ID   PYRD_CANAL              Reviewed;         444 AA.
AC   Q874I4;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-NOV-2008, entry version 41.
DE   RecName: Full=Dihydroorotate dehydrogenase, mitochondrial;
DE            Short=DHOdehase;
DE            Short=DHODase;
DE            Short=DHOD;
DE            EC=1.3.3.1;
DE   AltName: Full=Dihydroorotate oxidase;
DE   Flags: Precursor;
GN   Name=URA9;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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., Moller K., Loffler M., Piskur J.;
RT   "Horizontal gene transfer promoted evolution of the ability to
RT   propagate under anaerobic conditions in yeasts.";
RL   Mol. Genet. Genomics 271:387-393(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MMRL 2010;
RA   Hall C.R., Dietrich F.S.;
RT   "Candida albicans DHOD.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + O(2) = orotate +
CC       H(2)O(2).
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from HCO(3)(-): step 4/6.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
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DR   EMBL; AY230865; AAO74621.1; -; Genomic_DNA.
DR   EMBL; AY240959; AAP39962.1; -; Genomic_DNA.
DR   HSSP; Q02127; 1D3G.
DR   CGD; CAL0005359; URA1.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine base biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005719; DHO_DHase_2.
DR   InterPro; IPR001295; Dihydroorotate_DHase_core.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF01180; DHO_dh; 1.
DR   TIGRFAMs; TIGR01036; pyrD_sub2; 1.
DR   PROSITE; PS00911; DHODEHASE_1; 1.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Pyrimidine biosynthesis;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    444       Dihydroorotate dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000029891.
FT   ACT_SITE    257    257       Nucleophile (By similarity).
SQ   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
//