ID   PYRD_BACTN              Reviewed;         303 AA.
AC   Q8A9C3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Dihydroorotate dehydrogenase;
DE            EC=1.3.3.1;
DE   AltName: Full=Dihydroorotate oxidase;
DE   AltName: Full=DHOdehase;
DE            Short=DHODase;
DE            Short=DHOD;
GN   Name=pyrD; OrderedLocusNames=BT_0892;
OS   Bacteroides thetaiotaomicron.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX   MEDLINE=22550858; PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA   Chiang H.C., Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + O(2) = orotate +
CC       H(2)O(2).
CC   -!- COFACTOR: Binds 1 FMN per subunit (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from HCO(3)(-): step 4/6.
CC   -!- SUBUNIT: Heterotetramer of 2 pyrK and 2 pyrD subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC       Type 1 subfamily.
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DR   EMBL; AE015928; AAO75999.1; -; Genomic_DNA.
DR   RefSeq; NP_809805.1; -.
DR   HSSP; P54322; 1EP2.
DR   GeneID; 1074664; -.
DR   GenomeReviews; AE015928_GR; BT_0892.
DR   KEGG; bth:BT_0892; -.
DR   NMPDR; fig|226186.1.peg.892; -.
DR   HOGENOM; Q8A9C3; -.
DR   OMA; Q8A9C3; NSIGLQN.
DR   BioCyc; BTHE226186:BT_0892-MON; -.
DR   BRENDA; 1.3.3.1; 21018.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:HAMAP.
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:0006222; P:UMP biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00224; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR005720; Dihydroorotate_DH_1_core.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
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   Complete proteome; Cytoplasm; Flavoprotein; FMN; Oxidoreductase;
KW   Pyrimidine biosynthesis.
FT   CHAIN         1    303       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_1000024131.
FT   ACT_SITE    130    130       Nucleophile (By similarity).
SQ   SEQUENCE   303 AA;  32296 MW;  B51FAAF443050485 CRC64;
     MADLSVNIGE LQMKNPVMTA SGTFGYGEEF SDFIDIARIG GIIVKGTTLH KREGNPYPRM
     AETPSGMLNA VGLQNKGVDY FVEQIYPRIK DIQTNMIVNV SGSAIEDYVK TAEIINELDK
     IPAIELNISC PNVKQGGMAF GVSAKGASEV VKAVRAAYKK TLIVKLSPNV TDITEIARAA
     EESGADSVSL INTLLGMAID AERKRPILST VTGGMSGAAV KPIALRMVWQ VAKAVNIPVI
     GLGGIMNWKD AVEFMLAGAS AIQIGTANFI DPAVTIKVED GINNYLERHG CKSVKEIIGA
     LEV
//