ID   J8ATZ9_BACCE            Unreviewed;       539 AA.
AC   J8ATZ9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=IEE_01971 {ECO:0000313|EMBL:EJQ46472.1};
OS   Bacillus cereus BAG5X1-1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1053189 {ECO:0000313|EMBL:EJQ46472.1, ECO:0000313|Proteomes:UP000006600};
RN   [1] {ECO:0000313|EMBL:EJQ46472.1, ECO:0000313|Proteomes:UP000006600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAG5X1-1 {ECO:0000313|EMBL:EJQ46472.1,
RC   ECO:0000313|Proteomes:UP000006600};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA   Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA   Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus cereus BAG5X1-1.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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:EJQ46472.1}.
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DR   EMBL; AHDJ01000020; EJQ46472.1; -; Genomic_DNA.
DR   RefSeq; WP_002199782.1; NZ_JH791996.1.
DR   AlphaFoldDB; J8ATZ9; -.
DR   PATRIC; fig|1053189.3.peg.1994; -.
DR   HOGENOM; CLU_009942_2_0_9; -.
DR   Proteomes; UP000006600; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01300; YtcJ_like; 1.
DR   Gene3D; 3.10.310.70; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR033932; YtcJ-like.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR   PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
FT   DOMAIN          50..531
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   539 AA;  59564 MW;  125284B1369AB7FC CRC64;
     MKADVVLING EVITVDKKNT VVEAVAIKDN RIVVVGSNQE VKSFIGEKTD VIDLQGKTLL
     PGFIDSHLHI ISHGLNQLAV SCKAEHIDSI EALLDDLKKK ALETPKGEWI RAWGFNETAV
     KEKRYPTITE LDEISVEHPI IVTRTCHHIS VVNSKALEIA QINENTPNTS GGVIEKNQAG
     RLTGKLIEAA NMRMSEVASY TESEMMKAVK IASDHFVAAG ITSIHDAGGD GPESYRLLQQ
     AVKSRDIRVR IYAMICQINN SHEFVNKMVE AGVVTGTGDE RFKVGPAKLF TDGSSTGPTI
     ATRKSYSSDP TNYGILYYSE EEIYRVLGEA HKKGYQITVH AQGDKAIEMY LNCVERALEK
     SPRKNHRHRI EHAGISSPDL QERMKKLEMI PIPNPPFPYE FGEIYVEHYG ARVNHMYAAR
     DFIDRGIIAA GGSDAPVTDY NPLLGIHVAV NRKTKSGIEV GANQSISVME AIKLYTWNGA
     YASFEEEIKG SIEAGKLADL VILNDSILSV NPNQIKDLKV ETTIIDGEII YQKEQSVKI
//