ID   PYRD_ARCFU              Reviewed;         299 AA.
AC   O29513;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 72.
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=AF_0745;
OS   Archaeoglobus fulgidus.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=2234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   MEDLINE=98049343; PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB90494.1; -; Genomic_DNA.
DR   PIR; A69343; A69343.
DR   RefSeq; NP_069579.1; -.
DR   HSSP; P54322; 1EP2.
DR   GeneID; 1483962; -.
DR   GenomeReviews; AE000782_GR; AF_0745.
DR   KEGG; afu:AF0745; -.
DR   NMPDR; fig|224325.1.peg.738; -.
DR   TIGR; AF_0745; -.
DR   HOGENOM; O29513; -.
DR   OMA; O29513; NSIGLQN.
DR   BioCyc; AFUL224325:AF_0745-MON; -.
DR   BRENDA; 1.3.3.1; 7576.
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    299       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_0000148407.
FT   ACT_SITE    128    128       Nucleophile (By similarity).
SQ   SEQUENCE   299 AA;  32114 MW;  03578C9CA8F3FB75 CRC64;
     MNPLETEIGG LRMKNPLMLA SGIMGSKVHS LNLIARDAGA VVTKSVGVEE REGYRNPTVV
     NWKCGLINAV GLASPAAKDF AEELKDYTNE APLLISLYGH SVEEFSDLVD TFDSALPYLH
     GYELNLSCPH VKGAGLDIGM DLELSAAIVE ELKGKTKNPV FAKLSAMHDY LKLAKVLEDA
     GVDGITISNT LRGMKIDIMS GKPVLSNLSG GVSGPAIKPI ALKCVYDLYK EIEVPIVGCG
     GITSFEDVLE FIMAGARAVQ IGSAVYYSRR IFYSLKESLI AFTRARDCTI SDLIGIAHS
//