ID   PYRDB_SACS2             Reviewed;         290 AA.
AC   Q9UX04;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   28-JAN-2026, entry version 148.
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=SSO0610; ORFNames=C08_040;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=10701121; DOI=10.1139/g99-108;
RA   Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA   Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA   Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA   Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA   Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT   "Gene content and organization of a 281-kbp contig from the genome of the
RT   extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL   Genome 43:116-136(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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(+) = orotate + NADH + H(+);
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; Y18930; CAB57690.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK40921.1; -; Genomic_DNA.
DR   PIR; B90208; B90208.
DR   RefSeq; WP_009991136.1; NC_002754.1.
DR   AlphaFoldDB; Q9UX04; -.
DR   SMR; Q9UX04; -.
DR   FunCoup; Q9UX04; 117.
DR   STRING; 273057.SSO0610; -.
DR   PaxDb; 273057-SSO0610; -.
DR   EnsemblBacteria; AAK40921; AAK40921; SSO0610.
DR   GeneID; 1454888; -.
DR   GeneID; 44129612; -.
DR   KEGG; sso:SSO0610; -.
DR   PATRIC; fig|273057.12.peg.618; -.
DR   eggNOG; arCOG00603; Archaea.
DR   HOGENOM; CLU_042042_0_1_2; -.
DR   InParanoid; Q9UX04; -.
DR   PhylomeDB; Q9UX04; -.
DR   UniPathway; UPA00070; UER00945.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004589; F:dihydroorotate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04740; DHOD_1B_like; 1.
DR   FunFam; 3.20.20.70:FF:000027; Dihydropyrimidine dehydrogenase [NADP(+)]; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00224; DHO_dh_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR050074; DHO_dehydrogenase.
DR   InterPro; IPR033888; DHOD_1B.
DR   InterPro; IPR053488; DHODH_Type1.
DR   InterPro; IPR024920; Dihydroorotate_DH_1.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR005720; Dihydroorotate_DH_cat.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   NCBIfam; NF041011; dihydoor_dh_Arch; 1.
DR   PANTHER; PTHR48109:SF1; DIHYDROOROTATE DEHYDROGENASE (FUMARATE); 1.
DR   PANTHER; PTHR48109; DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF01180; DHO_dh; 1.
DR   PIRSF; PIRSF000164; DHO_oxidase; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 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..290
FT                   /note="Dihydroorotate dehydrogenase B (NAD(+)), catalytic
FT                   subunit"
FT                   /id="PRO_0000148417"
FT   ACT_SITE        120
FT                   /note="Nucleophile"
FT   BINDING         17
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         42..43
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         67..71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         178..179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         229..230
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         251..252
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   290 AA;  31154 MW;  65AA1512509A78CC CRC64;
     MITIKNITLN DPLIIASGII PDVPNYVETI CEKYKPSAIT TKTVTLNPLE PHKPPTVIKL
     HDGIYMNAIG LGNPGAKAIN EIGVLCPLIV SVGGSSINEI KEVVEVVQSK AKIIEINVSS
     PNRKGYGESL SKLIGDIIES VKSVTKLPVF VKLGPWDNVI ELAGKALEKG ADGLTLINTI
     KGLIIDVETF KPILYYGTGG VSGRCLYPIA LRIIKDVYEE YGVDIIGVGG VYDWTDVIGM
     LAAGAKLVGL GTVLIEKGFS VIEEIRKGLQ SYLLEKGLKF EDIIGISVRK
//