N-methylisocyanuric acid as substrate
CC (PubMed:12788776). {ECO:0000269|PubMed:12788776,
CC ECO:0000269|PubMed:22730121};
CC pH dependence:
CC Optimum pH is 8.2. {ECO:0000269|PubMed:12788776};
CC -!- PATHWAY: Xenobiotic degradation; atrazine degradation; biuret from
CC cyanurate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01989,
CC ECO:0000269|PubMed:11544232}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01989,
CC ECO:0000269|PubMed:23651355}.
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 ECO:0000305|PubMed:23651355}.
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; U66917; AAK50331.1; -; Genomic_DNA.
DR EMBL; JN607164; AET43038.1; -; Genomic_DNA.
DR EMBL; LKAX01000023; KSW21436.1; -; Genomic_DNA.
DR RefSeq; NP_862537.1; NC_004956.1.
DR RefSeq; WP_011117191.1; NC_004956.1.
DR PDB; 4BVQ; X-ray; 1.90 A; A/B=1-363.
DR PDB; 4BVR; X-ray; 2.58 A; A/B=1-363.
DR PDB; 4BVS; X-ray; 2.60 A; A/B=1-363.
DR PDB; 4BVT; X-ray; 3.10 A; A/B=1-363.
DR PDBsum; 4BVQ; -.
DR PDBsum; 4BVR; -.
DR PDBsum; 4BVS; -.
DR PDBsum; 4BVT; -.
DR AlphaFoldDB; P58329; -.
DR SMR; P58329; -.
DR EnsemblBacteria; KSW21436; KSW21436; AOX63_31675.
DR BioCyc; MetaCyc:MON-13543; -.
DR BRENDA; 3.5.2.15; 5085.
DR UniPathway; UPA00008; UER00502.
DR Proteomes; UP000054734; Plasmid padp1.
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 3D-structure; Hydrolase; Magnesium; Metal-binding; Plasmid.
FT CHAIN 1..363
FT /note="Cyanuric acid amidohydrolase"
FT /id="PRO_0000064761"
FT REGION 1..104
FT /note="RU A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 112..249
FT /note="RU B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 255..363
FT /note="RU C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 162
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 232
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989,
FT ECO:0000269|PubMed:23651355"
FT BINDING 83..84
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989,
FT ECO:0000269|PubMed:23651355"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989,
FT ECO:0000269|PubMed:23651355"
FT BINDING 232..233
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989,
FT ECO:0000269|PubMed:23651355"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989,
FT ECO:0000269|PubMed:23651355"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989,
FT ECO:0000269|PubMed:23651355"
FT BINDING 343..344
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989,
FT ECO:0000269|PubMed:23651355"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989,
FT ECO:0000269|PubMed:23651355"
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 ECO:0000269|PubMed:23651355"
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 ECO:0000269|PubMed:23651355"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989,
FT ECO:0000269|PubMed:23651355"
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 ECO:0000269|PubMed:23651355"
FT SITE 320
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989,
FT ECO:0000305|PubMed:23651355"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 51..67
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 131..148
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 168..176
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 186..204
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4BVQ"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:4BVQ"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:4BVQ"
FT HELIX 319..335
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:4BVQ"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:4BVQ"
SQ 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
