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PYRK_BACC7
ID   PYRK_BACC7              Reviewed;         259 AA.
AC   B7HLL9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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};
GN   OrderedLocusNames=BCAH187_A3934;
OS   Bacillus cereus (strain AH187).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH187;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA   Okstad O.A., Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH187.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001177; ACJ82336.1; -; Genomic_DNA.
DR   RefSeq; WP_000983358.1; NC_011658.1.
DR   AlphaFoldDB; B7HLL9; -.
DR   SMR; B7HLL9; -.
DR   EnsemblBacteria; ACJ82336; ACJ82336; BCAH187_A3934.
DR   GeneID; 59155614; -.
DR   KEGG; bcr:BCAH187_A3934; -.
DR   HOGENOM; CLU_003827_1_2_9; -.
DR   OMA; RYMKCGI; -.
DR   OrthoDB; 1885467at2; -.
DR   UniPathway; UPA00070; UER00945.
DR   Proteomes; UP000002214; 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; 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; 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; Transport.
FT   CHAIN           1..259
FT                   /note="Dihydroorotate dehydrogenase B (NAD(+)), electron
FT                   transfer subunit"
FT                   /id="PRO_1000138909"
FT   DOMAIN          2..102
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         53..56
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         70..72
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         77..78
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         221
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         226
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         229
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         246
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
SQ   SEQUENCE   259 AA;  28439 MW;  DC2768827E220805 CRC64;
     MMQKQNMIVV NQKEIAKNIY ELVLQGTLVQ QMNEPGQFVH IKVAEGIAPL LRRPISICNV
     DQEKNEFTML YRAEGQGTKT LATRKQGEMV DVLGPLGHGF PVEEAEAGQT ALLVGGGIGV
     PPLYELSQRL VAKGVRVIHI LGFQTKDVVF YEEKFAELGD TYVATVDGTH GTKGFVTDVI
     DHYGIDFDIL YSCGPLAMLR ALEGRYKEKK AYISLEERMG CGIGACFACV CHLQEDPSGH
     SYKKVCSDGP VFPIGEVVL
 
 
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