ID   A0A1A3HI32_9MYCO        Unreviewed;       534 AA.
AC   A0A1A3HI32;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:OBJ47882.1};
GN   ORFNames=A9W95_05810 {ECO:0000313|EMBL:OBJ47882.1};
OS   Mycobacterium sp. 1423905.2.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1856859 {ECO:0000313|EMBL:OBJ47882.1, ECO:0000313|Proteomes:UP000092291};
RN   [1] {ECO:0000313|Proteomes:UP000092291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1423905.2 {ECO:0000313|Proteomes:UP000092291};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Garcia-Basteiro A.,
RA   Lopez-Varela E., Palencia S.;
RL   Submitted (JUN-2016) 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:OBJ47882.1}.
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DR   EMBL; LZLE01000350; OBJ47882.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A3HI32; -.
DR   Proteomes; UP000092291; 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   Hydrolase {ECO:0000313|EMBL:OBJ47882.1}.
FT   DOMAIN          51..533
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          498..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  55663 MW;  94050F15CBE413CE CRC64;
     MTATSTKLLV NGRVYSPTHP DATAMAVRGD TIAWLGSDDV GRHQFPGADL EDLAGAFVAP
     GFVDSHIHLS ATGLMLSGLD LRPATSQAHC LQLVADYAAA HPGQPLWGHG WDESAWPEHS
     PPSTADLDAV LGDRPAYLAR VDVHSALAST ALRRLTPELP MATGFGADHP LTGEAHHLVR
     AAARNLLTDT QLAQARIAAL RALAAAGIVA VHECAGPEIG GLDDWFALRG VDHGVEIIGY
     WGEAVTTAAQ ARALIAETGA RGLAGDLFID GALGSRTAWL HEPYADAPGC VGTRHLEPDA
     VEAHVRACTE ADVTAGFHVI GDAAVSAVVA AFERVVTDLG VVAVAGRGHR LEHVEMVTAD
     QAAKLGAWGI IASVQPNFDA LWGGDDGMYA ERLGPDRGQR LNPLALLASQ GVPLALGSDA
     PVTGFEPWAS VRAAVQHRTP GSGLSARAAF AAATRGGWRA CGVRDGHAGT LVPGAPASYA
     IWEADAFDVS APPDAVQRWS TDPRSRVPAL PRLGPTDSLP RCRRTVHRGS VIYG
//