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PYRDB_ALKHC
ID   PYRDB_ALKHC             Reviewed;         305 AA.
AC   Q9K9W1;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 130.
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=BH2534;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB06253.1; -; Genomic_DNA.
DR   PIR; F83966; F83966.
DR   RefSeq; WP_010898685.1; NC_002570.2.
DR   AlphaFoldDB; Q9K9W1; -.
DR   SMR; Q9K9W1; -.
DR   STRING; 272558.10175154; -.
DR   EnsemblBacteria; BAB06253; BAB06253; BAB06253.
DR   KEGG; bha:BH2534; -.
DR   eggNOG; COG0167; Bacteria.
DR   HOGENOM; CLU_042042_0_0_9; -.
DR   OMA; SCPHAKG; -.
DR   OrthoDB; 1109542at2; -.
DR   UniPathway; UPA00070; UER00945.
DR   Proteomes; UP000001258; 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;
KW   Reference proteome.
FT   CHAIN           1..305
FT                   /note="Dihydroorotate dehydrogenase B (NAD(+)), catalytic
FT                   subunit"
FT                   /id="PRO_0000148388"
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   305 AA;  32133 MW;  726B468AA5ECD726 CRC64;
     MSRLAVELPG LSMKNPIMPA SGCFGFGKEF AGFYDLNHLG AIAIKATTVE PRFGNPTPRV
     AETHSGMLNA IGLQNPGLNN VIDNELARLA DVDVPIVANI AGSTVNDYVE VAEAISRVDN
     VHALELNISC PNVKEGGIAF GTVPDVAAQL TQEVKRVSTV PVYVKLSPNV SDIVEMAQAV
     ERAGADGLSM INTLLGMRLD LKRRTPILAN GTGGLSGPAI KPVAIRMIYQ VSQAVSIPII
     GMGGIQSADD VLEFMLAGAD AVAVGTANFT DPYVCPTIID ELPKRMDELG IERIADIVGG
     SWKQS
 
 
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