ID X5HJ69_9RICK Unreviewed; 438 AA.
AC X5HJ69;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 13-SEP-2023, entry version 48.
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 ECO:0000313|EMBL:AHX11109.1};
GN ORFNames=NHE_0141 {ECO:0000313|EMBL:AHX11109.1};
OS Neorickettsia helminthoeca str. Oregon.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Neorickettsia.
OX NCBI_TaxID=1286528 {ECO:0000313|EMBL:AHX11109.1, ECO:0000313|Proteomes:UP000023755};
RN [1] {ECO:0000313|EMBL:AHX11109.1, ECO:0000313|Proteomes:UP000023755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon {ECO:0000313|EMBL:AHX11109.1,
RC ECO:0000313|Proteomes:UP000023755};
RA Lin M., Daugherty S.C., Nagaraj S., Cheng Z., Xiong Q., Lin F.-Y.,
RA Sengamalay N., Ott S., Godinez A., Tallon L.J., Sadzewicz L., Fraser C.M.,
RA Dunning Hotopp J.C., Rikihisa Y.;
RT "Sequencing and Comparison of Genomes and Transcriptome Profiles of Human
RT Ehrlichiosis Agents.";
RL Submitted (MAR-2014) 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}.
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DR EMBL; CP007481; AHX11109.1; -; Genomic_DNA.
DR RefSeq; WP_038558849.1; NZ_CP007481.1.
DR AlphaFoldDB; X5HJ69; -.
DR STRING; 1286528.NHE_0141; -.
DR KEGG; nhm:NHE_0141; -.
DR HOGENOM; CLU_015572_1_0_5; -.
DR OrthoDB; 9803027at2; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000023755; Chromosome.
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; PS00482; DIHYDROOROTASE_1; 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:UP000023755};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00220}.
FT DOMAIN 67..434
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 319
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 78..80
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 337..338
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
SQ SEQUENCE 438 AA; 47697 MW; 3153087C7DFBB2A3 CRC64;
MAKWNLPERR DKKIAFVDAN IIDPESGLEI FGDLVVSDGK ISDFGESLLS EIELKSFDEV
INCSGYFLIP GVIDIHVHLR DPGQLYNEDI HSGTKAAAAG GVTTVVCQPN TKPPINTVET
LKYIRDKART EGFVNVLCYA AITNDGNELT DMFALHKAGA VGFTDDGLPV MNPLLMRQAF
ANAAFLKVPV AQHAEDLYLS NGGCINEGVM SHKLNVPGIT DLAESVMVAR DVMLLDQLDS
HYHVLHVSTK KAVEIIETAK SRGMNVTCEV TPHHFLLTEE AVVDYNTDAK MNPPLRTEQD
RLYMIEALKN STIDAIASDH APHNGLYKNL PLREAAFGII GLETILPLSL ELYHDGVMDL
HSLLAKLTCN PARIINSSAG RIKVGAPADL VLLDLNAEIV IDSAKFVSKS KNSPFVGRKT
KGKVLRTIVA GDSVYTAD
//
