CYAH_FRAIE
ID CYAH_FRAIE Reviewed; 390 AA.
AC E3JD18;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 47.
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=FraEuI1c_3137;
OS Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298654;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45817 / CECT 9037 / EuI1c;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Beauchemin N., Sen A.,
RA Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT "Complete sequence of Frankia sp. EuI1c.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:5HY0, ECO:0007744|PDB:5HY2, ECO:0007744|PDB:5HY4}
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS), DISULFIDE BONDS, AND FUNCTION.
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: 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:28235873}.
CC -!- SUBUNIT: Homotetramer; disulfide-linked. The disulfide forms between 2
CC monomers in the tetramer, such that each tetramer contains 2 sets of
CC vicinal disulfides. {ECO:0000255|HAMAP-Rule:MF_01989,
CC ECO:0000269|PubMed:28235873}.
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, ECO:0000305|PubMed:28235873}.
CC -!- MISCELLANEOUS: The structural metal found in both cyanuric acid
CC hydrolase and barbiturase is absent in the Frankia CyAH.
CC {ECO:0000305|PubMed:28235873}.
CC -!- SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family.
CC {ECO:0000255|HAMAP-Rule:MF_01989}.
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DR EMBL; CP002299; ADP81157.1; -; Genomic_DNA.
DR PDB; 5HY0; X-ray; 2.40 A; A/B/C/D=1-390.
DR PDB; 5HY2; X-ray; 2.60 A; A/B=1-390.
DR PDB; 5HY4; X-ray; 2.56 A; A/B/C/D/E/F/G/H=1-390.
DR PDBsum; 5HY0; -.
DR PDBsum; 5HY2; -.
DR PDBsum; 5HY4; -.
DR AlphaFoldDB; E3JD18; -.
DR SMR; E3JD18; -.
DR STRING; 298654.FraEuI1c_3137; -.
DR EnsemblBacteria; ADP81157; ADP81157; FraEuI1c_3137.
DR KEGG; fri:FraEuI1c_3137; -.
DR eggNOG; ENOG502Z8BS; Bacteria.
DR HOGENOM; CLU_808206_0_0_11; -.
DR OMA; GRYRIGH; -.
DR Proteomes; UP000002484; 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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hydrolase; Reference proteome.
FT CHAIN 1..390
FT /note="Cyclic amide hydrolase"
FT /id="PRO_0000439911"
FT REGION 1..118
FT /note="RU A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 127..268
FT /note="RU B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 274..390
FT /note="RU C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 177
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 251
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 97..98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 251..252
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 365..366
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT DISULFID 303
FT /note="Interchain (with C-304)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989,
FT ECO:0000269|PubMed:28235873"
FT DISULFID 304
FT /note="Interchain (with C-303)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989,
FT ECO:0000269|PubMed:28235873"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:5HY0"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5HY0"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:5HY0"
FT HELIX 64..81
FT /evidence="ECO:0007829|PDB:5HY0"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:5HY0"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 107..118
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:5HY0"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:5HY0"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:5HY0"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:5HY0"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:5HY0"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:5HY0"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:5HY0"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:5HY4"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:5HY0"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:5HY0"
FT HELIX 307..311
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:5HY0"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:5HY0"
FT HELIX 341..357
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:5HY0"
FT STRAND 379..386
FT /evidence="ECO:0007829|PDB:5HY0"
SQ SEQUENCE 390 AA; 39889 MW; 78011D49AA2CD3E0 CRC64;
MPNPEASLSP RSARYPKASM HVVPMLAPND TAAFRALFAS GAVDPASVVA LIAKSEGSGL
HNDHARVFAD VSLRTALAEA RGCPVEDLAD SVTVAVSGGS PGVISPHVTV VTQEWVADLP
AGLPGVGLVV GRGHTEPILP EDIGRTAQVD KVADAVAAAM LDAGVTDPDD VHLVMVKGPA
LSSRAVADAL SRGKTVVTGD YGIGPMGSMC WSNDASALGV AVALGEVKRD LVADDRIRSD
WDLFSAVAAT SSGGEKRGGE VLLLANSAQS ASELRIGHGI TRDMADTEGI KTAIRTAGVD
FDCCLSPAQQ AQVVQVFGKF VLPGSDVLRG QHITALDDHE AHHVAKAVGG ALVVSITGQP
MSFISGGERN SHMGPPGGNP VAAVVRRLPA
