ID   PYRDB_LACLA             Reviewed;         311 AA.
AC   Q9CFW8;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   04-NOV-2008, entry version 58.
DE   RecName: Full=Dihydroorotate dehydrogenase B, catalytic subunit;
DE            EC=1.3.3.1;
DE   AltName: Full=Dihydroorotate oxidase B;
DE   AltName: Full=DHOdehase B;
DE            Short=DHODase B;
DE            Short=DHOD B;
GN   Name=pyrDB; Synonyms=pydB; OrderedLocusNames=LL1346; ORFNames=L182555;
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: 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE006366; AAK05444.1; -; Genomic_DNA.
DR   PIR; B86793; B86793.
DR   RefSeq; NP_267502.1; -.
DR   HSSP; P54322; 1EP2.
DR   SMR; Q9CFW8; 1-311.
DR   GeneID; 1114996; -.
DR   GenomeReviews; AE005176_GR; LL1346.
DR   KEGG; lla:L182555; -.
DR   NMPDR; fig|272623.1.peg.1381; -.
DR   HOGENOM; Q9CFW8; -.
DR   BioCyc; LLAC272623:L182555-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 B, catalytic
FT                                subunit.
FT                                /FTId=PRO_0000148395.
FT   ACT_SITE    135    135       Nucleophile (By similarity).
SQ   SEQUENCE   311 AA;  32916 MW;  6FF419606B2E733C CRC64;
     MTENNRLSVK LPGLDLKNPI IPASGCFGFG EEYAKYYDLN KLGSIMVKAT TLHPRFGNPT
     PRVAETASGM LNAIGLQNPG LEVIMAEKLP WLNENFPDLP IIANVAGSEE DDYVAVCAKI
     GDAPNVKVIE LNISCPNVKH GGQAFGTDPD VAAALVKACK AVSKVPLYVK LSPNVTDIVP
     IAKAVEAAGA DGLTMINTLM GVRFDLKTRK PVLANITGGL SGPAIKPVAL KLIHQVAQVV
     DIPIIGMGGV ESAQDVLEMY MAGASAVAVG TANFADPFVC PKIIEKLPEV MDQYGIDSLE
     NLIQEVKNSK K
//