ID   PYRDA_ENTFA             Reviewed;         311 AA.
AC   P59626;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 1.
DT   25-NOV-2008, entry version 49.
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, pyrD-1; OrderedLocusNames=EF_0285;
OS   Enterococcus faecalis (Streptococcus faecalis).
OC   Bacteria; Firmicutes; Lactobacillales; Enterococcaceae; Enterococcus.
OX   NCBI_TaxID=1351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V583 / ATCC 700802;
RX   MEDLINE=22550857; PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F.,
RA   Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J.,
RA   Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A.,
RA   Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant
RT   Enterococcus faecalis.";
RL   Science 299:2071-2074(2003).
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; AE016830; AAO80148.1; -; Genomic_DNA.
DR   RefSeq; NP_814077.1; -.
DR   HSSP; P54321; 2DOR.
DR   GeneID; 1199203; -.
DR   GenomeReviews; AE016830_GR; EF_0285.
DR   KEGG; efa:EF0285; -.
DR   NMPDR; fig|226185.1.peg.263; -.
DR   TIGR; EF_0285; -.
DR   HOGENOM; P59626; -.
DR   BioCyc; EFAE226185:EF_0285-MON; -.
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; 1.
DR   PROSITE; PS00912; DHODEHASE_2; FALSE_NEG.
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_0000148390.
FT   ACT_SITE    130    130       Nucleophile (By similarity).
SQ   SEQUENCE   311 AA;  34477 MW;  A534C74755E914CD CRC64;
     MDISVEFSGH KLANVLMNAS GIHCMTIKEM DELAASQAGA FVAKTATPNP RQGNEEPRYF
     DTPLGSINSM GLPNLGIDYY LDYQIARQKE FPEELRFLSV SGMNYEENIA ILKKVQESEY
     TGVTEFNLSC PNLPGKPQIA YDFELTEKLL TEVFQFFTKP LGVKLPPFFD IAHFDAMAEI
     LNKFPLVYVN SINSIGNGLY IDSDKEEVVI KPKGGFGGLG GEYVKPTALA NVRAFAQRLK
     PEIKIIGTGG ITCGKDVFEH LLCGATLVQV GTQLHQEGPQ VFERLAKELQ EIMAAKGYES
     IEEFRGKLKE M
//