ID   PYRD_ALKMQ              Reviewed;         302 AA.
AC   A6TVS0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-NOV-2008, entry version 17.
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=Amet_4208;
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Ye Q.,
RA   Zhou J., Fields M., Richardson P.;
RT   "Complete sequence of Alkaliphilus metalliredigens QYMF.";
RL   Submitted (JUN-2007) 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: 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; CP000724; ABR50288.1; -; Genomic_DNA.
DR   RefSeq; YP_001321947.1; -.
DR   GeneID; 5314289; -.
DR   GenomeReviews; CP000724_GR; Amet_4208.
DR   KEGG; amt:Amet_4208; -.
DR   GO; GO:0005737; C:cytoplasm; 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_00224; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012135; DHO_DHase_1_2.
DR   InterPro; IPR005720; DHO_DHase_1_core.
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; TIGR01037; pyrD_sub1_fam; 1.
DR   PROSITE; PS00911; DHODEHASE_1; FALSE_NEG.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Flavoprotein; FMN; Oxidoreductase;
KW   Pyrimidine biosynthesis.
FT   CHAIN         1    302       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_0000336441.
FT   ACT_SITE    131    131       Nucleophile (By similarity).
SQ   SEQUENCE   302 AA;  31990 MW;  10B9FD75BCFE7B4F CRC64;
     MTKVNMKVNI AGVELKNPVM TASGTFGSGR EYGEYVDLNQ LGAVVVKGVA NEPWKGNPSP
     RIAETYGGML NSVGLQNPGV DEFIEKDIPF LRQYNTKIIV NIAGRTIEDY CEVVKKLGDA
     DVDLLELNIS CPNVKAGGVC FGTDPFMVEE VTKAVKKVAK QPLIVKLTPN VTDIVPIAKA
     AVAGGADGIS LINTLLGMAI DIHKRKPILA NVMGGFSGPA IKPVALRMVY QVANAVDVPI
     IGMGGIMTGE DAVEFILAGA SGVAVGTANF INPRATIDVI EGIQGYMEQY SIKDLKEIRG
     SL
//