ID   A0A239RIH0_9BACT        Unreviewed;       449 AA.
AC   A0A239RIH0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:SNU10720.1};
GN   ORFNames=SAMN06298210_104110 {ECO:0000313|EMBL:SNU10720.1};
OS   Prevotellaceae bacterium KH2P17.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae.
OX   NCBI_TaxID=1945886 {ECO:0000313|EMBL:SNU10720.1, ECO:0000313|Proteomes:UP000214740};
RN   [1] {ECO:0000313|EMBL:SNU10720.1, ECO:0000313|Proteomes:UP000214740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH2P17 {ECO:0000313|EMBL:SNU10720.1,
RC   ECO:0000313|Proteomes:UP000214740};
RA   Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL   Submitted (JUL-2017) 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; FZRE01000004; SNU10720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239RIH0; -.
DR   Proteomes; UP000214740; 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   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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214740}.
FT   DOMAIN          52..400
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   449 AA;  49230 MW;  192CF5F26D96E649 CRC64;
     MKIRIVGGTV VNEGRSFKAD IVTENDRIAE IIEDTKTPRG SYNQEVDATG CFVLPGVIDE
     HVHFREPGLT RKGDIGSESR AAAYGGVTSY FEMPNTVPQT TTPEALASKF TLAREKSHVN
     YSFFFGATND NAPLFKQLDC HSIPGIKLFM GASTGNMLVD KTDSLALVFR TAADLGLPVM
     THCEDTALIN RNMSEAKKRY GDDPPIALHP LIRSAQACFN SSSLAVRLAR ENGTRLHIAH
     VSTAAELELI TANAPAEALP QITMEATPAH LFFSDADYHD LGARIKCNPA VKTDADRAAL
     RKALADGRIT CIGTDHAPHE LADKQGGCAK AASGMPMVQF SLPLMLELVD RKVLTIERLV
     ELMSHNPARL FGVNGRGYLR KGCKADIVIV KPHSPWTVTE RTIQSKCKWS PLLGHRFSWQ
     IRQTLCNGRL IYNLGQFDES SRGEAINFR
//