CAH_ENTCL
ID CAH_ENTCL Reviewed; 370 AA.
AC P0A3V4; O87589;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 44.
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};
GN Name=trzD;
OS Enterobacter cloacae.
OG Plasmid pPDL12.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=550;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=99;
RX PubMed=1991731; DOI=10.1128/jb.173.3.1363-1366.1991;
RA Eaton R.W., Karns J.S.;
RT "Cloning and comparison of the DNA encoding ammelide aminohydrolase and
RT cyanuric acid amidohydrolase from three s-triazine-degrading bacterial
RT strains.";
RL J. Bacteriol. 173:1363-1366(1991).
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}.
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 -!- ACTIVITY REGULATION: Inhibited by barbituric acid. {ECO:0000255|HAMAP-
CC Rule:MF_01989}.
CC -!- PATHWAY: Xenobiotic degradation; atrazine degradation; biuret from
CC cyanurate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01989}.
CC -!- SUBUNIT: Homotetramer. {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; AF342826; AAK11688.1; -; Genomic_DNA.
DR PDB; 5T13; X-ray; 2.19 A; A=1-370.
DR PDBsum; 5T13; -.
DR AlphaFoldDB; P0A3V4; -.
DR SMR; P0A3V4; -.
DR BRENDA; 3.5.2.15; 155.
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 3D-structure; Hydrolase; Magnesium; Metal-binding; Plasmid.
FT CHAIN 1..370
FT /note="Cyanuric acid amidohydrolase"
FT /id="PRO_0000065648"
FT REGION 1..103
FT /note="RU A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 113..250
FT /note="RU B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 256..370
FT /note="RU C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 163
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 233
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 233..234
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 349..350
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 356
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 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT SITE 326
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT STRAND 1..9
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 50..66
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 92..106
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 132..148
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 187..205
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:5T13"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 252..265
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 269..278
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:5T13"
FT HELIX 325..341
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:5T13"
FT STRAND 361..368
FT /evidence="ECO:0007829|PDB:5T13"
SQ SEQUENCE 370 AA; 39420 MW; E02B447694802035 CRC64;
MQAQVFRVPM SNPADVSGVA KLIDEGVIRA EEVVCVLGKT EGNGCVNDFT RGYTTLAFKV
YFSEKLGVSR QEVGERIAFI MSGGTEGVMA PHCTIFTVQK TDNKQKTAAE GKRLAVQQIF
TREFLPEEIG RMPQVTETAD AVRRAMREAG IADASDVHFV QVKCPLLTAG RMHDAVERGH
TVATEDTYES MGYSRGASAL GIALALGEVE KANLSDEVIT ADYSLYSSVA STSAGIELMN
NEIIVMGNSR AWGGDLVIGH AEMKDAIDGA AVRQALRDVG CCENDLPTVD ELGRVVNVFA
KAEASPDGEV RNRRHTMLDD SDINSTRHAR AVVNAVIASI VGDPMVYVSG GSEHQGPAGG
GPVAVIARTA
