ID   PYRD_BUCAP              Reviewed;         336 AA.
AC   Q8K9I5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 54.
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=BUsg_350;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC       Type 2 subfamily.
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DR   EMBL; AE013218; AAM67903.1; -; Genomic_DNA.
DR   RefSeq; NP_660692.1; -.
DR   HSSP; P05021; 1F76.
DR   GeneID; 1005806; -.
DR   GenomeReviews; AE013218_GR; BUsg_350.
DR   KEGG; bas:BUsg350; -.
DR   HOGENOM; Q8K9I5; -.
DR   OMA; Q8K9I5; NAEQQGG.
DR   BioCyc; BAPH198804:BUSG350-MON; -.
DR   GO; GO:0005886; C:plasma membrane; 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_00225; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR005719; Dihydroorotate_DH_2.
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; TIGR01036; pyrD_sub2; 1.
DR   PROSITE; PS00911; DHODEHASE_1; 1.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Flavoprotein; FMN; Membrane;
KW   Oxidoreductase; Pyrimidine biosynthesis.
FT   CHAIN         1    336       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_0000148427.
FT   ACT_SITE    175    175       Nucleophile (By similarity).
SQ   SEQUENCE   336 AA;  38101 MW;  19B8F807BF49DE83 CRC64;
     MFYYLIRKLL FLIDPEKAHT LVLMYLNSKK IQILRKIFIK PIPLKQIKCM GLTFNNKIGL
     AAGMDKNGDY IDSLSKIGFG FIEVGTVTPL PQYGNPKPRI FRVPSIEGII NRMGFNNLGI
     DYLVNNVKKS KFKGIIGINI GKNKDTKIED AIKDYLICIE KIYFYASYIA INISSPNTIN
     LRKLQYGILF ENLLRDIKKK QSEMHSKYSK YVPIVIKISP DLSKKELIHI SNKLIHYKID
     GVIATNTTLD HSSIPKIKNN KEEGGLSGLP LQKKSNDVIS ILYKNLKRKI PIIGVGGINS
     INSAREKIMC GANLIQVYSG LIYHGPNFIR EIIRNL
//