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PYRDB_CALBD
ID   PYRDB_CALBD             Reviewed;         300 AA.
AC   B9MS26;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-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=Athe_1380;
OS   Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
OS   (Anaerocellum thermophilum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX   NCBI_TaxID=521460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kataeva I., Adams M.W.W.;
RT   "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725.";
RL   Submitted (JAN-2009) 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; CP001393; ACM60480.1; -; Genomic_DNA.
DR   RefSeq; WP_015907849.1; NC_012034.1.
DR   AlphaFoldDB; B9MS26; -.
DR   SMR; B9MS26; -.
DR   STRING; 521460.Athe_1380; -.
DR   EnsemblBacteria; ACM60480; ACM60480; Athe_1380.
DR   GeneID; 31772727; -.
DR   KEGG; ate:Athe_1380; -.
DR   eggNOG; COG0167; Bacteria.
DR   HOGENOM; CLU_042042_0_0_9; -.
DR   OMA; ERIKMGA; -.
DR   OrthoDB; 1109542at2; -.
DR   UniPathway; UPA00070; UER00945.
DR   Proteomes; UP000007723; 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..300
FT                   /note="Dihydroorotate dehydrogenase B (NAD(+)), catalytic
FT                   subunit"
FT                   /id="PRO_1000195037"
FT   ACT_SITE        127
FT                   /note="Nucleophile"
FT   BINDING         20
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         44..45
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         68..72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         189..190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         240..241
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         262..263
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   300 AA;  32393 MW;  BF8351295FC957EB CRC64;
     MNLEVEIAGI KLKNPVIAAS GTFGFGREYS KLIDISEFGA ICTKGITLKK RIGNPQPRLC
     EVYAGIINSV GLENPGVEAF INDELPFLKS FDTKIIANIN GFSKEEFVEL TKILTSLVDM
     IEVNLSCPNV KEGGMVFGKD PKKVYEITKS VKDVASCPII VKLTPNVTDI TQLAVAAENA
     GADAISLINT VSAMAIDIET RKPLIKMVTG GLSGPAIKPI AVRMVYECFK KVRIPIIGMG
     GIMNYKDAIE FFIAGATAIQ IGTVNFINPK AVCEIKEGIE AYLERKGFKS IKELVGSINI
 
 
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