ID A0A0T1SRM4_9ACTN Unreviewed; 538 AA.
AC A0A0T1SRM4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=N-acyl-D-amino acid deacylase {ECO:0000313|EMBL:KQX58905.1};
GN ORFNames=ASD33_00915 {ECO:0000313|EMBL:KQX58905.1};
OS Streptomyces sp. Root1304.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736450 {ECO:0000313|EMBL:KQX58905.1, ECO:0000313|Proteomes:UP000051136};
RN [1] {ECO:0000313|Proteomes:UP000051136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1304 {ECO:0000313|Proteomes:UP000051136};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX58905.1, ECO:0000313|Proteomes:UP000051136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1304 {ECO:0000313|EMBL:KQX58905.1,
RC ECO:0000313|Proteomes:UP000051136};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQX58905.1}.
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DR EMBL; LMEP01000001; KQX58905.1; -; Genomic_DNA.
DR RefSeq; WP_056551687.1; NZ_LMEP01000001.1.
DR AlphaFoldDB; A0A0T1SRM4; -.
DR STRING; 1736450.ASD33_00915; -.
DR Proteomes; UP000051136; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000051136}.
FT DOMAIN 49..512
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 518..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 58055 MW; A280ACBEE9B44DED CRC64;
MDLVFRDAEV VDGTGAPSYR ADVAVEGGRI ASIVQEGAAA GCLRPTARRI VDAEGLVLSP
GFIDMHAHSD LALLRDPDHS AKAAQGVTLE VLGQDGLSYA PVDDRTLAEV RRAITGWNGY
GDDIDFDWRT VGEYLDRLDR AHGGRGIAVN AAYLVPQGTV RMYAVGWDDR PATERELARM
RRLVAEGLEQ GAFGMSSGLT YTPGMYAKDA ELTELCRVVA EYGGYYCPHH RSYGAGALEA
YGEMVRLTRE AGCALHLAHA TMNFGVNEGR APELLALLDE ALDAGADISL DTYPYTPGCT
TLVALLPGWA SEGGPEAVLA RLRDEATAER VRHHLEVLGS DGCHGVPVDW DTIEVSGVSA
PGLAEYVGRR VDGWPTARRL LLEDGLGTTI LQHVGHEENV RAIMRHRVHT GGSDGILQGT
KPHPRAYGTF PRYLGRYVRE LGVLSLEECV ARLTGRPAAR LRLPDRGRIR EGYVADLVLF
DPETVAAGST YASPRTPPTG IPHVLVDGRF VIEDGRRTDA LPGKSLRSTR RGGARPQG
//