ID   U2ZXC0_9SPHN            Unreviewed;       581 AA.
AC   U2ZXC0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Putative D-aminoacylase {ECO:0000313|EMBL:GAD50034.1};
GN   ORFNames=NT2_07_00340 {ECO:0000313|EMBL:GAD50034.1};
OS   Caenibius tardaugens NBRC 16725.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Caenibius.
OX   NCBI_TaxID=1219035 {ECO:0000313|EMBL:GAD50034.1, ECO:0000313|Proteomes:UP000016568};
RN   [1] {ECO:0000313|EMBL:GAD50034.1, ECO:0000313|Proteomes:UP000016568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 16725 {ECO:0000313|EMBL:GAD50034.1,
RC   ECO:0000313|Proteomes:UP000016568};
RA   Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Novosphingobium tardaugens NBRC 16725.";
RL   Submitted (SEP-2013) 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:GAD50034.1}.
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DR   EMBL; BASZ01000007; GAD50034.1; -; Genomic_DNA.
DR   RefSeq; WP_021690852.1; NZ_CP034179.1.
DR   AlphaFoldDB; U2ZXC0; -.
DR   KEGG; ntd:EGO55_06600; -.
DR   eggNOG; COG3653; Bacteria.
DR   OrthoDB; 9766983at2; -.
DR   Proteomes; UP000016568; Unassembled WGS sequence.
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; 2.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2.
DR   InterPro; IPR013108; Amidohydro_3.
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; 2.
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:UP000016568}.
FT   DOMAIN          48..269
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   DOMAIN          430..552
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   581 AA;  64784 MW;  B7C890861E99D16B CRC64;
     MSDLLIKGGT VVDGTGAAAY KADVRVKDGI IAEIGEDLRP DGEKVYFADD CYVTPGFVES
     HTHYDATMWW QNDLDPLPGY GVTSIIMGNC GFSAAPISRE EAARNEMVKI FAFFEDIPEG
     PFLQNLPWDW EKWSEYKTSM IKHVRVPANY AAFVGHLALR LAVLGLEAWD RAATPAEIAK
     MAELLDDALA AGALGMSDNL FDHDGSDRPV PTLLADDAEF EALFDVLERY EGVSYQVILD
     IFTRKTAPQM LERVARLTKG RKLRIQTAGT IATLDFQKDL AGPLENRMIE MQAEGYDIWP
     TASHVAPTNV LSIVKSLIFA QSNDYVWHEV VMADDHEEKR RLLADPEWRA RARESWDTKA
     WQWAPMNNPQ RLELINSDNG VGPVNITLAE FAESRGLHRS DAMAQWILEN GILSTVHMSP
     FPKDEEMTTR WMTNPMSVGN VTDAGAHGQM LCGGGENVEL ITKYVMQDKR ISLEQAVHIL
     TGKLMNFFGL TDRGELKVGK RADITVFKLD EIKRRDMIKA FDVPDGKGGH TWRFTREPAP
     MRLTIVNGVV TFDGKKFTGE MPGQFLSPVA NDQLAQVAAA E
//