Entry
Name
dihydroorotate dehydrogenase (NAD+);
orotate reductase (NADH);
orotate reductase (NADH2);
DHOdehase (ambiguous);
DHOD (ambiguous);
DHODase (ambiguous);
dihydroorotate oxidase, pyrD (gene name)
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
(S)-dihydroorotate:NAD+ oxidoreductase
Reaction(IUBMB)
(S)-dihydroorotate + NAD+ = orotate + NADH + H+ [RN:
R01869 ]
Reaction(KEGG)
Substrate
Product
Comment
Binds FMN, FAD and a [2Fe-2S] cluster. The enzyme consists of two subunits, an FMN binding catalytic subunit and a FAD and iron-sulfur binding electron transfer subunit [4]. The reaction, which takes place in the cytosol, is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. Other class 1 dihydroorotate dehydrogenases use either fumarate (EC
1.3.98.1 ) or NADP+ (EC
1.3.1.15 ) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC
1.3.5.2 ) uses quinone as electron acceptor.
History
EC 1.3.1.14 created 1972, modified 2011
Pathway
Orthology
K17828 dihydroorotate dehydrogenase (NAD+) catalytic subunit
Genes
VIB : VspSTUT11_24310(pyrD_2)
TIB : THMIRHAM_20110(pyrD)
TSE : THMIRHAS_23260(pyrD)
TZO : THMIRHAT_02470(pyrD_2)
THIC : TspCOW1_25580(pyrDB)
ORB : IPMB12_05515 IPMB12_10475
BYI : BYI23_C001800 BYI23_D012310
PCAF : DSC91_002389 DSC91_006858
PANN : PanNE5_43890(pyrD_2)
BUE : BRPE67_CCDS10430(pyrD) BRPE67_DCDS00980(pyrD)
PIG : EGT29_01300 EGT29_03805
RHZ : RHPLAN_48670 RHPLAN_64950
GBN : GEOBRER4_22460(pyrD)
DDN : DND132_0926 DND132_2790
PPOR : JCM14722_06970(pyrD)
LCRE : Pla8534_13150(pyrD_1) Pla8534_33100(pyrD_2)
SMAM : Mal15_31920(pyrD_2)
SNEP : Enr13x_46440(pyrD_1)
SMAE : TBK1r_13020(pyrD_1)
AMUC : Pan181_32940(pyrD_2)
AMOB : HG15A2_18270(pyrD_1)
FMR : Fuma_02382(pyrD_1) Fuma_03188(pyrD_2)
GMR : GmarT_12760(pyrD_1) GmarT_40220(pyrD_2)
GIM : F1728_08355 F1728_26040
GPN : Pan110_12610(preA) Pan110_39020(pyrD)
MRI : Mal4_21340(pyrDB) Mal4_57660(pyrD)
PLON : Pla110_22860(pyrD_1) Pla110_26720(pyrD_2)
TPOL : Mal48_29370(pyrD_2)
CCOP : Mal65_23310(pyrD_2)
VBL : L21SP4_02054(pyrD_2)
TRC : DYE49_03925 DYE49_11335
BTHO : Btheta7330_02524(pyrD_1)
BCEL : BcellWH2_05364(pyrD)
PCRE : NCTC12858_01373(pyrD_2)
PCAG : NCTC12856_00396(pyrD)
PSOE : CE91St14_13170(pyrD)
PMUC : ING2E5A_1707(pyrD3)
PMER : INE87_00645(pyrD_1) INE87_01272(pyrD_2)
COPR : Cop2CBH44_05760(pyrD)
PHER : prwr041_02290(pyrD)
POC : NCTC13071_02754(pyrDB)
ACOU : A5CBH24_14910(pyrDB)
ADA : A5CPEGH6_17530(pyrDB)
PROC : Ptc2401_00574(pyrD_1)
BAZ : BAMTA208_09385(pyrD)
BACF : AM500_15560 AM500_17505
BCIR : C2I06_03105 C2I06_15825
VNE : CFK40_12810 CFK40_14805
LAO : AOX59_01610 AOX59_03430
GCS : MUN88_01950 MUN88_18040
GSM : MUN87_00995 MUN87_17685
BLEN : NCTC4824_02724(pyrD)
PSUA : FLK61_32920 FLK61_37550
PARG : PspKH34_26720(pyrD)
STEA : C0679_02275 C0679_06430
SDP : NCTC12225_01839(pyrD)
SPIC : SAMEA4384060_1744(pyrD)
SSTE : SAMEA4384403_1628(pyrD)
LMOC : LMOSLCC5850_1895(pyrD)
LMW : LMOSLCC2755_1894(pyrD)
LMX : LMOSLCC2372_1899(pyrD)
LMZ : LMOSLCC2482_1895(pyrD)
LMON : LMOSLCC2376_1794(pyrD)
LMOS : LMOSLCC7179_1806(pyrD)
LMOO : LMOSLCC2378_1856(pyrD)
LMOY : LMOSLCC2479_1897(pyrD)
LMOT : LMOSLCC2540_1915(pyrD)
LMOA : LMOATCC19117_1850(pyrD)
LGZ : NCTC10812_00986(pyrDB)
GMO : NCTC11323_01176(pyrD)
GHA : NCTC10459_00574(pyrD)
KYR : CVV65_09550 CVV65_09570
SNV : SPNINV200_08850(pyrD)
SPNE : SPN034156_19080(pyrD)
SPNU : SPN034183_08640(pyrD)
SPNM : SPN994038_08530(pyrD)
SPNO : SPN994039_08540(pyrD)
SMC : SmuNN2025_0830(pyrDB)
SGG : SGGBAA2069_c09410(pyrD1)
SSAH : HSISS4_00974(pyrDb)
SVB : NCTC12167_00949(pyrD)
SFER : NCTC12278_00813(pyrDB)
SAUP : NCTC3168_01795(pyrD)
SVF : NCTC3166_00952(pyrD)
SMIE : NCTC11169_00782(pyrD)
SPAM : SP4011_13540(pyrD1)
LHO : LOOC260_122150(pyrD)
EFC : EFAU004_00964(pyrDB)
EFAU : EFAU085_01382(pyrDB)
EFU : HMPREF0351_11355(pyrD)
ECEC : NCTC12421_01280(pyrDB)
CTET : BN906_00982 BN906_02591
CBI : CLJ_0029 CLJ_B3509(pyrD)
CBT : CLH_0590 CLH_2342(pyrD)
CLS : CXIVA_05180(PyrD) CXIVA_14370(PyrD)
CPAE : CPAST_c26860(pyrD2)
CTAE : BGI42_03070 BGI42_10205
CCOH : SAMEA4530647_2048(pyrD)
CAUN : CLAUR_042450(pyrDB)
CGEL : psyc5s11_44110(pyrD)
CLOD : C820_002120(pyrD_1)
CALE : FDN13_07875 FDN13_13190
CLO : HMPREF0868_0716(pyrD)
PFAA : MM59RIKEN_03390(pyrD)
VCOP : MM50RIKEN_17470(pyrD)
FWA : DCMF_18530 DCMF_22635
STHR : BXT84_03445 BXT84_11140
BPRO : PMF13cell1_03083(pyrD)
LACY : A4V08_00350 A4V08_30805
CSCI : HDCHBGLK_02210(pyrD)
CHYL : CE91St63_09660(pyrD)
ACEL : acsn021_33540(pyrD)
ACHT : bsdcttw_36710(pyrD)
CBAR : PATL70BA_0976(pyrD) PATL70BA_2725
ETM : CE91St48_02670(pyrD)
GFE : Gferi_09860 Gferi_18475
PDF : CD630DERM_01860(pyrD)
ROC : HF520_12345 HF520_15120
PHX : KGNDJEFE_00374(pyrDB)
HAS : Halsa_1758 Halsa_2099
HHL : Halha_0919 Halha_1052
PHAR : NCTC13077_00459(pyrDB)
PIV : NCTC13079_01370(pyrD)
VRM : 44547418_00589(pyrDB)
VDN : NCTC11831_01373(pyrDB)
DHO : Dia5BBH33_11780(pyrD)
MANA : MAMMFC1_04096(pyrD)
PFAC : PFJ30894_01894(pyrD)
AARG : Aargi30884_09550(pyrD)
ABSI : A9CBEGH2_10750(pyrD)
FIT : Fi14EGH31_18670(pyrD)
CDIA : CaldiYA01_11300(pyrD)
EFR : EFREU_v1c01010(pyrDI)
ELJ : ELUMI_v1c00160(pyrDI)
SCR : SCHRY_v1c02480(pyrD)
SERI : SERIO_v1c04270(pyrDI)
SLL : SLITO_v1c07830(pyrDI)
SCOU : SCORR_v1c07420(pyrDI)
SPRN : S100390_v1c06850(pyrD)
SPIT : STU14_v1c06850(pyrD)
STAB : STABA_v1c06930(pyrDI)
SGQ : SGLAD_v1c05900(pyrDI)
PCAT : Pcatena_07380(pyrD)
RTS : CE91St31_17780(pyrD)
SAMB : SAM23877_6661(cgc5)
BEI : GCM100_19350(pyrD_1)
OFA : NF556_11835 NF556_15515
DCO : SAMEA4475696_1263(pyrD)
CGRN : 4412665_01193(pyrDB)
NAQU : ENKNEFLB_02741(pyrD_1)
ACTQ : OG417_19835 OG417_22600 OG417_35190
AACD : LWP59_18190 LWP59_24765
BBP : BBPR_0215(pyr) BBPR_0942(pyrD)
BBI : BBIF_0238 BBIF_0898(pyrD1)
BSCA : BBSC_1273 BBSC_2214
BGX : ESN35_01280 ESN35_05175
RMAR : GBA65_08140 GBA65_10310
PARQ : DSM112329_02632(pyrD)
CAP : CLDAP_23600 CLDAP_25040(pyrD)
AMO : Anamo_0627 Anamo_1358
PPIO : CE91St28_04770(pyrD)
THP : BG95_01770 BG95_02455
THER : Y592_01775 Y592_02465
OCY : OSSY52_21570(pyrD_2)
FPOL : ERS445057_01921(pyrD_1)
MEHF : MmiHf6_15670(pyrD_2)
MEES : MmiEs2_01060(pyrD_1)
TVO : TVG1224769(TVG1224769)
LOKI : Lokiarch_03490(pyrD_1) Lokiarch_48320(pyrD_2)
» show all
Taxonomy
Reference
Authors
FRIEDMANN HC, VENNESLAND B.
Title
Purification and properties of dihydro-orotic dehydrogenase.
Journal
J Biol Chem 233:1398-406 (1958)
Reference
Authors
FRIEDMANN HC, VENNESLAND B.
Title
Crystalline dihydroorotic dehydrogenase.
Journal
J Biol Chem 235:1526-32 (1960)
Reference
Authors
LIEBERMAN I, KORNBERG A.
Title
Enzymic synthesis and breakdown of a pyrimidine, orotic acid. I. Dihydro-orotic dehydrogenase.
Journal
Reference
Authors
Nielsen FS, Andersen PS, Jensen KF
Title
The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers.
Journal
Sequence
Reference
Authors
Rowland P, Norager S, Jensen KF, Larsen S
Title
Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster.
Journal
Sequence
Reference
Authors
Kahler AE, Nielsen FS, Switzer RL
Title
Biochemical characterization of the heteromeric Bacillus subtilis dihydroorotate dehydrogenase and its isolated subunits.
Journal
Sequence
Reference
Authors
Marcinkeviciene J, Tinney LM, Wang KH, Rogers MJ, Copeland RA
Title
Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.3.1.14
ExPASy - ENZYME nomenclature database: 1.3.1.14
LinkDB
All DBs