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Dihydroorotate dehydrogenase (quinone), mitochondrial (DHOD) (DHODase) (DHOdehase) (EC 1.3.5.2) (Dihydroorotate oxidase)

 PYRD_CANAL              Reviewed;         444 AA.
Q874I4; A0A1D8PEM9; Q5APC9;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
23-MAY-2018, entry version 103.
RecName: Full=Dihydroorotate dehydrogenase (quinone), mitochondrial;
Short=DHOD;
Short=DHODase;
Short=DHOdehase;
EC=1.3.5.2;
AltName: Full=Dihydroorotate oxidase;
Flags: Precursor;
Name=URA9; Synonyms=URA1; OrderedLocusNames=CAALFM_C109720WA;
ORFNames=CaO19.12299, CaO19.4836;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=15014982; DOI=10.1007/s00438-004-0995-7;
Gojkovic Z., Knecht W., Zameitat E., Warneboldt J., Coutelis J.-B.,
Pynyaha Y., Neuveglise C., Moeller K., Loeffler M., Piskur J.;
"Horizontal gene transfer promoted evolution of the ability to
propagate under anaerobic conditions in yeasts.";
Mol. Genet. Genomics 271:387-393(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MMRL 2010;
PubMed=15947202; DOI=10.1128/EC.4.6.1102-1115.2005;
Hall C.R., Brachat S., Dietrich F.S.;
"Contribution of horizontal gene transfer to the evolution of
Saccharomyces cerevisiae.";
Eukaryot. Cell 4:1102-1115(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[4]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[6]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
PubMed=16774642; DOI=10.1111/j.1742-4658.2006.05327.x;
Zameitat E., Gojkovic Z., Knecht W., Piskur J., Loeffler M.;
"Biochemical characterization of recombinant dihydroorotate
dehydrogenase from the opportunistic pathogenic yeast Candida
albicans.";
FEBS J. 273:3183-3191(2006).
-!- FUNCTION: In the de novo pyrimidine biosynthesis pathway,
catalyzes the stereospecific oxidation of (S)-dihydroorotate to
orotate with reduction of flavin and the transfer of electrons to
ubiquinone, which is part of the repiratory chain. Does not use
fumarate and NAD as electron acceptors.
{ECO:0000269|PubMed:16774642}.
-!- CATALYTIC ACTIVITY: (S)-dihydroorotate + a quinone = orotate + a
quinol.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
Note=Binds 1 FMN per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by the dianisidine derivative redoxal
and by brequinar.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=108 uM for (S)-dihydroorotate {ECO:0000269|PubMed:16774642};
KM=42 uM for decylubiquinone {ECO:0000269|PubMed:16774642};
KM=122 uM for 2,6-dichloroindophenol
{ECO:0000269|PubMed:16774642};
Vmax=6 umol/min/mg enzyme {ECO:0000269|PubMed:16774642};
pH dependence:
Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:16774642};
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; orotate from (S)-dihydroorotate (quinone route): step
1/1.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
Single-pass membrane protein {ECO:0000305}.
-!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
Type 2 subfamily. {ECO:0000305}.
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EMBL; AY230865; AAO74621.1; -; Genomic_DNA.
EMBL; AY240959; AAP39962.1; -; Genomic_DNA.
EMBL; CP017623; AOW26604.1; -; Genomic_DNA.
RefSeq; XP_723522.1; XM_718429.1.
ProteinModelPortal; Q874I4; -.
SMR; Q874I4; -.
EnsemblFungi; AOW26604; AOW26604; CAALFM_C109720WA.
GeneID; 3634819; -.
KEGG; cal:CAALFM_C109720WA; -.
CGD; CAL0000178448; URA1.
InParanoid; Q874I4; -.
KO; K00254; -.
OMA; LQNAMGF; -.
OrthoDB; EOG092C261S; -.
BRENDA; 1.3.5.2; 1096.
SABIO-RK; Q874I4; -.
UniPathway; UPA00070; UER00946.
PRO; PR:Q874I4; -.
Proteomes; UP000000559; Chromosome 1.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; NAS:CGD.
GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IDA:CGD.
GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; NAS:CGD.
GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd04738; DHOD_2_like; 1.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR005720; Dihydroorotate_DH.
InterPro; IPR005719; Dihydroorotate_DH_2.
InterPro; IPR001295; Dihydroorotate_DH_CS.
Pfam; PF01180; DHO_dh; 1.
TIGRFAMs; TIGR01036; pyrD_sub2; 1.
PROSITE; PS00911; DHODEHASE_1; 1.
PROSITE; PS00912; DHODEHASE_2; 1.
1: Evidence at protein level;
Complete proteome; Flavoprotein; FMN; Membrane; Mitochondrion;
Mitochondrion inner membrane; Oxidoreductase; Pyrimidine biosynthesis;
Reference proteome; Transit peptide; Transmembrane;
Transmembrane helix.
TRANSIT 1 27 Mitochondrion. {ECO:0000255}.
CHAIN 28 444 Dihydroorotate dehydrogenase (quinone),
mitochondrial.
/FTId=PRO_0000029891.
TRANSMEM 33 53 Helical. {ECO:0000255}.
NP_BIND 124 128 FMN. {ECO:0000250}.
NP_BIND 406 407 FMN. {ECO:0000250}.
REGION 173 177 Substrate binding. {ECO:0000250}.
REGION 254 259 Substrate binding. {ECO:0000250}.
REGION 329 330 Substrate binding. {ECO:0000250}.
ACT_SITE 257 257 Nucleophile. {ECO:0000250}.
BINDING 128 128 Substrate. {ECO:0000250}.
BINDING 148 148 FMN. {ECO:0000250}.
BINDING 224 224 FMN. {ECO:0000250}.
BINDING 254 254 FMN. {ECO:0000250}.
BINDING 300 300 FMN. {ECO:0000250}.
BINDING 328 328 FMN; via carbonyl oxygen. {ECO:0000250}.
BINDING 355 355 FMN; via amide nitrogen. {ECO:0000250}.
BINDING 385 385 FMN; via amide nitrogen. {ECO:0000250}.
SEQUENCE 444 AA; 48426 MW; CD37C62FFA2E6902 CRC64;
MFRPSIKFKQ STLSIIARRL KSSAQHQPLR SSFVPSPIVF VAGLAVAAVG GYYCLDSRSA
IHEYVLCPLI RTFTDAESGH KLGIFFMKYG LSPRLLDDGK NDQSDVLGVQ VFGHKLKNPI
GLAAGLDKDG EAIESLFNCG FSYVEIGSIT PEPQPGNPQP RFFRLPKDDA VINRYGFNSS
GHFNVLATLK LRFNKLLNKF GTSHSSEQHP FSNAFQQGKL LGINLGKNKF GDEVNDYVKG
VERLGPYADV LVINVSSPNT PGLRDLQSEA KLTNLLTTVV KERNVLGKNL LGNKPPVLVK
VAPDLTEPEI ESIANSAKEA KVDGIIISNT TIQRPVDRLL TTDKQLINQA GGLSGKPLKP
LSLKALRTLR KYTKDSDLVL IGCGGISNGK DALEFGKAGA TFIELYTAFA YKGPGLVGKI
RDELAEELRK EGKTWEQIIG SDDK


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