ID   B3RIP0_TRIAD            Unreviewed;       394 AA.
AC   B3RIP0;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 82.
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=TRIADDRAFT_20390 {ECO:0000313|EMBL:EDV29753.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV29753.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV29753.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV29753.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + a quinone = orotate + a quinol;
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:ARBA00048639,
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|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU361255}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004434,
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}.
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DR   EMBL; DS985241; EDV29753.1; -; Genomic_DNA.
DR   RefSeq; XP_002108955.1; XM_002108919.1.
DR   AlphaFoldDB; B3RIP0; -.
DR   FunCoup; B3RIP0; 890.
DR   STRING; 10228.B3RIP0; -.
DR   GeneID; 6750169; -.
DR   KEGG; tad:TRIADDRAFT_20390; -.
DR   CTD; 6750169; -.
DR   eggNOG; KOG1436; Eukaryota.
DR   HOGENOM; CLU_013640_0_0_1; -.
DR   InParanoid; B3RIP0; -.
DR   OMA; ERIKMGA; -.
DR   OrthoDB; 14784at2759; -.
DR   PhylomeDB; B3RIP0; -.
DR   UniPathway; UPA00070; UER00946.
DR   Proteomes; UP000009022; 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: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   CDD; cd04738; DHOD_2_like; 1.
DR   FunFam; 3.20.20.70:FF:000066; Dihydroorotate dehydrogenase (quinone), mitochondrial; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR050074; DHO_dehydrogenase.
DR   InterPro; IPR005719; Dihydroorotate_DH_2.
DR   InterPro; IPR005720; Dihydroorotate_DH_cat.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   NCBIfam; NF003645; PRK05286.1-2; 1.
DR   NCBIfam; NF003652; PRK05286.2-5; 1.
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|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU361255};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW   ECO:0000256|RuleBase:RU361255};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361255};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          77..374
FT                   /note="Dihydroorotate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01180"
SQ   SEQUENCE   394 AA;  43335 MW;  563C8702B4537C41 CRC64;
     MQIRNLWKLV GGVAFASVAV SGLIVSQKLL RNDEVFYRTF ALPLLHRLDP ETAHRLAIKC
     ASLGLVPRQS TEDPAELVTT VFKQKFSNPI GLAAGFDKHA EAINDLLQMG FGFIEIGSVT
     PLPQAGNPKP RIFRLIEDRA IINRYGFNSD GHEIVAQKLE KWHKNRGREN SSGIVGINLG
     KNKLSDSAVE DYVKGIQAIG KYADYLVINV SSPNTPGLRA LQKKEELQTI ITQISIEREK
     LKNKPALLIK LAPDLTVQDK KDIADVILKE RRNVDGLVIS NTTVRRPNCL TSVSKSEAGG
     LSGPPLREMA TKTIYDMYRL TEGKIPIIGV GGVQSGEDAY EKIRAGASLI QVLTALTYNG
     PSIIQKIKAD LVTLLRQDGF KSVEEAVGID HRRQ
//