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PYRDB_BACC2
ID   PYRDB_BACC2             Reviewed;         309 AA.
AC   B7IUP4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=pyrD; OrderedLocusNames=BCG9842_B1259;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001186; ACK93607.1; -; Genomic_DNA.
DR   RefSeq; WP_001081049.1; NC_011772.1.
DR   AlphaFoldDB; B7IUP4; -.
DR   SMR; B7IUP4; -.
DR   EnsemblBacteria; ACK93607; ACK93607; BCG9842_B1259.
DR   GeneID; 67508518; -.
DR   KEGG; bcg:BCG9842_B1259; -.
DR   HOGENOM; CLU_042042_0_0_9; -.
DR   OMA; SCPHAKG; -.
DR   UniPathway; UPA00070; UER00945.
DR   Proteomes; UP000006744; Chromosome.
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..309
FT                   /note="Dihydroorotate dehydrogenase B (NAD(+)), catalytic
FT                   subunit"
FT                   /id="PRO_1000195045"
FT   ACT_SITE        130
FT                   /note="Nucleophile"
FT   BINDING         21
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         45..46
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         69..73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         192..193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         243..244
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         265..266
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   309 AA;  32976 MW;  F33935CDD1C39E99 CRC64;
     MNRLQVELPG LSLKNPIIPA SGCFGFGREY AQFYDLSVLG SIMIKATTEQ PRYGNPTPRV
     AETPGGMLNA IGLQNPGLDK VMNSELPWLE QFDLPIIANV AGSQAEDYVA VAKEISKAPN
     VHALELNISC PNVKTGGIAF GTNPEIAADL TKRVKEVSEV PVYVKLSPNV ANIVEIAKAI
     ENAGADGLTM INTLLGMRLD LKTAKPILAN RTGGLSGPAI KPVAIRMVHE VSQAVNIPII
     GMGGIETAED VIEFFYAGAS AVAVGTANFI DPFVCPTIIE ELPALLDELG FDHISECQGR
     SWKQTCHSR
 
 
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