ID   CYAH_AZOC5              Reviewed;         366 AA.
AC   A8ICF8;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
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};
GN   OrderedLocusNames=AZC_3203;
OS   Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS   6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC   13405 / ORS 571;
RA   Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT   "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT   caulinodans ORS571.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
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: 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:22730121}.
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; AP009384; BAF89201.1; -; Genomic_DNA.
DR   RefSeq; WP_012171727.1; NC_009937.1.
DR   AlphaFoldDB; A8ICF8; -.
DR   SMR; A8ICF8; -.
DR   STRING; 438753.AZC_3203; -.
DR   EnsemblBacteria; BAF89201; BAF89201; AZC_3203.
DR   KEGG; azc:AZC_3203; -.
DR   eggNOG; ENOG502Z8BS; Bacteria.
DR   HOGENOM; CLU_808206_0_0_5; -.
DR   OrthoDB; 984718at2; -.
DR   Proteomes; UP000000270; Chromosome.
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; Reference proteome.
FT   CHAIN           1..366
FT                   /note="Cyclic amide hydrolase"
FT                   /id="PRO_0000439910"
FT   REGION          1..103
FT                   /note="RU A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   REGION          110..247
FT                   /note="RU B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   REGION          253..366
FT                   /note="RU C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   ACT_SITE        160
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   ACT_SITE        230
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         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   BINDING         230..231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT   BINDING         346..347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
SQ   SEQUENCE   366 AA;  37486 MW;  F60462E1161ACE9C CRC64;
     MKVGVHKLAM SAPGDVSELA ALIETGAVNP REIVALVGKT EGNGGANDFT RGLATLSYQL
     LLARHLGLSP EEVGQRIAFV WSGGTEGVLS PHATLFTRAP DDGPMPAEPR LALGIGITRD
     IAPEEVGTTA MVEAVAGAVH TALAEAGITE PADVHYVQVK GPLLTPATIA DADRRGARLV
     TRDPNGSKPY ARGAMALGVA LGLGEVAAER ITPDMIACDM EVFSAVASTS AGGELTKCEV
     LLFGNAPGAT SAFRIGHGVL KDAIDVAGVK EALRSAGLSF HGTPSEEQAH EIVAVFAKAE
     APVNGRLRGR RTTMLSDADI HYERHARAAV GAVIASVTGD PAIFVSGGTE HQCAPGAAPI
     AAIVRA