ID   E5WJG0_9BACI            Unreviewed;       531 AA.
AC   E5WJG0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=HMPREF1013_02592 {ECO:0000313|EMBL:EFV77220.1};
OS   Bacillus sp. 2_A_57_CT2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV77220.1, ECO:0000313|Proteomes:UP000003283};
RN   [1] {ECO:0000313|EMBL:EFV77220.1, ECO:0000313|Proteomes:UP000003283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV77220.1,
RC   ECO:0000313|Proteomes:UP000003283};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2.";
RL   Submitted (DEC-2010) 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:EFV77220.1}.
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DR   EMBL; ACWD01000035; EFV77220.1; -; Genomic_DNA.
DR   RefSeq; WP_009333296.1; NZ_GL635752.1.
DR   AlphaFoldDB; E5WJG0; -.
DR   eggNOG; COG1574; Bacteria.
DR   HOGENOM; CLU_009942_3_1_9; -.
DR   Proteomes; UP000003283; 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:SF23; AMIDOHYDROLASE YTCJ-RELATED; 1.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000003283}.
FT   DOMAIN          50..529
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   531 AA;  58785 MW;  1C60BE5627F37BB8 CRC64;
     MGTLWHGGSI YTLQQEGHQI EAVFTEGSQI IEIGALRDLK SKYKEEIQNE IDLQGSTMLP
     GFVDSHMHLI GHGERLIRLD LSKHTSKHEV LMAVKEFSET IEEGEWVIGE GWNENLWDQP
     EPIYASELDQ FVPKHPVMLK RVCRHALAVN SLGLEKANIT ADTECPPGGV IDKDESGKLN
     GLLKDQAQEL LFNVMPAVSE SYLKKALHAA IKDAYRLGLT GGHTEDLNYY GGFSQTYQAF
     KQVIEADGLS FRAHLLVHHG VADEMKESGG GYLEGSNHIE FGAMKIFADG ALGGRTALLS
     HPYADDPSTS GVAIYSQEQL DELVEKARKH ELPVAVHTIG DLAFEMALNA IEKHPLEGLG
     RDRLIHAQIL RKELIDRAKK LPLIIDIQPR FTASDFPWVI DRIGEEHMEY CYAWKTLLKE
     GIHCAGGSDA PIEPANPFLG IHAAVTRTNI DDPHNTVYYP SEALTVYEAV SLFTKGSAYA
     ASHENDRGII KEGYLADFTI LNEDIFKMPI GQIAAISVNK TVIDGIIVYE A
//