ID   A0A2G5HHX1_CERBT        Unreviewed;       590 AA.
AC   A0A2G5HHX1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=N-acyl-D-glutamate deacylase {ECO:0000313|EMBL:PIA91802.1};
GN   ORFNames=CB0940_09442 {ECO:0000313|EMBL:PIA91802.1};
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA91802.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA91802.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA91802.1,
RC   ECO:0000313|Proteomes:UP000230605};
RA   De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA   Thomma B.P., Van De Peer Y., Bolton M.D.;
RT   "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT   several fungal lineages and shown to be expanded in Cercospora beticola
RT   based on microsynteny with recipient genomes.";
RL   Submitted (OCT-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:PIA91802.1}.
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DR   EMBL; LKMD01000106; PIA91802.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5HHX1; -.
DR   OrthoDB; 1445523at2759; -.
DR   Proteomes; UP000230605; Chromosome 7.
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; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 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;
FT   DOMAIN          72..556
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   590 AA;  64639 MW;  DB34DE4A4372B077 CRC64;
     MEHSSEQDIT FLNATIFDGS GETPRFIASV LVKEGYITAI RDATSSIEPN ELKQMRDAGV
     HIVDCENGRW SLCPGFIDMH AHSDLSLLHT PSHEAKITQG VTTEVIGQDG ISYSPVDDAS
     MARIREQISG WNGNPTDPPD FFNRWKTVGE YLDVLDRERI ATNAAYLVPQ GNLRILVKGW
     DSSPATPDEI AQMQRILAKS LAEGAVGMSS GLTYVPGNFA SDDEIAELCK VVKQYGGYYC
     PHTRSYGKGA LKAYADMIDI GRKTGVRLHL THATLNYAEN AGRADELVTM IDQAISEGVD
     ISLDTYPYLP GSTTLASTLP SWAASADDKL EVLNDPAKLA EIKRLALFEG TDGCHGCTLH
     WDILEIGGVQ KQELASAYVG KTIAQIAEEQ SKDPFDKYVE ILREDNFHST ILSHSGHEGN
     VRKIMRHPRH TGGSDGILTS TKPHPRGWGT FPRYLGHYAR DLPQGKSRNI YHPRSSEVYD
     AVEPETVFQG GLEEAIAHLT SRPAKVVEVS DRGWIKTGFR ADLVLFDAEI IRDAATYAKP
     RQPANGIRAV LVNGRFAVAE GKATGERAGK TIRLRSVQSG EQTASNYVVS
//