ID   A0A1T5GLH5_9FLAO        Unreviewed;       444 AA.
AC   A0A1T5GLH5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:SKC09190.1};
GN   ORFNames=SAMN05660477_02950 {ECO:0000313|EMBL:SKC09190.1};
OS   Soonwooa buanensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Soonwooa.
OX   NCBI_TaxID=619805 {ECO:0000313|EMBL:SKC09190.1, ECO:0000313|Proteomes:UP000191112};
RN   [1] {ECO:0000313|EMBL:SKC09190.1, ECO:0000313|Proteomes:UP000191112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22323 {ECO:0000313|EMBL:SKC09190.1,
RC   ECO:0000313|Proteomes:UP000191112};
RA   Peterson S.W.;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FUYZ01000013; SKC09190.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5GLH5; -.
DR   STRING; 619805.SAMN05660477_02950; -.
DR   OrthoDB; 9765462at2; -.
DR   Proteomes; UP000191112; 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:UP000191112}.
FT   DOMAIN          50..424
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   444 AA;  49635 MW;  AF459F98C97037F4 CRC64;
     MKSLIKNAKI VNEGQIFESD LLIENDLISK IAKNIPESEA DKVIDATGKY LLPGVIDDQV
     HFREPGLTNK GDIASESKSA IAGGVTSFID QPNTVPNAVT QELLEEKYKL GAEKSYANYS
     FSMGGTNDNL EEVLKTNPKN VSAIKLFLGS STGNMLVDNP ETLEKIFSST KMLICVHCED
     EDTIKANTEK YKSEYGDDIP VKFHHLIRSE GACYKSSSKA IELAQKTGAR LHIFHLSTAK
     ETALFRNDIP LKDKKITAEV CVHHLTFTND DYETKGSLIK WNPAVKTQAD KDGLWEALLD
     DRIDVIATDH APHTWEEKQN LYTSCPSGAP LVQHSLPVML ENYHNGKISL EKLVEKMCHN
     PAILFEVDKR GFVKEGYKAD LVLIDMDNPW TIAKDNILYK CGWSPLEGTN LKSKITQTFV
     NGHLAYDNGI FSEEKHGERL EFDR
//