ID   A0A437M4V5_9SPHN        Unreviewed;       443 AA.
AC   A0A437M4V5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:RVT92709.1};
DE            EC=3.5.2.3 {ECO:0000313|EMBL:RVT92709.1};
GN   ORFNames=EOD43_01955 {ECO:0000313|EMBL:RVT92709.1};
OS   Sphingomonas crocodyli.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1979270 {ECO:0000313|EMBL:RVT92709.1, ECO:0000313|Proteomes:UP000282971};
RN   [1] {ECO:0000313|EMBL:RVT92709.1, ECO:0000313|Proteomes:UP000282971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCP-7 {ECO:0000313|EMBL:RVT92709.1,
RC   ECO:0000313|Proteomes:UP000282971};
RA   Chen W.-M.;
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC       to dihydroorotate. {ECO:0000256|ARBA:ARBA00002368}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       DHOase family. Class I DHOase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010286}.
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:RVT92709.1}.
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DR   EMBL; SACN01000001; RVT92709.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A437M4V5; -.
DR   OrthoDB; 9775759at2; -.
DR   Proteomes; UP000282971; Unassembled WGS sequence.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   CDD; cd01318; DHOase_IIb; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR00857; pyrC_multi; 1.
DR   PANTHER; PTHR43668; ALLANTOINASE; 1.
DR   PANTHER; PTHR43668:SF4; ALLANTOINASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RVT92709.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          52..420
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   443 AA;  48102 MW;  3C04FB91EF60D7AB CRC64;
     MTSPTYDLIL KNGTVWTVGG PIETSVGVRG GKIVAIGEDG DAGEVIDCAG LTVLPGVIDS
     QVHFREPGLE AKEDLESGSR SAVLGGVTAV FEMPNTKPNT DSAEAINDKL ARAKDRMWCD
     HAFYVGATTE NAEKLAELEM LPGTAGVKIF MGSSTGNLLV AEDDHLARVL RSGKRRVAIH
     AEDEQRMIAR MSERVEGDPA SHPVWRDDES ALLATRRILK IARETGRKIH ILHITTPAEL
     ALIAQNKDIA TCEVTPQHLT LAGEEAYPRL GTYAQMNPPI RSGAHRDGLW HYLRQGVPDV
     LGSDHAPHTI EEKAKTYPAS PSGMPGVQTL LPLMLNHVAE GRLTLQHLIE LTSAGPQRVF
     GLRSKGRIAL GYDADFTIVD LKKRWKVEES WLASRCGWSP FTDMELTGKP IGTVIRGNRV
     MWDGGLANQA IGAPIRFDSV ALV
//