PYRK_ENTFA
ID PYRK_ENTFA Reviewed; 263 AA.
AC P0DH76; P56967;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 49.
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=EF_1715;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX 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., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 29212 / DSM 2570;
RX PubMed=10529184; DOI=10.1021/bi990674q;
RA Marcinkeviciene J., Tinney L.M., Wang K.H., Rogers M.J., Copeland R.A.;
RT "Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization
RT and insights into chemical mechanism.";
RL Biochemistry 38:13129-13137(1999).
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(+).
CC {ECO:0000269|PubMed:10529184}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:10529184};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000269|PubMed:10529184};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10529184};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10529184};
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:0000269|PubMed:10529184}.
CC -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000305}.
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DR EMBL; AE016830; AAO81491.1; -; Genomic_DNA.
DR RefSeq; NP_815421.1; NC_004668.1.
DR RefSeq; WP_002365731.1; NZ_KE136528.1.
DR AlphaFoldDB; P0DH76; -.
DR SMR; P0DH76; -.
DR STRING; 226185.EF_1715; -.
DR EnsemblBacteria; AAO81491; AAO81491; EF_1715.
DR GeneID; 60894011; -.
DR KEGG; efa:EF1715; -.
DR PATRIC; fig|226185.45.peg.1797; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_1_2_9; -.
DR OMA; RYMKCGI; -.
DR UniPathway; UPA00070; UER00945.
DR Proteomes; UP000001415; Chromosome.
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 1: Evidence at protein level;
KW 2Fe-2S; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; Pyrimidine biosynthesis; Reference proteome; Transport.
FT CHAIN 1..263
FT /note="Dihydroorotate dehydrogenase B (NAD(+)), electron
FT transfer subunit"
FT /id="PRO_0000148360"
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:0000305"
FT BINDING 230
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
FT BINDING 233
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
FT BINDING 250
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 28572 MW; 5F2E24FDFE90B42F CRC64;
MQRKQEMMTI VAQKQLAPRI YQLDLQGELV KEMTRPGQFV HIKVPRADLL LRRPISINQI
DHSNETCRLI YRVEGAGTEV FATMKAGEQL DILGPLGNGF DITTVAAGQT AFIVGGGIGI
PPLYELSKQL NEKGVKVIHF LGYASKEVAY YQQEFMALGE THFATDDGSF GAHGNVGRLL
SEALAKGRIP DAVYACGANG MLKAIDSLFP THPHVYLSLE ERMACGIGAC YACVCHKKGD
TTGAKSVKVC DEGPIFKASE VIL
