ID   PYRK_ENTFO              Reviewed;         263 AA.
AC   F2MMP0; P56967;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit;
DE   AltName: Full=Dihydroorotate oxidase B, electron transfer subunit;
GN   Name=pyrK; Synonyms=pyrDII; OrderedLocusNames=OG1RF_11426;
OS   Enterococcus faecalis (strain ATCC 47077 / OG1RF).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=474186;
RN   [1]
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 189-263.
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).
CC   -!- FUNCTION: Responsible for channeling the electrons from the oxidation
CC       of dihydroorotate from the FMN redox center in the PyrD type B subunit
CC       to the ultimate electron acceptor NAD(+). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD 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   -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000305}.
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DR   EMBL; CP002621; AEA94113.1; -; Genomic_DNA.
DR   EMBL; U24692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_002380354.1; NZ_CP025020.1.
DR   AlphaFoldDB; F2MMP0; -.
DR   SMR; F2MMP0; -.
DR   KEGG; efi:OG1RF_11426; -.
DR   HOGENOM; CLU_003827_1_2_9; -.
DR   OMA; RYMKCGI; -.
DR   UniPathway; UPA00070; UER00945.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.10.240.10; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
DR   HAMAP; MF_01211; DHODB_Fe_S_bind; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR   InterPro; IPR037117; Dihydroorotate_DH_ele_sf.
DR   InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR   InterPro; IPR023455; Dihydroorotate_DHASE_ETsu.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur;
KW   Metal-binding; Pyrimidine biosynthesis; Transport.
FT   CHAIN           1..263
FT                   /note="Dihydroorotate dehydrogenase B (NAD(+)), electron
FT                   transfer subunit"
FT                   /id="PRO_0000412180"
FT   DOMAIN          3..102
FT                   /note="FAD-binding FR-type"
FT   BINDING         53..56
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         70..72
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         77..78
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   263 AA;  28558 MW;  A28DFEC0CA43F91B CRC64;
     MQRKQEMMTI VAQKQLAPRI YQLDLQGELV KDMTRPGQFV HIKVPRADLL LRRPISINQI
     DHSNETCRLI YRVEGAGTEV FATMKAGEQL DILGPLGNGF DITTVAAGQT AFIVGGGIGI
     PPLYELSKQL NEKGVKVIHF LGYASKEVAY YQQEFMALGE THFATDDGSF GAHGNVGRLL
     SEALAKGRIP DAVYACGANG MLKAIDSLFP THPHVYLSLE ERMACGIGAC YACVCHKKGD
     TTGAKSVKVC DEGPIFKASE VIL