CAH_RHIL3
ID CAH_RHIL3 Reviewed; 351 AA.
AC Q1M7F3;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=pRL100353;
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OG Plasmid pRL10.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
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=130 uM for cyanuric acid {ECO:0000269|PubMed:22730121};
CC Note=kcat is 5 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; AM236084; CAK10579.1; -; Genomic_DNA.
DR RefSeq; WP_011654380.1; NC_008381.1.
DR AlphaFoldDB; Q1M7F3; -.
DR SMR; Q1M7F3; -.
DR EnsemblBacteria; CAK10579; CAK10579; pRL100353.
DR KEGG; rle:pRL100353; -.
DR HOGENOM; CLU_808206_0_0_5; -.
DR OMA; GRYRIGH; -.
DR OrthoDB; 984718at2; -.
DR BioCyc; MetaCyc:MON-20659; -.
DR UniPathway; UPA00008; UER00502.
DR Proteomes; UP000006575; Plasmid pRL10.
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; Plasmid.
FT CHAIN 1..351
FT /note="Cyanuric acid amidohydrolase"
FT /id="PRO_0000439918"
FT REGION 1..96
FT /note="RU A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 103..240
FT /note="RU B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 246..351
FT /note="RU C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 153
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 223
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 77..78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 223..224
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 329..330
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT SITE 306
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
SQ SEQUENCE 351 AA; 36854 MW; AA90284C62B6EC42 CRC64;
MPSLRAHVFR VPADGPDDVA GVEALFASGL QANNIVAVLG KTEGNGCVND FTRGYATRSF
ETLFSRYGVD GVSIIMSGGT EGALSPHWTV FARETVETPG ERALAIGVSR TPALSPEHLG
RREQILLVAE GVKSAMRDAG IDDPADAHFV QIKCPLLTSR RIAEAEAAGR TVATHDTLKS
MGLSRGASAL GVAVALGEID ATSINDADIC TRFDLFSRCA STSSGVELTD HEIIVLGMSA
KWSGPLSIDH AVMRDAIDAH SVRKARERLP ENSRLAAVLA KAEPDPSGEI DGRRHTMLDD
SDIAGTRHAR AFVGGVLAGI FGITDLYVSG GAEHQGPPGG GPVAIIVEKE Q
