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PYRDB_ALKCK
ID   PYRDB_ALKCK             Reviewed;         304 AA.
AC   Q5WFJ4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=ABC2331;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) 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; AP006627; BAD64866.1; -; Genomic_DNA.
DR   RefSeq; WP_011247174.1; NC_006582.1.
DR   AlphaFoldDB; Q5WFJ4; -.
DR   SMR; Q5WFJ4; -.
DR   STRING; 66692.ABC2331; -.
DR   EnsemblBacteria; BAD64866; BAD64866; ABC2331.
DR   KEGG; bcl:ABC2331; -.
DR   eggNOG; COG0167; Bacteria.
DR   HOGENOM; CLU_042042_0_0_9; -.
DR   OMA; SCPHAKG; -.
DR   OrthoDB; 1109542at2; -.
DR   UniPathway; UPA00070; UER00945.
DR   Proteomes; UP000001168; 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..304
FT                   /note="Dihydroorotate dehydrogenase B (NAD(+)), catalytic
FT                   subunit"
FT                   /id="PRO_1000024130"
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   304 AA;  32447 MW;  795EFBE0FF5E488A CRC64;
     MERLQISLPG LEMKNPVMPA SGCFGFGKEY GQFFDLNQLG AIAIKATTKE ARFGNETPRV
     AETKAGMLNA IGLQNPGLQG VIEQELPRFD DYDVPILANI AGSTMDDYIE VAAELSQQRN
     VSAIELNISC PNVKQGGIAF GTVPEIAAEL TKEVKAVSAV PVYVKLSPNV ADIVAIAKAI
     EKAGADGLAM INTLLGMRID AKTRRPVLAN QYGGLSGAAI KPVALRMIHQ VSQQVDIPII
     GMGGIQTAED VIEFLLAGAS CIAVGTANFT DPYTCPNIIR DLPHWLDRLE VQSITDLIGG
     SWNE
 
 
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