ID A0A0A2M6Q8_9FLAO Unreviewed; 447 AA.
AC A0A0A2M6Q8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:KGO87301.1};
DE EC=3.5.2.3 {ECO:0000313|EMBL:KGO87301.1};
GN ORFNames=Q765_06440 {ECO:0000313|EMBL:KGO87301.1};
OS Flavobacterium rivuli WB 3.3-2 = DSM 21788.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1121895 {ECO:0000313|EMBL:KGO87301.1, ECO:0000313|Proteomes:UP000030152};
RN [1] {ECO:0000313|EMBL:KGO87301.1, ECO:0000313|Proteomes:UP000030152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB 3.3-2 {ECO:0000313|EMBL:KGO87301.1,
RC ECO:0000313|Proteomes:UP000030152};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO87301.1}.
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DR EMBL; JRLX01000005; KGO87301.1; -; Genomic_DNA.
DR RefSeq; WP_020213380.1; NZ_KB899970.1.
DR AlphaFoldDB; A0A0A2M6Q8; -.
DR STRING; 1121895.GCA_000378485_02221; -.
DR eggNOG; COG0044; Bacteria.
DR OrthoDB; 9765462at2; -.
DR Proteomes; UP000030152; Unassembled WGS sequence.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:KGO87301.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030152}.
FT DOMAIN 52..427
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 447 AA; 49892 MW; 2AD50FFCDF2238B5 CRC64;
MNRILIKNAK IVNEGTIFEG DLFIEDKFIK EIGEKISPKT GDCVIIDAEG SFLIPGAIDD
QVHFREPGLT HKGTIETESR AAVAGGITSY IEQPNTVPNA VTQELLEDKY NRAAGVSFAN
YSFMMGGTND NLEEVLKTNP KNVAGIKLFL GSSTGNMLVD NTEVLEKIFS STKMLIAVHC
EDEATIQANL ARFKEEYGDD IPVKFHPEIR SAEACYISSS RAVELAKKTG ARLHVFHVST
GIETDLFTNK IPLEDKMITA EVCVHHLWFT DADYATKGAL IKWNPAVKSA ADKDALWKAL
LDDRIDVIAT DHAPHTLEEK KNPYTSSPSG GPLVQHAVVA MFEAYHQKKI SVEKIVEKMA
HNPAKIFKIE KRGFIREGYY ADLVIVNPGL PWNVKKENIL YKCGWSPFEG VNFKSRISHT
FVNGQLVYNN FKVKDIRSGE RLLFNRE
//
