ID   A0A1H1QU02_9FLAO        Unreviewed;       447 AA.
AC   A0A1H1QU02;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:SDS26867.1};
GN   ORFNames=SAMN04489797_1231 {ECO:0000313|EMBL:SDS26867.1};
OS   Winogradskyella sediminis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=1382466 {ECO:0000313|EMBL:SDS26867.1, ECO:0000313|Proteomes:UP000198963};
RN   [1] {ECO:0000313|EMBL:SDS26867.1, ECO:0000313|Proteomes:UP000198963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA_55 {ECO:0000313|EMBL:SDS26867.1,
RC   ECO:0000313|Proteomes:UP000198963};
RA   Varghese N., Submissions S.;
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; LT629774; SDS26867.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1QU02; -.
DR   STRING; 1249933.SAMN04489797_1231; -.
DR   Proteomes; UP000198963; Chromosome I.
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}.
FT   DOMAIN          53..428
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   447 AA;  49975 MW;  8E23F8C1E1518BF3 CRC64;
     MKRNTLIKNA RIVNEGKIIE GDIFIEDQII KEIETSISVK SADINVIDAE GKYVFPGMID
     DQVHFREPGL THKANIESES KAAIAGGITS FIEMPNTNPQ TTTVEKLEDK FAIAAASSYA
     NYSFMFGGTN DNLEEILKVD PKTVAGLKLF LGSSTGNMLV DDPKVIEKIF SSTDMVISVH
     CEDEATIKAN LAKYNAEYGD DIPMEMHPII RSEEACYMSS SKAIELAKKT GARLHVFHLS
     TGKETKLFSN KIPLKDKKIT AEVCVHHLWF SDEDYAKKGS HIKWNPAVKT SKDRDQLWKA
     LLDDRIDVIA TDHAPHTLEE KNNNYTNAPS GGPLVQHALV ALMEAHHQGK ISVEKIVEKA
     CHNPAILFNV EKRGYIKEGY FADLVIIDPQ SPWTVNKSNI LYKCAWSPFE GNTFKSRITH
     TFVNGQLVYN NFNVLDVKAG QRLTFDR
//