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Database: UniProt
Entry: U5Q6N3_9BACT
LinkDB: U5Q6N3_9BACT
Original site: U5Q6N3_9BACT 
ID   U5Q6N3_9BACT            Unreviewed;       539 AA.
AC   U5Q6N3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=N-acyl-D-glutamate deacylase {ECO:0000313|EMBL:AGY54252.1};
DE            EC=3.5.1.82 {ECO:0000313|EMBL:AGY54252.1};
GN   ORFNames=BRDCF_p1625 {ECO:0000313|EMBL:AGY54252.1};
OS   Bacteroidales bacterium CF.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1400053 {ECO:0000313|EMBL:AGY54252.1, ECO:0000313|Proteomes:UP000017642};
RN   [1] {ECO:0000313|EMBL:AGY54252.1, ECO:0000313|Proteomes:UP000017642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF {ECO:0000313|EMBL:AGY54252.1};
RX   PubMed=24356833;
RA   Tang S., Edwards E.A.;
RT   "Complete Genome Sequence of Bacteroidales Strain CF from a Chloroform-
RT   Dechlorinating Enrichment Culture.";
RL   Genome Announc. 1:e01066-13(2013).
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DR   EMBL; CP006772; AGY54252.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5Q6N3; -.
DR   STRING; 1400053.BRDCF_p1625; -.
DR   KEGG; bacc:BRDCF_p1625; -.
DR   HOGENOM; CLU_016107_2_1_10; -.
DR   OrthoDB; 9776488at2; -.
DR   Proteomes; UP000017642; Chromosome.
DR   GO; GO:0047421; F:N-acyl-D-glutamate 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   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR   PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR   Pfam; PF07969; Amidohydro_3; 2.
DR   Pfam; PF10518; TAT_signal; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:AGY54252.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017642}.
FT   DOMAIN          78..293
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   DOMAIN          435..522
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   539 AA;  59535 MW;  7E93981A2891809A CRC64;
     MAQTISRRNF LKGSVVAGAT LGLSFYDSKK VGVNNQFDTI ISNGVIYTGD GGKPVRGSVG
     IKEGKIAAIG NIGESADQII DAKGMAVSPG FIDIHSHTDG NIRYAQLGDS KIYQGITTDV
     SGNCGESVFP QSEWKSISDY NEEIERMKIG INIRSYIGQG TLRHIVVGDN DVRATKEDIK
     KMKYLLEEEL EKGAIGVTCG LEYTPGSYAT NAEIVELLKV AAKHDKTFAI HMRNEDDMVE
     EALAETIDMA RKANVRLQVS HLKAQNAANW HKAPKLIKQI EDARNSGMDI AFDRYSYNAF
     STGMSIFIPL KYRQGTTEEI IARMNDEVQA KEIAKYVNTR LEKLGGAKNV MVTSAKTPEN
     RKFIGYNVEE CAKMTNLSNW EFMKKILIEE KLIVDIVGFS MNEDNLKMFL SHPLGMPITD
     CSVYSPVGKL AENMPHPRAY GSFTRFVGKY CRDEKLMDLS AAVRKCTSLP ASRIGLKNRG
     LIQVGYMADL LVFNPDTIID RATYAEPHQY STGIEHILVN GVWTIANGMP TGEFGGRAS
//
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