ID   D8RAG3_SELML            Unreviewed;       464 AA.
AC   D8RAG3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Dihydroorotate dehydrogenase (quinone), mitochondrial {ECO:0000256|ARBA:ARBA00017599, ECO:0000256|RuleBase:RU361255};
DE            Short=DHOdehase {ECO:0000256|RuleBase:RU361255};
DE            EC=1.3.5.2 {ECO:0000256|ARBA:ARBA00012791, ECO:0000256|RuleBase:RU361255};
GN   ORFNames=SELMODRAFT_440247 {ECO:0000313|EMBL:EFJ30613.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ30613.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate;
CC         Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839,
CC         ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001532,
CC         ECO:0000256|RuleBase:RU361255};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|RuleBase:RU361255};
CC       Note=Binds 1 FMN per subunit. {ECO:0000256|RuleBase:RU361255};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       orotate from (S)-dihydroorotate (quinone route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005161, ECO:0000256|RuleBase:RU361255}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU361255}; Single-pass membrane protein
CC       {ECO:0000256|RuleBase:RU361255}.
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 2
CC       subfamily. {ECO:0000256|ARBA:ARBA00005359,
CC       ECO:0000256|RuleBase:RU361255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL377575; EFJ30613.1; -; Genomic_DNA.
DR   RefSeq; XP_002968359.1; XM_002968313.1.
DR   AlphaFoldDB; D8RAG3; -.
DR   STRING; 88036.D8RAG3; -.
DR   EnsemblPlants; EFJ30613; EFJ30613; SELMODRAFT_440247.
DR   GeneID; 9631151; -.
DR   Gramene; EFJ30613; EFJ30613; SELMODRAFT_440247.
DR   KEGG; smo:SELMODRAFT_440247; -.
DR   eggNOG; KOG1436; Eukaryota.
DR   HOGENOM; CLU_013640_0_0_1; -.
DR   InParanoid; D8RAG3; -.
DR   OMA; IYGTDTR; -.
DR   OrthoDB; 313431at2759; -.
DR   UniPathway; UPA00070; UER00946.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0106430; F:dihydroorotate dehydrogenase (quinone) 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-UniPathway.
DR   GO; GO:0009220; P:pyrimidine ribonucleotide biosynthetic process; IBA:GO_Central.
DR   CDD; cd04738; DHOD_2_like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005719; Dihydroorotate_DH_2.
DR   InterPro; IPR005720; Dihydroorotate_DH_cat.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   NCBIfam; TIGR01036; pyrD_sub2; 1.
DR   PANTHER; PTHR48109:SF4; DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48109; DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF01180; DHO_dh; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS00911; DHODEHASE_1; 1.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361255};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|RuleBase:RU361255};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|RuleBase:RU361255};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU361255};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361255};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT   DOMAIN          127..447
FT                   /note="Dihydroorotate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01180"
SQ   SEQUENCE   464 AA;  49511 MW;  E1574FF94CF98AF5 CRC64;
     MREGRLLAAI ARRFAYGSSS CIHTAAETSG SAKEAVAAAF QKPPLPPKIR LTWGRVLTGT
     LLGAVIAGGA YVGTRDEATI SAWTFEAAKY INPLFRLLDP ENAHKVAIWA SSHCLCPRET
     RPDPPVLEVS VWGRTFSNPV GLAAGFDKNA EAVEGLLGIG FGFMEVGSVT PVPQEGNPKP
     RVFRLPEQGA IINRYGFNSE GIVAVAKRLG AQHGKRRMAE TVNSAITTNT EQRVLGGKAG
     PGILGVNLGK NKTSEDAAAD YVQGVHTLSQ YADYLVINVS SPNTPGLRKL QGRKQLKDLI
     KKVLAARDEM QWGEEGPPPL LVKIAPDLSK QDLADIAAVA LSLRLDGLII ANTTVSRPDS
     VIGLVHADEM GGLSGKPLFT LSTEVLREMY QLTWGKIPLV GCGGISSGEE AYVKIRAGAT
     LVQLYTTFAY EGPALIPRIK AELAACLERD GFKSAQEAIG ADHR
//