ID PYRDB_ENTFA Reviewed; 312 AA. AC Q47741; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-APR-2003, sequence version 2. DT 25-NOV-2008, entry version 69. 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=pyrD, pyrD-2; OrderedLocusNames=EF_1714; OS Enterococcus faecalis (Streptococcus faecalis). OC Bacteria; Firmicutes; Lactobacillales; Enterococcaceae; Enterococcus. OX NCBI_TaxID=1351; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 47077 / OG1RF; RX MEDLINE=96074317; PubMed=7592480; RA Li X., Weinstock G.M., Murray B.E.; RT "Generation of auxotrophic mutants of Enterococcus faecalis."; RL J. Bacteriol. 177:6866-6873(1995). RN [2] 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). RN [3] RP CHARACTERIZATION. RC STRAIN=ATCC 29212 / DSM 2570; RX MEDLINE=99459259; PubMed=10529184; DOI=10.1021/bi990674q; RA Marcinkeviciene J., Tinney L.M., Wang K.H., Rogers M.J., RA Copeland R.A.; RT "Dihydroorotate dehydrogenase B of Enterococcus faecalis. RT Characterization and insights into chemical mechanism."; RL Biochemistry 38:13129-13137(1999). CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + O(2) = orotate + CC H(2)O(2). CC -!- COFACTOR: Binds 1 FMN per subunit. 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; U24692; AAA67066.1; -; Genomic_DNA. DR EMBL; AE016830; AAO81490.1; -; Genomic_DNA. DR RefSeq; NP_815420.1; -. DR HSSP; P54322; 1EP2. DR SMR; Q47741; 4-309. DR GeneID; 1200606; -. DR GenomeReviews; AE016830_GR; EF_1714. DR KEGG; efa:EF1714; -. DR NMPDR; fig|226185.1.peg.1605; -. DR TIGR; EF_1714; -. DR HOGENOM; Q47741; -. DR BioCyc; EFAE226185:EF_1714-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; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Flavoprotein; FMN; Oxidoreductase; KW Pyrimidine biosynthesis. FT CHAIN 1 312 Dihydroorotate dehydrogenase B, catalytic FT subunit. FT /FTId=PRO_0000148391. FT ACT_SITE 133 133 Nucleophile (By similarity). FT CONFLICT 81 81 E -> D (in Ref. 1; AAA67066). SQ SEQUENCE 312 AA; 33093 MW; B97956521B85541F CRC64; MMKNPLAVSI PGLTLKNPII PASGCFGFGE EYANYYDLDQ LGSIMIKATT PQARYGNPTP RVAETPSGML NAIGLQNPGL EVVMQEKLPK LEKYPNLPII ANVAGACEED YVAVCAKIGQ APNVKAIELN ISCPNVKHGG IAFGTDPEVA FQLTQAVKKV ASVPIYVKLS PNVTDIVPIA QAIEAGGADG FSMINTLLGM RIDLKTRKPI LANQTGGLSG PAIKPVAIRL IRQVASVSQL PIIGMGGVQT VDDVLEMFMA GASAVGVGTA NFTDPYICPK LIDGLPKRME ELGIESLEQL IKEVREGQQN AR //