ID   1.3.1.14
DE   Dihydroorotate dehydrogenase (NAD(+)).
AN   DHOD.
AN   DHODase.
AN   DHOdehase.
AN   Dihydroorotate oxidase.
AN   Orotate reductase (NADH(2)).
AN   Orotate reductase (NADH).
CA   (S)-dihydroorotate + NAD(+) = orotate + NADH.
CF   FAD; FMN; Iron-sulfur.
CC   -!- The enzyme consists of two subunits, an FMN binding catalytic subunit
CC       and a FAD and iron-sulfur binding electron transfer subunit.
CC   -!- The reaction, which takes place in the cytosol, is the only redox
CC       reaction in the de-novo biosynthesis of pyrimidine nucleotides.
CC   -!- Other class 1 dihydroorotate dehydrogenases use either fumarate
CC       (EC 1.3.98.1) or NADP(+) (EC 1.3.1.15) as electron acceptor.
CC   -!- The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2)
CC       uses quinone as electron acceptor.
DR   Q9K9W1, PYRDB_ALKHC;  A6TVS0, PYRDB_ALKMQ;  A8MIU4, PYRDB_ALKOO;
DR   B7GFA1, PYRDB_ANOFW;  O29513, PYRDB_ARCFU;  B6YRL9, PYRDB_AZOPC;
DR   C3P654, PYRDB_BACAA;  C3L742, PYRDB_BACAC;  A0RHQ6, PYRDB_BACAH;
DR   Q81WF4, PYRDB_BACAN;  B7JJX1, PYRDB_BACC0;  Q732I5, PYRDB_BACC1;
DR   B7IUP4, PYRDB_BACC2;  C1EPP8, PYRDB_BACC3;  B7H6M0, PYRDB_BACC4;
DR   B7HLL8, PYRDB_BACC7;  P46539, PYRDB_BACCL;  A7GRK9, PYRDB_BACCN;
DR   B9IVW1, PYRDB_BACCQ;  Q819S5, PYRDB_BACCR;  Q636E2, PYRDB_BACCZ;
DR   Q5LCI2, PYRDB_BACFN;  Q64TN0, PYRDB_BACFR;  Q6HET0, PYRDB_BACHK;
DR   A9VTC4, PYRDB_BACMK;  A8FD19, PYRDB_BACP2;  Q5WFJ4, PYRDB_BACSK;
DR   P25996, PYRDB_BACSU;  Q8A9C3, PYRDB_BACTN;  A7Z4H4, PYRDB_BACVZ;
DR   C0QYH6, PYRDB_BRAHW;  B9MS26, PYRDB_CALBD;  Q8R9R7, PYRDB_CALS4;
DR   A4XKT6, PYRDB_CALS8;  Q3AC05, PYRDB_CARHZ;  B5EFU4, PYRDB_CITBB;
DR   Q18CS6, PYRDB_CLOD6;  Q6A912, PYRDB_CUTAK;  B1I4M6, PYRDB_DESAP;
DR   C4XPD6, PYRDB_DESMR;  A4J560, PYRDB_DESRM;  B1GYY3, PYRDB_ENDTX;
DR   P0DH74, PYRDB_ENTFA;  F2MMN9, PYRDB_ENTFO;  B1YIR7, PYRDB_EXIS2;
DR   Q8RG85, PYRDB_FUSNN;  B9M211, PYRDB_GEODF;  Q5L0U1, PYRDB_GEOKA;
DR   B3E4T4, PYRDB_GEOLS;  Q39UK4, PYRDB_GEOMG;  Q74CB9, PYRDB_GEOSL;
DR   C6E6N2, PYRDB_GEOSM;  C5D8Q2, PYRDB_GEOSW;  A4IM35, PYRDB_GEOTN;
DR   A5G3H0, PYRDB_GEOUR;  B0TGQ8, PYRDB_HELMI;  Q9CFW8, PYRDB_LACLA;
DR   P54322, PYRDB_LACLM;  A9KKR5, PYRDB_LACP7;  Q38X22, PYRDB_LATSS;
DR   Q92AH5, PYRDB_LISIN;  C1KWD2, PYRDB_LISMC;  Q71YI3, PYRDB_LISMF;
DR   B8DDR9, PYRDB_LISMH;  Q8Y667, PYRDB_LISMO;  A0AJT8, PYRDB_LISW6;
DR   C6BW12, PYRDB_MARSD;  Q8TT55, PYRDB_METAC;  Q0W8E1, PYRDB_METAR;
DR   Q58070, PYRDB_METJA;  Q8TXU6, PYRDB_METKA;  Q8PW56, PYRDB_METMA;
DR   O27281, PYRDB_METTH;  Q8EUY2, PYRDB_MYCPE;  B2A2U4, PYRDB_NATTJ;
DR   Q8CWG1, PYRDB_OCEIH;  A6LB11, PYRDB_PARD8;  A1ASB3, PYRDB_PELPD;
DR   A9BJH4, PYRDB_PETMO;  A6L5H1, PYRDB_PHOV8;  Q7MVJ6, PYRDB_PORGI;
DR   Q9V0Y6, PYRDB_PYRAB;  Q8U0P6, PYRDB_PYRFU;  O59185, PYRDB_PYRHO;
DR   Q9UX04, PYRDB_SACS2;  B9DPN4, PYRDB_STACT;  Q97R65, PYRDB_STRPN;
DR   Q8DQ37, PYRDB_STRR6;  O08358, PYRDB_SULAC;  Q0AXG6, PYRDB_SYNWW;
DR   Q9HL35, PYRDB_THEAC;  Q5JHR7, PYRDB_THEKO;  Q9WYG8, PYRDB_THEMA;
DR   A5IK84, PYRDB_THEP1;  B0KA32, PYRDB_THEP3;  B0K2E5, PYRDB_THEPX;
DR   Q979G6, PYRDB_THEVO;  B5YJH1, PYRDB_THEYD;
//