Entry
Name
dihydroorotate dehydrogenase (fumarate);
DHOdehase (ambiguous);
dihydroorotate dehydrogenase (ambiguous);
dihydoorotic acid dehydrogenase (ambiguous);
DHOD (ambiguous);
DHODase (ambiguous);
dihydroorotate oxidase;
pyr4 (gene name)
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With other, known, physiological acceptors
BRITE hierarchy
Sysname
(S)-dihydroorotate:fumarate oxidoreductase
Reaction(IUBMB)
(S)-dihydroorotate + fumarate = orotate + succinate [RN:
R01867 ]
Reaction(KEGG)
Substrate
Product
Comment
Binds FMN. The reaction, which takes place in the cytosol, is the only redox reaction in the de novo biosynthesis of pyrimidine nucleotides. Molecular oxygen can replace fumarate in vitro. Other class 1 dihydroorotate dehydrogenases use either NAD+ (EC
1.3.1.14 ) 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 1.3.98.1 created 1961 as EC 1.3.3.1, transferred 2011 to EC 1.3.98.1
Pathway
Orthology
K00226 dihydroorotate dehydrogenase (fumarate)
Genes
NCS : NCAS_0D03520(NCAS0D03520)
NDI : NDAI_0H00120(NDAI0H00120)
TPF : TPHA_0K00200(TPHA0K00200)
TBL : TBLA_0B10140(TBLA0B10140)
TDL : TDEL_0F05620(TDEL0F05620)
KAF : KAFR_0L00170(KAFR0L00170)
KNG : KNAG_0K02180(KNAG0K02180)
NTE : NEUTE1DRAFT15063(NEUTE1DRAFT_15063)
BFU : BCIN_16g04110(Bcura1)
ABP : AGABI1DRAFT51017(AGABI1DRAFT_51017)
ABV : AGABI2DRAFT214748(AGABI2DRAFT_214748)
SCM : SCHCO_02645180(SCHCODRAFT_02645180)
SMIN : v1.2.031230.t1(symbB.v1.2.031230.t1)
EHX : EMIHUDRAFT_447879 EMIHUDRAFT_454934
TCR : 507091.40 508375.50 511643.20 511923.120
MARA : D0851_10945 D0851_18410
KAK : Kalk_02580 Kalk_07040
ECOR : SAMEA4412678_1339(pyrDA)
CHAE : CH06BL_34350(pyrDA)
MTUN : MTUNDRAET4_0045.1 MTUNDRAET4_4084
RCP : RCAP_rcc01727(pyrD1)
DWD : DSCW_05980 DSCW_06290
SAX : USA300HOU_2583(pyrD)
SUQ : HMPREF0772_10602(pyrD)
SSH : NCTC13712_02544(pyrD)
SSIM : SAMEA4384339_2389(pyrD)
GMO : NCTC11323_00512(pyrDA)
GHA : NCTC10459_00606(pyrDA)
LLX : NCDO2118_1571(pyrDA)
SPYM : M1GAS476_1227(pyrD)
SPH : MGAS10270_Spy1236(pyrD)
SPI : MGAS10750_Spy1273(pyrD)
SPJ : MGAS2096_Spy1237(pyrD)
SPK : MGAS9429_Spy1214(pyrD)
STG : MGAS15252_1104(pyrD)
STZ : SPYALAB49_001164(pyrD)
SNV : SPNINV200_06750(pyrD)
SPNG : HMPREF1038_00774(pyrDA)
SPNE : SPN034156_17400(pyrD)
SPNU : SPN034183_06920(pyrD)
SPNM : SPN994038_06810(pyrD)
SPNO : SPN994039_06820(pyrD)
SMC : SmuNN2025_1383(pyrD)
SGG : SGGBAA2069_c05820(pyrD)
SSAH : HSISS4_00782(pyrDa)
SVB : NCTC12167_01130(pyrDa)
SMEN : SAMEA4412692_1637(pyrDA)
SFER : NCTC12278_00551(pyrD)
SCAI : NCTC12191_01271(pyrD)
SAUP : NCTC3168_01081(pyrA)
SURN : NCTC13766_00581(pyrDa)
SVF : NCTC3166_01667(pyrA)
LDB : Ldb1530(pyrD2) Ldb2114(pyrD1)
LPW : LpgJCM5343_08490(pyrD)
EFC : EFAU004_00893(pyrDA)
EFAU : EFAU085_01453(pyrDA)
EFU : HMPREF0351_11431(pyrD2)
PDC : CDIF630_02300(preA1)
PDF : CD630DERM_20770(pyrD1)
MMEH : M5I08_10365 M5I08_19645
AUS : IPK37_15620 IPK37_16900
CGRN : 4412665_00536(pyrD)
PFR : PFREUD_01850 PFREUD_07080
PFRE : RM25_0187 RM25_0674
PACD : EGX94_05835 EGX94_10695
PAUS : NCTC13651_00002(preA_1) NCTC13651_01709(preA_2)
PROP : QQ658_02755 QQ658_12810
BROO : brsh051_11910 brsh051_22910
SYY : SYNGTS_2808(sll0744)
SYT : SYNGTI_2807(sll0744)
SYS : SYNPCCN_2806(sll0744)
SYQ : SYNPCCP_2806(sll0744)
PAGH : NIES204_36800(pyrD_2)
STAN : STA3757_05380(pyrD_1)
PBF : CFX0092_A0455 CFX0092_A0485
OBG : Verru16b_00598(preA_1) Verru16b_01854(preA_2)
MIN : Minf_1387(pyrD) Minf_2385(pyrD)
RUL : UC8_16580(pyrDB) UC8_27550
RML : FF011L_27520(pyrDB_1) FF011L_29420(pyrDB_2) FF011L_48580
AHEL : Q31a_47690(pyrDB_1) Q31a_48380(pyrDB_2)
RLC : K227x_04690(pyrDB) K227x_04760(pyrD_1)
AMUC : Pan181_30330(pyrD_1)
AMOB : HG15A2_35930(pyrD_2)
VBL : L21SP4_00337(pyrD_1)
SFC : Spiaf_0536 Spiaf_0539
SLR : L21SP2_1672 L21SP2_2986
ABAC : LuPra_04112(preA_2)
BTHO : Btheta7330_01888(preA)
BCEL : BcellWH2_05077(preA)
PCRE : NCTC12858_00853(pyrD_1)
PCAG : NCTC12856_00153(preA)
PBT : ING2E5B_1970 ING2E5B_2366
PMUC : ING2E5A_0046(URA1) ING2E5A_0807(pyrD1) ING2E5A_2689(pyrD5)
PET : PEIBARAKI_4230 PEIBARAKI_6575
PSAC : PSM36_0452 PSM36_3125
TTZ : FHG85_06125 FHG85_08615 FHG85_09540
BLQ : L21SP5_00505(pyrD_2) L21SP5_00918(preA) L21SP5_01040(pyrDA_1) L21SP5_02712(pyrDA_2)
DORI : FH5T_12270 FH5T_15380
DRC : G0Q07_05720 G0Q07_13085
MCOS : GM418_18080 GM418_18895 GM418_19895
ASX : CDL62_00045 CDL62_02800 CDL62_03795 CDL62_17350
ALKQ : M9189_03830 M9189_05245 M9189_06755 M9189_09210
MBAS : ALGA_0168 ALGA_1617 ALGA_2539
SHYR : LA303_01790 LA303_02695 LA303_05480 LA303_05520 LA303_06845
PROC : Ptc2401_02228(pyrD_2)
DAP : Dacet_2754 Dacet_2941
NKF : Nkreftii_000175 Nkreftii_002103
» show all
Taxonomy
Reference
Authors
Bjornberg O, Rowland P, Larsen S, Jensen KF
Title
Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis.
Journal
Sequence
Reference
Authors
Rowland P, Bjornberg O, Nielsen FS, Jensen KF, Larsen S
Title
The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function.
Journal
Sequence
Reference
Authors
Norager S, Arent S, Bjornberg O, Ottosen M, Lo Leggio L, Jensen KF, Larsen S
Title
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function.
Journal
Sequence
Reference
Authors
Zameitat E, Pierik AJ, Zocher K, Loffler M
Title
Dihydroorotate dehydrogenase from Saccharomyces cerevisiae: spectroscopic investigations with the recombinant enzyme throw light on catalytic properties and metabolism of fumarate analogues.
Journal
Sequence
Reference
Authors
Inaoka DK, Sakamoto K, Shimizu H, Shiba T, Kurisu G, Nara T, Aoki T, Kita K, Harada S
Title
Structures of Trypanosoma cruzi dihydroorotate dehydrogenase complexed with substrates and products: atomic resolution insights into mechanisms of dihydroorotate oxidation and fumarate reduction.
Journal
Sequence
Reference
Authors
Cheleski J, Wiggers HJ, Citadini AP, da Costa Filho AJ, Nonato MC, Montanari CA
Title
Kinetic mechanism and catalysis of Trypanosoma cruzi dihydroorotate dehydrogenase enzyme evaluated by isothermal titration calorimetry.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 1.3.98.1
ExPASy - ENZYME nomenclature database: 1.3.98.1