ID   CYAH_RHOSO              Reviewed;         349 AA.
AC   H8ZKS8;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Cyclic amide hydrolase {ECO:0000255|HAMAP-Rule:MF_01989};
DE            Short=CyAH {ECO:0000255|HAMAP-Rule:MF_01989};
DE            EC=3.5.2.- {ECO:0000255|HAMAP-Rule:MF_01989};
DE   AltName: Full=Ring-opening amidohydrolase {ECO:0000255|HAMAP-Rule:MF_01989};
OS   Rhodococcus sp.
OG   Plasmid pMel2.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=Mel;
RX   PubMed=22210223; DOI=10.1128/aem.06468-11;
RA   Dodge A.G., Wackett L.P., Sadowsky M.J.;
RT   "Plasmid localization and organization of melamine degradation genes in
RT   Rhodococcus sp. strain Mel.";
RL   Appl. Environ. Microbiol. 78:1397-1403(2012).
CC   -!- FUNCTION: Cyclic amide hydrolase of unknown substrate specificity.
CC       Catalyzes the hydrolytic ring-opening of a cyclic amide. Does not act
CC       on cyanuric acid nor barbituric acid. {ECO:0000255|HAMAP-Rule:MF_01989,
CC       ECO:0000269|PubMed:22210223}.
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 and the
CC       active site possess nearly threefold rotational symmetry, to the extent
CC       that the active site possesses three potential Ser-Lys catalytic dyads,
CC       but one of the 3 active site surfaces varies in composition suggesting
CC       it is involved in confering substrate specificity. {ECO:0000255|HAMAP-
CC       Rule:MF_01989}.
CC   -!- SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family.
CC       {ECO:0000255|HAMAP-Rule:MF_01989}.
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DR   EMBL; JN241636; AEX65050.1; -; Genomic_DNA.
DR   AlphaFoldDB; H8ZKS8; -.
DR   SMR; H8ZKS8; -.
DR   GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; 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   3: Inferred from homology;
KW   Hydrolase; Plasmid.
FT   CHAIN           1..349
FT                   /note="Cyclic amide hydrolase"
FT                   /id="PRO_0000439921"
FT   REGION          1..90
FT                   /note="RU A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   REGION          99..231
FT                   /note="RU B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   REGION          237..349
FT                   /note="RU C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   ACT_SITE        214
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   BINDING         214..215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   BINDING         330..331
FT                   /ligand="substrate"
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   349 AA;  35242 MW;  83A4563410EA2CA7 CRC64;
     MTSPEDTAGV EAALAAEGFS PTDVRAVMCM TESDGFGRGY ASLAFAHAFA PALGCPPEDV
     AQQIPMIMIG GCSGLVTPYA AVFVDDPASS WVTDGSGGGL SIGVTTTATL NPLDVGTPAM
     VDAVADAVRS AMAAAGIDKV ADVHNVQIKT PWPSSAALLD GPLSGLDAGS VGAMARAAGA
     LGVAVALGEV SRADITADVF LRDPNLRSDV ASVSAGTERV DAAVLVMGNS PTSASPYRIG
     HGVLRDGIDP HGVLDALRAV GIDSGWPFTA DTTPVEHVFL KSAVDGTDEC RGRRHVLRTD
     YLGPYSWLLG KAVVHATVAS IVGDPMMQVS GGGEHQGPPG GGTVAVIAR