ID   PYRD_ANASP              Reviewed;         376 AA.
AC   Q8YPC6;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-NOV-2008, entry version 45.
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=all4272;
OS   Anabaena sp. (strain PCC 7120).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA   Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB75971.1; -; Genomic_DNA.
DR   PIR; AI2339; AI2339.
DR   RefSeq; NP_488312.1; -.
DR   HSSP; Q02127; 1D3G.
DR   GeneID; 1107874; -.
DR   GenomeReviews; BA000019_GR; all4272.
DR   KEGG; ana:all4272; -.
DR   NMPDR; fig|103690.1.peg.4579; -.
DR   HOGENOM; Q8YPC6; -.
DR   BioCyc; NSP103690:ALL4272-MON; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:HAMAP.
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; DHO_DHase_1_2.
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   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    376       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_0000148421.
FT   ACT_SITE    193    193       Nucleophile (By similarity).
SQ   SEQUENCE   376 AA;  41291 MW;  4F6A60E6734144A1 CRC64;
     MDIYKFAVRP LLFDLVKADP EWLHQQTMRS LSWLSHTSDR TSTKWVQNIL QKSLCLEDSR
     LEQNLFGLRF PNPVGLAAGF DKDGVAARIW SSLGFGFAEL GTVTFVGQPG NPPPRLFRLP
     LDQAALNRMG FNNHGAAVMA ARLADEKGQF SIPIGINLGK SKVTPLEAAA EDYLNSFRLL
     KELGDYFVVN VSSPNTPGLR SLQDASMLSS ILDVLQKENN SHKPIFVKIA PDLEWEAIAD
     IIGLAKTYQL AGIIATNTTI RRDGLKTQVI EQTGKAPQEE AGGISGAPVR DRSTEIIRFI
     WQQTQGEIPI IGVGGIFTPE DAWAKITAGA SLIQVYTGWI YQGPMMVSQI LTGLLSKLEE
     HELNSISEAI GLEFKS
//