ID   A0A1H9LSH7_9GAMM        Unreviewed;       440 AA.
AC   A0A1H9LSH7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:SER14268.1};
GN   ORFNames=SAMN04488038_11728 {ECO:0000313|EMBL:SER14268.1};
OS   Solimonas aquatica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC   Solimonas.
OX   NCBI_TaxID=489703 {ECO:0000313|EMBL:SER14268.1, ECO:0000313|Proteomes:UP000199233};
RN   [1] {ECO:0000313|EMBL:SER14268.1, ECO:0000313|Proteomes:UP000199233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25927 {ECO:0000313|EMBL:SER14268.1,
RC   ECO:0000313|Proteomes:UP000199233};
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; FOFS01000017; SER14268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9LSH7; -.
DR   STRING; 489703.SAMN04488038_11728; -.
DR   OrthoDB; 5687299at2; -.
DR   Proteomes; UP000199233; 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:UP000199233}.
FT   DOMAIN          49..419
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   440 AA;  48441 MW;  7F9827A5990D0901 CRC64;
     MLITNAHIIN EGHETAADLL IKNGRIEKIA PQIRAPAGVE VFDAQGLWLI PGVIDDQVHF
     REPGLTHKGD LYTESRAAVA GGTTSYMDMP NNKPAITTRA LLAEKYANAQ GRSFANYAFY
     FGGANDNLEE IAALKRDEAC AIKVFMGAST GNMLVDDPQT LDGIFRRAPM MVVTHCEDTP
     MIVASENAAR AQFGEDVPAA EHPRIRSEAA CYKSTELAVG LARQHGSNLH VLHLTTAKEL
     AFFTAGPLKD KKITVEACVH HLFFSEADYA SLGHLIKCNP AIKTEADRRA LLRAVMEDRI
     DVIATDHAPH TAEEKANTYF KAPSGLPLVQ HTLLMLLELV HRGELNMRTV VRKTSHAVAD
     RFGVVDRGYI REGYWADLAL VDHHARTTVR KEDVLYKVGW SPLEGRTLRG AVRATWVNGA
     LAYKDGVVLP QPLGQRLRFV
//