ID   PYRDA_LACLA             Reviewed;         311 AA.
AC   Q9CFC9;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   04-NOV-2008, entry version 59.
DE   RecName: Full=Dihydroorotate dehydrogenase A;
DE            EC=1.3.3.1;
DE   AltName: Full=Dihydroorotate oxidase A;
DE   AltName: Full=DHOdehase A;
DE            Short=DHODase A;
DE            Short=DHOD A;
GN   Name=pyrDA; Synonyms=pydA; OrderedLocusNames=LL1552; ORFNames=L192589;
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   MEDLINE=21235186; PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K.,
RA   Weissenbach J., Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(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: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC       Type 1 subfamily.
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DR   EMBL; AE006386; AAK05650.1; -; Genomic_DNA.
DR   PIR; H86818; H86818.
DR   RefSeq; NP_267708.1; -.
DR   HSSP; P54321; 2DOR.
DR   SMR; Q9CFC9; 1-311.
DR   GeneID; 1115211; -.
DR   GenomeReviews; AE005176_GR; LL1552.
DR   KEGG; lla:L192589; -.
DR   NMPDR; fig|272623.1.peg.1594; -.
DR   HOGENOM; Q9CFC9; -.
DR   BioCyc; LLAC272623:L192589-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
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; 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    311       Dihydroorotate dehydrogenase A.
FT                                /FTId=PRO_0000148393.
FT   ACT_SITE    130    130       Nucleophile (By similarity).
SQ   SEQUENCE   311 AA;  34231 MW;  80B3619EC408BBA8 CRC64;
     MLKTTFANAE FANPFMNASG VHCMTTEDLE ELKASQAGAY ITKSSTLEKR EGNPLPRYVD
     LELGSINSMG LPNLGFDYYL DYVLKNQKEK AQEAPIFFSI AGMSAAENIA MLKKIQESNF
     SGITELNLSC PNVPGKPQLA YDFEATEKLL KEVFTFFTKP LGVKLPPYFD LVHFDIMAEI
     LNQFPLTYVN SVNSIGNGLF IDSEAESVVI KPKDGFGGIG GAYIKPTALA NVRAFYTRLK
     PEIKIIGTGG IETGQDAFEH LLCGATMLQI GTALHKEGPA IFDRIIKELE EIMDKKGYQS
     IADFHGKLKS L
//