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Database: UniProt
Entry: Q9CFC9
LinkDB: Q9CFC9
Original site: Q9CFC9 
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   03-SEP-2014, entry version 100.
DE   RecName: Full=Dihydroorotate dehydrogenase A (fumarate);
DE            Short=DHOD A;
DE            Short=DHODase A;
DE            Short=DHOdehase A;
DE            EC=1.3.98.1;
GN   Name=pyrDA; Synonyms=pydA; OrderedLocusNames=LL1552; ORFNames=L192589;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus
OS   lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   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   -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate
CC       with fumarate as the electron acceptor (By similarity).
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + fumarate = orotate +
CC       succinate.
CC   -!- COFACTOR: Binds 1 FMN per subunit (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway.
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; AE005176; AAK05650.1; -; Genomic_DNA.
DR   PIR; H86818; H86818.
DR   RefSeq; NP_267708.1; NC_002662.1.
DR   ProteinModelPortal; Q9CFC9; -.
DR   SMR; Q9CFC9; 1-311.
DR   STRING; 272623.L192589; -.
DR   EnsemblBacteria; AAK05650; AAK05650; L192589.
DR   GeneID; 1115211; -.
DR   KEGG; lla:L192589; -.
DR   PATRIC; 22295518; VBILacLac136773_1666.
DR   eggNOG; COG0167; -.
DR   HOGENOM; HOG000225104; -.
DR   KO; K00226; -.
DR   OMA; DFDNCLM; -.
DR   OrthoDB; EOG6NPM9S; -.
DR   BioCyc; LLAC272623:GHSH-1651-MONOMER; -.
DR   SABIO-RK; Q9CFC9; -.
DR   UniPathway; UPA00070; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00224; DHO_dh_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005720; Dihydroorotate_DH.
DR   InterPro; IPR024920; Dihydroorotate_DH_1.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
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; Reference proteome.
FT   CHAIN         1    311       Dihydroorotate dehydrogenase A
FT                                (fumarate).
FT                                /FTId=PRO_0000148393.
FT   NP_BIND      43     44       FMN (By similarity).
FT   NP_BIND     249    250       FMN (By similarity).
FT   NP_BIND     271    272       FMN (By similarity).
FT   REGION       67     71       Substrate binding (By similarity).
FT   REGION      193    194       Substrate binding (By similarity).
FT   ACT_SITE    130    130       Nucleophile.
FT   BINDING      19     19       FMN (By similarity).
FT   BINDING      43     43       Substrate (By similarity).
FT   BINDING     127    127       FMN (By similarity).
FT   BINDING     127    127       Substrate (By similarity).
FT   BINDING     164    164       FMN (By similarity).
FT   BINDING     192    192       FMN; via carbonyl oxygen (By similarity).
FT   BINDING     221    221       FMN; via amide nitrogen (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
//
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