PYRDB_ENTFO
ID PYRDB_ENTFO Reviewed; 312 AA.
AC F2MMN9; Q47741;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit;
DE Short=DHOD B;
DE Short=DHODase B;
DE Short=DHOdehase B;
DE EC=1.3.1.14;
DE AltName: Full=Dihydroorotate oxidase B;
DE AltName: Full=Orotate reductase (NADH);
GN Name=pyrDB; Synonyms=pyrD, pyrD-2; OrderedLocusNames=OG1RF_11425;
OS Enterococcus faecalis (strain ATCC 47077 / OG1RF).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=474186;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 47077 / OG1RF;
RX PubMed=7592480; DOI=10.1128/jb.177.23.6866-6873.1995;
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=ATCC 47077 / OG1RF;
RX PubMed=18611278; DOI=10.1186/gb-2008-9-7-r110;
RA Bourgogne A., Garsin D.A., Qin X., Singh K.V., Sillanpaa J.,
RA Yerrapragada S., Ding Y., Dugan-Rocha S., Buhay C., Shen H., Chen G.,
RA Williams G., Muzny D., Maadani A., Fox K.A., Gioia J., Chen L., Shang Y.,
RA Arias C.A., Nallapareddy S.R., Zhao M., Prakash V.P., Chowdhury S.,
RA Jiang H., Gibbs R.A., Murray B.E., Highlander S.K., Weinstock G.M.;
RT "Large scale variation in Enterococcus faecalis illustrated by the genome
RT analysis of strain OG1RF.";
RL Genome Biol. 9:R110.1-R110.16(2008).
CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with
CC NAD(+) as electron acceptor. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate;
CC Xref=Rhea:RHEA:13513, ChEBI:CHEBI:15378, ChEBI:CHEBI:30839,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.14;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 1 FMN per subunit. {ECO:0000250};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
CC -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; U24692; AAA67066.1; -; Genomic_DNA.
DR EMBL; CP002621; AEA94112.1; -; Genomic_DNA.
DR RefSeq; WP_002379493.1; NZ_CP025020.1.
DR AlphaFoldDB; F2MMN9; -.
DR SMR; F2MMN9; -.
DR GeneID; 60894010; -.
DR KEGG; efi:OG1RF_11425; -.
DR HOGENOM; CLU_042042_0_0_9; -.
DR OMA; SCPHAKG; -.
DR UniPathway; UPA00070; UER00945.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004589; F:orotate reductase (NADH) activity; IEA:UniProtKB-EC.
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 CDD; cd04740; DHOD_1B_like; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00224; DHO_dh_type1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR033888; DHOD_1B.
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 Cytoplasm; Flavoprotein; FMN; NAD; Oxidoreductase; Pyrimidine biosynthesis.
FT CHAIN 1..312
FT /note="Dihydroorotate dehydrogenase B (NAD(+)), catalytic
FT subunit"
FT /id="PRO_0000412178"
FT ACT_SITE 133
FT /note="Nucleophile"
FT BINDING 23
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 47..48
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 71..75
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 195..196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 246..247
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 268..269
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
SQ SEQUENCE 312 AA; 33079 MW; 44DA8C6F2F56192B CRC64;
MMKNPLAVSI PGLTLKNPII PASGCFGFGE EYANYYDLDQ LGSIMIKATT PQARYGNPTP
RVAETPSGML NAIGLQNPGL DVVMQEKLPK LEKYPNLPII ANVAGACEED YVAVCAKIGQ
APNVKAIELN ISCPNVKHGG IAFGTDPEVA FQLTQAVKKV ASVPIYVKLS PNVTDIVPIA
QAIEAGGADG FSMINTLLGM RIDLKTRKPI LANQTGGLSG PAIKPVAIRL IRQVASVSQL
PIIGMGGVQT VDDVLEMFMA GASAVGVGTA NFTDPYICPK LIDGLPKRME ELGIESLEQL
IKEVREGQQN AR
