PYRD1_LACK1
ID PYRD1_LACK1 Reviewed; 314 AA.
AC Q7Z892;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
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;
OS Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 /
OS JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=226302;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543
RC / NRRL Y-12651;
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 [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=15014982; DOI=10.1007/s00438-004-0995-7;
RA Gojkovic Z., Knecht W., Zameitat E., Warneboldt J., Coutelis J.-B.,
RA Pynyaha Y., Neuveglise C., Moeller K., Loeffler M., Piskur J.;
RT "Horizontal gene transfer promoted evolution of the ability to propagate
RT under anaerobic conditions in yeasts.";
RL Mol. Genet. Genomics 271:387-393(2004).
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 -!- ACTIVITY REGULATION: The activity is independent of the presence of
CC oxygen.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: S.kluyveri has two isoforms of DHODase, a cytoplasmic
CC isoform and a mitochondrial isoform.
CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY323902; AAQ01779.1; -; Genomic_DNA.
DR EMBL; AF452109; AAQ04683.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7Z892; -.
DR SMR; Q7Z892; -.
DR SABIO-RK; Q7Z892; -.
DR UniPathway; UPA00070; -.
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 1: Evidence at protein level;
KW Cytoplasm; Flavoprotein; FMN; Oxidoreductase; Pyrimidine biosynthesis.
FT CHAIN 1..314
FT /note="Dihydroorotate dehydrogenase (fumarate)"
FT /id="PRO_0000148503"
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; 34855 MW; C7501535D7800D84 CRC64;
MSASLAINFL NHTYENPFMN ASGVHCMSTK ELDELKDSRA GAFITKSSTT SKREGNPEPR
YFSVPLGSIN SMGLPNEGFD YYLKYALEYQ KNGSTSTPLF FSVAGMSVEE NLKMLQKIQD
SDFNGITELN LSCPNVPGKP QVAYDFELTK EILTKVFEFF KKPLGVKLPP YFDFAHFDIM
AGILNQLPLS YVNCINSIGN GLYINVETES VVVKPKNGFG GIGGEYVKPT ALANVRAFYT
RLNPTIKIIG TGGIKTGQDA FEHLLCGATM LQVGTELYKE GVSIFDRLER ELKELMDKKG
YTSIEQFRGK LNSL
