ID A0QRP1_MYCS2 Unreviewed; 531 AA.
AC A0QRP1;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=N-acyl-D-aspartate deacylase {ECO:0000313|EMBL:ABK72900.1};
DE EC=3.5.1.83 {ECO:0000313|EMBL:ABK72900.1};
GN OrderedLocusNames=MSMEG_1187 {ECO:0000313|EMBL:ABK72900.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK72900.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK72900.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000480; ABK72900.1; -; Genomic_DNA.
DR RefSeq; WP_011727481.1; NZ_SIJM01000011.1.
DR RefSeq; YP_885579.1; NC_008596.1.
DR AlphaFoldDB; A0QRP1; -.
DR STRING; 246196.MSMEG_1187; -.
DR PaxDb; 246196-MSMEI_1155; -.
DR GeneID; 66732650; -.
DR KEGG; msm:MSMEG_1187; -.
DR PATRIC; fig|246196.19.peg.1181; -.
DR eggNOG; COG3653; Bacteria.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000000757; Chromosome.
DR GO; GO:0047422; F:N-acyl-D-aspartate deacylase activity; IEA:UniProtKB-EC.
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; 1.
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.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABK72900.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757}.
FT DOMAIN 50..509
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 531 AA; 56672 MW; 6F7715A720200A0C CRC64;
MNHAITHDIV ITGGRVIDGT GRPAERADLA VTGDVITAIG MGPYQATTRI DATDRVVAPG
FIDLHSHADF TVAGHPTAET AIAQGVTTLI TGNCGQSTFP VRDQEEARLS TAFRDFPLSW
EWTDAAGFGE TVMAAGPAVN VGLQVGHNAL RVAVMGQQDR APDTRELREM CSLIEESAQH
PGVVGFSTGL IYIPGLFAFT DELVALVSAA ASCDLLYSTH MRSETSELVE AVEEAIGTAE
RSGARLEISH LKAMGPENWG AVDKALELID AARARGVDVA ADVYPYTASS TDLSSRVPRW
AIDGGRPALL DRLADPVQRA RIAEEMRARF GRDIDPEGVV IADLPPGEFD SYVGWSIARI
GRDRGVDAAE VALDVLAAHA GSVTIVNHAM SEDDVRTVLA HPWVSVASDG WMLAPSGPGR
PHPRSFGTFP RVLGRYVREQ PTISLEEAIR KMTTLPASRI GITDRGSLTV GAAADIVVLD
PHSIADTSTF DDPWQLARGV HTVLVNGTPT LLDGEFTKNH AGRLLQKRKP A
//
