ID A0A260BEB9_9NOCA Unreviewed; 537 AA.
AC A0A260BEB9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:OZD02341.1};
GN ORFNames=CH275_16985 {ECO:0000313|EMBL:OZD02341.1};
OS Rhodococcus sp. 06-235-1A.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2022508 {ECO:0000313|EMBL:OZD02341.1, ECO:0000313|Proteomes:UP000215839};
RN [1] {ECO:0000313|EMBL:OZD02341.1, ECO:0000313|Proteomes:UP000215839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=06-235-1A {ECO:0000313|EMBL:OZD02341.1,
RC ECO:0000313|Proteomes:UP000215839};
RA Savory E.A., Fuller S.L., Weisberg A.J., Thomas W.J., Gordon M.I.,
RA Stevens D.M., Creason A.L., Belcher M.S., Wiseman M., Putnam M.L.,
RA Grunwald N.J., Chang J.H.;
RT "Evolutionary transitions between beneficial and phytopathogenic
RT Rhodococcus challenge disease management.";
RL Submitted (JUL-2017) 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:OZD02341.1}.
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DR EMBL; NOYI01000018; OZD02341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A260BEB9; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000215839; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01297; D-aminoacylase; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
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 47..510
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 537 AA; 58361 MW; 1870C700CA18CFEE CRC64;
MPSTLFRGAD VIDGTGSPRL RRDVLVRDGI IASIGEPGTV PGADRIVDAS PGQILSPGFI
DMHAHSDLRL LTDPDHFPKI SQGVTTEVIG QDGIAYAPID DATLDVVRRQ IAGWNGNPVD
LDFSWRSVSE YLARLDQGIT PNAAYLVPQG TLRYLAVGAD QRPATPSEIV HMQELLAQGL
REGAVGMSSG LTYTPGMYAD TSELRALCEV VAEFGGFYAP HTRSYGAGAL DAYQEMLDLS
RDTGCALHLT HATMNFGVNR GRAREFLDRV DSAIADGCDV TLDTYPYLPG ATTLSALLPS
WAMSGGPDRA LERLDDPEMR RRITQDVDVD GSDGCHGVTV EWDTIQLSGV ANPELDRYVG
RTMSDIAADE GRSPVNVFFD FLRRDALATT ILQHVGHEEN VRAIMAHPHH MGGSDAILVG
EKPHPRAWGT FPRYLGHYVR DEQLLTLEDC INHLTGRPAA RLRLHGRGTI AEGHAADLVL
FDPATVRDTA TFEHPKQQAE GISHVMVNGA FAIDDHRSTH SLAGHALRMD STRKQTS
//