ID A0A1I5S898_9BACT Unreviewed; 567 AA.
AC A0A1I5S898;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:SFP66923.1};
GN ORFNames=SAMN05444277_101634 {ECO:0000313|EMBL:SFP66923.1};
OS Parafilimonas terrae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Parafilimonas.
OX NCBI_TaxID=1465490 {ECO:0000313|EMBL:SFP66923.1, ECO:0000313|Proteomes:UP000199031};
RN [1] {ECO:0000313|EMBL:SFP66923.1, ECO:0000313|Proteomes:UP000199031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28286 {ECO:0000313|EMBL:SFP66923.1,
RC ECO:0000313|Proteomes:UP000199031};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOXQ01000001; SFP66923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5S898; -.
DR STRING; 1465490.SAMN05444277_101634; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000199031; Unassembled WGS sequence.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR CDD; cd01297; D-aminoacylase; 1.
DR Gene3D; 3.30.1490.130; D-aminoacylase. Domain 3; 1.
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; IPR023100; D-aminoacylase_insert_dom_sf.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000199031};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..567
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011447885"
FT DOMAIN 76..545
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 567 AA; 62098 MW; 8D35CABBFD8D7070 CRC64;
MNKIIKVPEL IQQTCIAFFL CLALAACNNK TSYETIIRNG IVYDGNGGEP YKADIALYAD
TIAFIGDLKN ASAKNEIDAN GKAIAPGFIN MLSWATESLI QDGRSQSDIR QGVTLEVMGE
GSSMGPLNAT MKKQMQEGQS DIKYKVEWNT LGEYLNYLEK KGISCNVASF IGAGTVRTYI
VGEDNRAATP VELDSMRMLV DHAMQEGAMG VGSSLIYPPD FFASTDELIA LCKEASKYGG
MYISHMRSEG NKLNEAVNEL ITIAREANIP AEIYHLKAAG KNNWPKMDSV IKQVEAARAS
GLKITADMYT YLAGATGMTA AFPPSLQDGG FGKLWQRLHD PAIRKQMAKA MNTDAKDWEN
LYYGAGSADN VLLLGFKQDS LKKYTGKTLA EVAALRGKTP EETAMDLIVE DSTRIGVAYF
LMSEDNVKKQ MTLPWVSFGS DEGSYTNEGV FLESNAHPRA YGNFVRVLGK YARDEKVLSL
QQAVYQLAKL PATNLKLKKR GELKVGNYAD VVVFDPATVT DHATYEKPHQ YATGVTDVWV
NGVQVLKDNE HTGATPGRFI KGPGYKQ
//
