ID   PYRD_ANAVT              Reviewed;         376 AA.
AC   Q3MDU0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=Ava_1222;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000117; ABA20846.1; -; Genomic_DNA.
DR   RefSeq; YP_321741.1; -.
DR   GeneID; 3683262; -.
DR   GenomeReviews; CP000117_GR; Ava_1222.
DR   KEGG; ava:Ava_1222; -.
DR   NMPDR; fig|240292.3.peg.1906; -.
DR   HOGENOM; Q3MDU0; -.
DR   OMA; Q3MDU0; AALNRMG.
DR   BioCyc; AVAR240292:AVA_1222-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    376       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_1000024151.
FT   ACT_SITE    193    193       Nucleophile (By similarity).
SQ   SEQUENCE   376 AA;  41318 MW;  0C58CDA5D2A728E8 CRC64;
     MDIYKFAVRP LLFDLVKADP EWLHQQTMRS LSWLSHTSDR TSTKWVQNIL QKSLCIEDSR
     LEQNLFGLRF PNPVGLAAGF DKDGVAARIW SSLGFGFAEL GTVTFVAQPG NPPPRLFRLP
     LDQAALNRMG FNNHGAAVMA TRLADEKGLF SIPIGINLGK SKVTPLEAAA EDYLNSFRLL
     KELGDYFVVN VSSPNTPGLR SLQDASMLSS ILDVLQKENQ SHKPIFVKIA PDLEWEAIAD
     IIGLAKTYQL AGIIATNTTI RRDGLKTQVI EQTGKAPQEE AGGISGAPVR DRSTEIIRFI
     WQQTQGEIPI IGVGGIFTPE DAWAKITAGA SLIQVYTGWI YQGPMMVSQI LTGLLAKLEE
     HELNSISEAI GLEFKS
//