ID A0A3N1KPG7_9PROT Unreviewed; 430 AA.
AC A0A3N1KPG7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Dihydroorotase {ECO:0000256|HAMAP-Rule:MF_00220};
DE Short=DHOase {ECO:0000256|HAMAP-Rule:MF_00220};
DE EC=3.5.2.3 {ECO:0000256|HAMAP-Rule:MF_00220};
GN Name=pyrC {ECO:0000256|HAMAP-Rule:MF_00220};
GN ORFNames=EDC65_5038 {ECO:0000313|EMBL:ROP81182.1};
OS Stella humosa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Stellaceae; Stella.
OX NCBI_TaxID=94 {ECO:0000313|EMBL:ROP81182.1, ECO:0000313|Proteomes:UP000278222};
RN [1] {ECO:0000313|EMBL:ROP81182.1, ECO:0000313|Proteomes:UP000278222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5900 {ECO:0000313|EMBL:ROP81182.1,
RC ECO:0000313|Proteomes:UP000278222};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC to dihydroorotate. {ECO:0000256|ARBA:ARBA00002368, ECO:0000256|HAMAP-
CC Rule:MF_00220}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00220};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00220};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00220};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000256|HAMAP-
CC Rule:MF_00220}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class I DHOase subfamily.
CC {ECO:0000256|ARBA:ARBA00010286, ECO:0000256|HAMAP-Rule:MF_00220}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00220}.
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:ROP81182.1}.
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DR EMBL; RJKX01000018; ROP81182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1KPG7; -.
DR OrthoDB; 9803027at2; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000278222; Unassembled WGS sequence.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01317; DHOase_IIa; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR HAMAP; MF_00220_B; PyrC_classI_B; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR004722; DHOase.
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:SF2; 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:0000256|HAMAP-Rule:MF_00220};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00220}; Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00220};
KW Reference proteome {ECO:0000313|Proteomes:UP000278222};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00220}.
FT DOMAIN 57..425
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 310
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
SQ SEQUENCE 430 AA; 45120 MW; 09863AE6743FDEE5 CRC64;
MTRVALANAR LFDPATGRDT PGGLLIVDGR IADLGPALFA DGVPEGAEAI DCAGRLLVPG
LIDMRAQLRE PGNEHQENMA TASQAAVAGG ITTIVCLPNT DPVIDDVALV EFVRRRGRDI
GLAHIHPYAA ATKGLAGKEL TEMGLLAEAG AVGFTDGTRA IANAGIMRRA LSYARTFDLL
LVQHPEEPTL SHPGGMNEGE IATRLGLPGI PAMAEVVLLE RDLRLVELTG ARYHAAHLST
AGAVEAIRDA KRRGLPVTCD TAPPYFALNE TAVGDYRTFA KLSPPLRSDG DRRAIVAGIA
DGTIDAIASD HAPHDQDSKR LPFSSAASGI IGLETLLPLV LELAHQGDVP LARALAAVTA
APAGILGLDC GRLAVGAPAD LTLIDLDRPW RIAVDRFRSK SKNSPFDGRP VQGRAAMTML
GGRVVHRVAD
//
