CAH_MOOTA
ID CAH_MOOTA Reviewed; 367 AA.
AC Q2RGM7;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
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:19767460, ECO:0000269|PubMed:28235873};
GN OrderedLocusNames=Moth_2120;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
RN [2]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19767460; DOI=10.1128/aem.01605-09;
RA Li Q., Seffernick J.L., Sadowsky M.J., Wackett L.P.;
RT "Thermostable cyanuric acid hydrolase from Moorella thermoacetica ATCC
RT 39073.";
RL Appl. Environ. Microbiol. 75:6986-6991(2009).
RN [3]
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:19767460,
CC 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:19767460, 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 KM=110 uM for cyanuric acid {ECO:0000269|PubMed:19767460};
CC KM=159 uM for cyanuric acid {ECO:0000269|PubMed:28235873};
CC Note=kcat is 10.6 sec(-1) with cyanuric acid as substrate
CC (PubMed:19767460). kcat is 5.2 sec(-1) with cyanuric acid as
CC substrate (PubMed:28235873). {ECO:0000269|PubMed:19767460,
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; CP000232; ABC20412.1; -; Genomic_DNA.
DR RefSeq; WP_011393610.1; NC_007644.1.
DR RefSeq; YP_430955.1; NC_007644.1.
DR PDB; 6BUM; X-ray; 1.51 A; A/B/C/D=1-367.
DR PDB; 6BUN; X-ray; 1.78 A; A/B/C/D=1-367.
DR PDB; 6BUO; X-ray; 1.85 A; A/B/C/D=1-367.
DR PDB; 6BUP; X-ray; 1.88 A; A/B/C/D=1-367.
DR PDB; 6BUQ; X-ray; 1.88 A; A/B/C/D=1-367.
DR PDB; 6BUR; X-ray; 2.18 A; A/B/C/D=1-367.
DR PDB; 6CWJ; X-ray; 2.25 A; A/B/C/D=1-367.
DR PDB; 6DHJ; X-ray; 3.20 A; A/B/C/D/E/F/G/H=1-367.
DR PDBsum; 6BUM; -.
DR PDBsum; 6BUN; -.
DR PDBsum; 6BUO; -.
DR PDBsum; 6BUP; -.
DR PDBsum; 6BUQ; -.
DR PDBsum; 6BUR; -.
DR PDBsum; 6CWJ; -.
DR PDBsum; 6DHJ; -.
DR AlphaFoldDB; Q2RGM7; -.
DR SMR; Q2RGM7; -.
DR STRING; 264732.Moth_2120; -.
DR EnsemblBacteria; ABC20412; ABC20412; Moth_2120.
DR KEGG; mta:Moth_2120; -.
DR PATRIC; fig|264732.11.peg.2305; -.
DR eggNOG; ENOG502Z8BS; Bacteria.
DR HOGENOM; CLU_808206_0_0_9; -.
DR OMA; GRYRIGH; -.
DR BRENDA; 3.5.2.15; 1528.
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.
FT CHAIN 1..367
FT /note="Cyanuric acid amidohydrolase"
FT /id="PRO_0000439915"
FT REGION 1..104
FT /note="RU A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 111..248
FT /note="RU B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 254..367
FT /note="RU C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 161
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 231
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 BINDING 83..84
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 231..232
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 347..348
FT /ligand="substrate"
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 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 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 358
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT SITE 324
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 51..67
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 130..146
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 185..203
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6BUM"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 253..263
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6BUM"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6BUM"
FT HELIX 323..339
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:6BUM"
FT STRAND 359..366
FT /evidence="ECO:0007829|PDB:6BUM"
SQ SEQUENCE 367 AA; 38900 MW; 6F0272BFDC00B579 CRC64;
MQKVEVFRIP TASPDDISGL ATLIDSGKIN PAEIVAILGK TEGNGCVNDF TRGFATQSLA
MYLAEKLGIS REEVVKKVAF IMSGGTEGVM TPHITVFVRK DVQEPAKPGK RLAVGVAFTR
DFLPEELGRM EQVNEVARAV KEAMKDAQID DPRDVHFVQI KCPLLTAERI EDAKRRGKDV
VVNDTYKSMA YSRGASALGV ALALGEISAD KISNEAICHD WNLYSSVAST SAGVELLNDE
IIVVGNSTNS ASDLVIGHSV MKDAIDADAV RAALKDAGLK FDCCPPAEEL AKIVNVLAKA
EAASSGTVRG RRNTMLDDSD INHTRSARAV VNAVIASVVG DPMVYVSGGA EHQGPDGGGP
IAVIARV
