ID   A0A1U9L982_9FLAO        Unreviewed;       446 AA.
AC   A0A1U9L982;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:AQS94624.1};
GN   ORFNames=BXQ17_11330 {ECO:0000313|EMBL:AQS94624.1};
OS   Polaribacter sp. BM10.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1529069 {ECO:0000313|EMBL:AQS94624.1, ECO:0000313|Proteomes:UP000189235};
RN   [1] {ECO:0000313|EMBL:AQS94624.1, ECO:0000313|Proteomes:UP000189235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BM10 {ECO:0000313|EMBL:AQS94624.1,
RC   ECO:0000313|Proteomes:UP000189235};
RA   Lee J.-Y., Bae J.-W.;
RT   "Polaribacter aureus sp. nov., isolated from the gut of a blood cockle,
RT   tegillarca granosa.";
RL   Submitted (FEB-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; CP019704; AQS94624.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9L982; -.
DR   STRING; 1529069.BXQ17_11330; -.
DR   KEGG; pola:BXQ17_11330; -.
DR   OrthoDB; 9765462at2; -.
DR   Proteomes; UP000189235; Chromosome.
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          52..426
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   446 AA;  49973 MW;  7FFB264599DFB0DE CRC64;
     MAKSTLIKNA TIVNENKTFK GDVLIENEII KEISTEIKAP ENVTVINADG KYLIPGFIDD
     QVHFREPGLT HKANIATESR AAVAGGITTF IEMPNTVPQA TTQELLEDKF KIAANDSYAN
     YSFMFGGTND NLDELLKTNP KQVAGIKLFL GSSTGNMLVD NEAVLEKIFS STKMIISVHC
     EDEATIRKNT QEYKDKYGDD IPVKYHPIIR SEEACYLSSS KAIELAKKTG ARLHIFHLST
     AKETELFRND IPLEEKQITA EVCIHHLWFS DKDYEEKGTH IKWNPAVKTE NDRQGLWKAL
     LDDRIDVLAT DHAPHTLEEK DNVYTKAPSG GPLVQHAVSA ILEKVKEGVI SIEKAVEKMS
     HNPAKLFQIE KRGFIKEGFY ADLVLIDANK PQTVSKENIL YKCGWSPFEG TTFSSTITHT
     FVNGNLMYNE GAFNDTIKGK RITFNR
//