ID   A0A1H9W5C4_9SPHI        Unreviewed;       444 AA.
AC   A0A1H9W5C4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:SES29156.1};
GN   ORFNames=SAMN04488023_1598 {ECO:0000313|EMBL:SES29156.1};
OS   Pedobacter rhizosphaerae.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=390241 {ECO:0000313|EMBL:SES29156.1, ECO:0000313|Proteomes:UP000199572};
RN   [1] {ECO:0000313|EMBL:SES29156.1, ECO:0000313|Proteomes:UP000199572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18610 {ECO:0000313|EMBL:SES29156.1,
RC   ECO:0000313|Proteomes:UP000199572};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOGG01000059; SES29156.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9W5C4; -.
DR   STRING; 390241.SAMN04488023_1598; -.
DR   OrthoDB; 9765462at2; -.
DR   Proteomes; UP000199572; Unassembled WGS sequence.
DR   GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:InterPro.
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   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199572}.
FT   DOMAIN          50..424
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   444 AA;  49307 MW;  93DD7D8FF7DAC022 CRC64;
     MNTYLIKGAT IVNEGQKQVA DVLIKDGLIA KIGQNLSAPE AKEINAEGQY LLPGMIDDQV
     HFREPGLTHK ADIFTESMAA VAGGITSFME MPNTVPNTLT QALLKDKYDI ASQTSLANYS
     FYMGASNDNI DEVLKTDPKN VCGIKVFMGS STGNMLVDNE KTLENIFSQA PILVATHCED
     EQTIRENLAK FKAEYGENLT IDMHPLIRSA EACYKSSSLA VELAKKYQTR LHILHISTAK
     EIALFDNTIP LKDKKITAEA CVHHLWFNDQ DYAAKGNFIK WNPAVKTKAD QDGILQGVLN
     DNIDVIATDH APHTLEEKQQ PYAQAPSGGP LVQHALPALL EMHLQGKISL EKIVEKTAHN
     LAICFDIEKR GFIREGYWAD LVLVDLNDPW TVIKLNNFYK CGWSPFDGNT FQASITHTFV
     SGNLAYQKGK FTTDEIGKRL TFTR
//