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Database: UniProt
Entry: A0A292YTQ0_9PSEU
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Original site: A0A292YTQ0_9PSEU 
ID   A0A292YTQ0_9PSEU        Unreviewed;       468 AA.
AC   A0A292YTQ0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:GAY07529.1};
DE            EC=3.5.2.2 {ECO:0000313|EMBL:GAY07529.1};
GN   ORFNames=TOK_3549 {ECO:0000313|EMBL:GAY07529.1};
OS   Pseudonocardia sp. N23.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1987376 {ECO:0000313|EMBL:GAY07529.1, ECO:0000313|Proteomes:UP000222857};
RN   [1] {ECO:0000313|EMBL:GAY07529.1, ECO:0000313|Proteomes:UP000222857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N23 {ECO:0000313|EMBL:GAY07529.1,
RC   ECO:0000313|Proteomes:UP000222857};
RA   Yamamoto N., Saito Y., Inoue D., Sei K., Ike M.;
RT   "Characterization of newly isolated Pseudonocardia sp. N23 with high 1,4-
RT   dioxane-degrading ability.";
RL   Submitted (AUG-2017) 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:GAY07529.1}.
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DR   EMBL; BEGX01000004; GAY07529.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A292YTQ0; -.
DR   OrthoDB; 9775759at2; -.
DR   Proteomes; UP000222857; Unassembled WGS sequence.
DR   GO; GO:0004157; F:dihydropyrimidinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
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; PF01979; Amidohydro_1; 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:GAY07529.1}.
FT   DOMAIN          53..443
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   468 AA;  51278 MW;  DC33A7866C15D9B7 CRC64;
     MYDLIVTNGL VADDRTVQPL DIAVKDEKIV AVGTHGQFSE TGAATVVDAA GKYVLPGGID
     SHVHYDLQIS EAMKAQSSEA GSRAGLWGGT TTYIDFSISW GEEDLVESIQ SKIEKSNSQN
     LYSDYALHAI MTGNWPQSNA DRIREAISGG VTSFKFFTTF AGSEAIGGMM TDDGRIYSAM
     LETEKHGGIV MVHCEDDCII DYNVRKLYSE GREHFSNIGE ARPPLAEEAA IRRMLLLSQR
     TGSPLYIVHV AAKESVEAIG EFRDKGAHAF GEVLHPNLVF DPELYKKPNG QRYMNYPPNK
     SIEHRDALWA ACENGSLHTL ASDDFTIPWD NKMTGDTVDN VTGGTNSVET RLSVFWSEGV
     RKGRLSVPRF VELTSANPAR LFGIYGTKGV LRPGADADIV ILDDGFTHTY KQGENLHSDC
     DYSNWDGWDV NGMPVTTILR GNVMIDKGAF VGPQNVGRFV PATTPETF
//
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