ID   B0SN39_LEPBP            Unreviewed;       582 AA.
AC   B0SN39;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=N-acyl-D-glutamate amidohydrolase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=LEPBI_I1107 {ECO:0000313|EMBL:ABZ97226.1};
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ97226.1, ECO:0000313|Proteomes:UP000001847};
RN   [1] {ECO:0000313|EMBL:ABZ97226.1, ECO:0000313|Proteomes:UP000001847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris
RC   {ECO:0000313|Proteomes:UP000001847};
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
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DR   EMBL; CP000786; ABZ97226.1; -; Genomic_DNA.
DR   RefSeq; WP_012388108.1; NC_010602.1.
DR   AlphaFoldDB; B0SN39; -.
DR   STRING; 456481.LEPBI_I1107; -.
DR   KEGG; lbi:LEPBI_I1107; -.
DR   HOGENOM; CLU_016107_1_0_12; -.
DR   OrthoDB; 9775607at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS05425-MONOMER; -.
DR   Proteomes; UP000001847; Chromosome I.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
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   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:UP000001847}.
SQ   SEQUENCE   582 AA;  65863 MW;  BE48FB0370FCD1AB CRC64;
     MAETLIKQAR IFDGSTNPSF IGDVRIKNGI VDTISKTELI PNPGETVIDA KGQWLTPGFI
     DFHTHYDAEI EVAPDLSESV RHGVTTISLG SCSLSLALGD PTDLADMFSR VEAIPRKNVL
     SILESKKNWN SAVDYKKHLN SLPLGPNVTS FAGHSAIRAH VMGLERSLTK GEKPTKQELN
     QMNQHLEEAL DAGFMGLSIN TLVWDKMDGS RFRSRPLPST FANWSEYQFL NRTLRKRGKI
     FQGVPNVSTK INVLMFLKEA FGIFRKPLKT TIISLMDVKF DPGLYKLLGV IGRITNTIFR
     SDFRFQALPE PFDLYADGMD VVVFEEFAAG AKANHIEDEL ERKQLMKDPK YRSWFKRQWT
     NWFLPRVFHR NFRETKIVDA PDKSLIGKSI DEVAKERGVH SVTAFLDLVA EHGNDVRWYT
     VMANHRKEPL QKIVSYPDIL IGFSDAGAHL RGMAHYNFPL RMLKLVRDAE LENKPFMTME
     KAVHRLTGEI GDWFGIDAGY IKEGKRADLV LIDPNKLDES LAKDVEAPMP FMEDFKRWVR
     RNDDTIKKVF INGKLAVDGG KPVSNLGKES GYGRFLESQI GV
//