ID   A0A1X2CJR6_9MYCO        Unreviewed;       574 AA.
AC   A0A1X2CJR6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Aminoacylase {ECO:0000313|EMBL:ORW76150.1};
GN   ORFNames=AWC22_21750 {ECO:0000313|EMBL:ORW76150.1};
OS   Mycobacterium riyadhense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=486698 {ECO:0000313|EMBL:ORW76150.1, ECO:0000313|Proteomes:UP000193087};
RN   [1] {ECO:0000313|EMBL:ORW76150.1, ECO:0000313|Proteomes:UP000193087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45176 {ECO:0000313|EMBL:ORW76150.1,
RC   ECO:0000313|Proteomes:UP000193087};
RA   Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA   Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA   Olivier J., Enrico T., Nicola S.;
RT   "The new phylogeny of the genus Mycobacterium.";
RL   Submitted (JAN-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:ORW76150.1}.
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DR   EMBL; LQPQ01000103; ORW76150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2CJR6; -.
DR   STRING; 486698.AWC22_21750; -.
DR   OrthoDB; 9766983at2; -.
DR   Proteomes; UP000193087; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
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   PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 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          43..545
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          189..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  60517 MW;  DFBE4E0DB383F444 CRC64;
     MLDLLIRDAD IVDGTGAPAR RGDVGVSAGR IVAVGHVDDP ATQTVDAHGL TLAPGFVDLH
     THYDAQLFWD PTASPSLQHG VTTVFGGNCG FTLAPAVDQQ DYLTRMLARV EGMPLNALRA
     GLDWQWSSFG DWLNRFEGRI AVNAGFLVGH SAVRLAAMGS DAVGGEATPE QIERMLAVLH
     EALDAGALGL STSQSPTHND GAGQPVPSRS ASREELVALA AAVGDHPGTT LEAIIPGCLA
     GFTDDEVALL TDLSLAADRP LNWNLLGVSA ANPAGHQRQL RASEVAAQRG ARVVALTLPH
     AMKIRLSFLS GFVLDGLPGW RDTMHLPVPE RLKALADPEV RRRLTEGAAS KEAGMLRGLA
     QWERLSVVET FAPENADAAG RTVGDVAAAR GGEPFDTLLD IVIADELRTG LSPPLAGDEA
     ADWRLRADVW HHPHAVIGGS DAGAHLDMMC GAIYTTSLLG RGVRKHKVVT LEEAVRLITD
     VPARLYGLTD RGRIAPGWHA DLVLFDPATV DHGPERTRYD LPAGAPRLVA DAHGITCVWV
     GGVEVCRDGV ATGATPGTVL RSGRDTQTIR AGAP
//