ID   PYRD_AQUAE              Reviewed;         306 AA.
AC   O66461;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 70.
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=aq_046;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC06426.1; -; Genomic_DNA.
DR   PIR; B70304; B70304.
DR   RefSeq; NP_213021.1; -.
DR   HSSP; P54322; 1EP3.
DR   GeneID; 1192658; -.
DR   GenomeReviews; AE000657_GR; aq_046.
DR   KEGG; aae:aq_046; -.
DR   NMPDR; fig|224324.1.peg.36; -.
DR   HOGENOM; O66461; -.
DR   OMA; O66461; NSIGLQN.
DR   BioCyc; AAEO224324:AQ_046-MON; -.
DR   BRENDA; 1.3.3.1; 189781.
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    306       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_0000148386.
FT   ACT_SITE    129    129       Nucleophile (By similarity).
SQ   SEQUENCE   306 AA;  33523 MW;  3E1E04D8DE1FCD53 CRC64;
     MDLSVELFGI RFKNPVWVAS GTFGYGVEAA EIYDISKLGA VVTKGLSLKE RLGNETPRIV
     ETPCGMLNSI GLQNPGVEKF LKEIYPKIKD VDTHFIANVF GETEEEYVEV CMALEDADKI
     VAYELNVSCP NVKKGGILFG HDPVILGNLV DRIKAKIKKP LLVKLSPNVT DVTEFAKVCI
     ENGADGLVLI NTLMGMKINI WKRKPDLATK TGGLSGPAIL PIAVRMIYQV YEKFGDRIPI
     IGVGGITTWE DAMEHVMAGA SAVQVGTANF YEPLAPLKVI EGIENFMKSQ NIKDFKELIG
     IAHRVE
//