PYRD_NAUCC
ID PYRD_NAUCC Reviewed; 314 AA.
AC Q6V3X0; G0VEE2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Dihydroorotate dehydrogenase (fumarate);
DE Short=DHOD;
DE Short=DHODase;
DE Short=DHOdehase;
DE EC=1.3.98.1;
DE AltName: Full=Dihydroorotate oxidase;
GN Name=URA1; OrderedLocusNames=NCAS_0D03520;
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630;
RX PubMed=15947202; DOI=10.1128/ec.4.6.1102-1115.2005;
RA Hall C.R., Brachat S., Dietrich F.S.;
RT "Contribution of horizontal gene transfer to the evolution of Saccharomyces
RT cerevisiae.";
RL Eukaryot. Cell 4:1102-1115(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with
CC fumarate as the electron acceptor. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + fumarate = orotate + succinate;
CC Xref=Rhea:RHEA:30059, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:30839, ChEBI:CHEBI:30864; EC=1.3.98.1;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 1 FMN per subunit. {ECO:0000250};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; AY352581; AAQ57200.1; -; Genomic_DNA.
DR EMBL; HE576755; CCC69933.1; -; Genomic_DNA.
DR RefSeq; XP_003676294.1; XM_003676246.1.
DR AlphaFoldDB; Q6V3X0; -.
DR SMR; Q6V3X0; -.
DR STRING; 1064592.Q6V3X0; -.
DR EnsemblFungi; CCC69933; CCC69933; NCAS_0D03520.
DR GeneID; 11528366; -.
DR KEGG; ncs:NCAS_0D03520; -.
DR eggNOG; KOG1436; Eukaryota.
DR HOGENOM; CLU_042042_3_0_1; -.
DR InParanoid; Q6V3X0; -.
DR OMA; SCPHAKG; -.
DR OrthoDB; 1194348at2759; -.
DR UniPathway; UPA00070; -.
DR Proteomes; UP000001640; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990663; F:dihydroorotate dehydrogenase (fumarate) activity; IEA:UniProtKB-EC.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04741; DHOD_1A_like; 1.
DR Gene3D; 2.30.26.10; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00224; DHO_dh_type1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR033886; DHOD_1A.
DR InterPro; IPR023359; Dihydro_DH_chainA_dom2.
DR InterPro; IPR005720; Dihydroorotate_DH.
DR InterPro; IPR024920; Dihydroorotate_DH_1.
DR InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR InterPro; IPR001295; Dihydroorotate_DH_CS.
DR Pfam; PF01180; DHO_dh; 1.
DR PIRSF; PIRSF000164; DHO_oxidase; 1.
DR TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1.
DR PROSITE; PS00911; DHODEHASE_1; 1.
DR PROSITE; PS00912; DHODEHASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Flavoprotein; FMN; Oxidoreductase; Pyrimidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..314
FT /note="Dihydroorotate dehydrogenase (fumarate)"
FT /id="PRO_0000148502"
FT ACT_SITE 132
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 133
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 46..47
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 70..74
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 196..197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 252..253
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 274..275
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
SQ SEQUENCE 314 AA; 34862 MW; E9D0960598AC30D4 CRC64;
MPASLTTKFL NQTYENPLMN ASGVHCMTTK ELDELAASRA GAFITKSSTT LERAGNPEPR
YVSVPLGSIN SMGLPNQGID YYLEYVLERQ RTHPNEPAIF FSVAGMSIDE NINMLRKIQD
SEFHGITELN LSCPNVPGKP QVAYDFDLTK EILDKVFQFF KKPLGIKLPP YFDFAHFDIM
AGILNQYPLA YVNSINSVGN GLYIDVDKES VVVKPKNGFG GIGGEYVKPT ALANVRAFYT
RLNPSIKIVG TGGIRTGKDV FEHLLCGASM VQIGTELVKE GVPIFERLER ELKEVMDKKG
YTTIEEFRGK LNSL
