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PYRK_STRMU
ID   PYRK_STRMU              Reviewed;         258 AA.
AC   Q8DTU9;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit {ECO:0000255|HAMAP-Rule:MF_01211};
DE   AltName: Full=Dihydroorotate oxidase B, electron transfer subunit {ECO:0000255|HAMAP-Rule:MF_01211};
GN   Name=pyrK {ECO:0000255|HAMAP-Rule:MF_01211}; OrderedLocusNames=SMU_1224;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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:0000255|HAMAP-
CC       Rule:MF_01211}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01211};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01211};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01211};
CC       Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01211};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01211}.
CC   -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_01211}.
CC   -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000255|HAMAP-
CC       Rule:MF_01211}.
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DR   EMBL; AE014133; AAN58909.1; -; Genomic_DNA.
DR   RefSeq; NP_721603.1; NC_004350.2.
DR   RefSeq; WP_002263218.1; NC_004350.2.
DR   AlphaFoldDB; Q8DTU9; -.
DR   SMR; Q8DTU9; -.
DR   STRING; 210007.SMU_1224; -.
DR   PRIDE; Q8DTU9; -.
DR   EnsemblBacteria; AAN58909; AAN58909; SMU_1224.
DR   KEGG; smu:SMU_1224; -.
DR   PATRIC; fig|210007.7.peg.1097; -.
DR   eggNOG; COG0543; Bacteria.
DR   HOGENOM; CLU_003827_1_2_9; -.
DR   OMA; RYMKCGI; -.
DR   PhylomeDB; Q8DTU9; -.
DR   UniPathway; UPA00070; UER00945.
DR   Proteomes; UP000002512; 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; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR000951; Ph_dOase_redase.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
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; Reference proteome; Transport.
FT   CHAIN           1..258
FT                   /note="Dihydroorotate dehydrogenase B (NAD(+)), electron
FT                   transfer subunit"
FT                   /id="PRO_0000148367"
FT   DOMAIN          2..100
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         51..54
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         68..70
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         75..76
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         220
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         225
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         228
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         244
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
SQ   SEQUENCE   258 AA;  28030 MW;  5A83D32B5D3481EA CRC64;
     MILKENLTVV SQREIAPRIF EMVLKGDMVA QMQAGQFLHI RVPDASKLLR RPISIADINK
     EAQEATIIYR IEGRGTAIFS QLKAGDKLDC LGPQGNGFDL SVIDKGQKAL IIGGGIGVPP
     LLEVAKQLCK KGVEAYAVLG FANKDAVILE EKMSQYATVV VTTDDGSYGQ KGYVSTVVDN
     LDFLADAIYA CGAPGMLKYV DKKFEKHPHA YLSTEERMAC GMGACYACVV HVKGQEDAQN
     LRVCEDGPIF ETGQIILD
 
 
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