ID   A0A0W7WAI6_9MICO        Unreviewed;       457 AA.
AC   A0A0W7WAI6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Cyclic amidohydrolase {ECO:0000313|EMBL:KUF07667.1};
GN   ORFNames=AUL38_07395 {ECO:0000313|EMBL:KUF07667.1};
OS   Leucobacter sp. G161.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF07667.1, ECO:0000313|Proteomes:UP000053012};
RN   [1] {ECO:0000313|EMBL:KUF07667.1, ECO:0000313|Proteomes:UP000053012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G161 {ECO:0000313|EMBL:KUF07667.1,
RC   ECO:0000313|Proteomes:UP000053012};
RA   Ge S., Dong X.;
RT   "High quality draft genome sequence of Leucobacter sp. G161, a distinct and
RT   effective chromium reducer.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUF07667.1}.
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DR   EMBL; LOHP01000047; KUF07667.1; -; Genomic_DNA.
DR   RefSeq; WP_059059743.1; NZ_LOHP01000047.1.
DR   AlphaFoldDB; A0A0W7WAI6; -.
DR   STRING; 663704.AUL38_07395; -.
DR   Proteomes; UP000053012; Unassembled WGS sequence.
DR   GO; GO:0004038; F:allantoinase activity; IEA:InterPro.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000256; P:allantoin catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR017593; Allantoinase.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR03178; allantoinase; 1.
DR   PANTHER; PTHR43668; ALLANTOINASE; 1.
DR   PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KUF07667.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053012}.
FT   DOMAIN          64..440
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   457 AA;  49223 MW;  0E31A68EF5B08389 CRC64;
     MTNATDTQPQ HDAFDLVIRG ERVVTTSGIR PREVGVRNGR IIALEPLGNG LVGKETIDLG
     DDETLIPGLV DTHVHVNEPG RTEWEGFDSA TRAAAAGGVT TIVDMPLNSI PPTVNVAGLQ
     AKREVAAPQS HVDVGFWGGA IPGSIGDLRG LHDAGVFGFK CFLLHSGVDE FPPLDADEME
     AVMRELLTYD AMLIVHAEDS RAIDRAPSPE GDVYDRFLHS RPRGAENLAI SEVIERARWT
     GARAHILHLS SSDALPMIRS AKRDGVRLTV ETCPHYLALT AEEIPAGGTA YKCCPPIREA
     HNRELLWEGL LDGTIDYIAS DHSPSTPELK DPENGDFAVA WGGVSSLQLE LPVIWTEARH
     RGVSLEQVIS WMSTKPAANV GLTGKGMIAP GNDADFVIFA ADDAFVVDPA KLHHKNPITP
     YAGRALSGVV RSTYLRGRLV TGNDPHGELI RRGMLGS
//