KEGG   ENZYME: 1.6.5.9
Entry
EC 1.6.5.9                  Enzyme                                 

Name
NADH:quinone reductase (non-electrogenic);
type II NAD(P)H:quinone oxidoreductase;
NDE2 (gene name);
ndh (gene name);
NDH-II;
NDH-2;
NADH dehydrogenase (quinone) (ambiguous);
ubiquinone reductase (ambiguous);
coenzyme Q reductase (ambiguous);
dihydronicotinamide adenine dinucleotide-coenzyme Q reductase (ambiguous);
DPNH-coenzyme Q reductase (ambiguous);
DPNH-ubiquinone reductase (ambiguous);
NADH-coenzyme Q oxidoreductase (ambiguous);
NADH-coenzyme Q reductase (ambiguous);
NADH-CoQ oxidoreductase (ambiguous);
NADH-CoQ reductase (ambiguous);
NADH-ubiquinone reductase (ambiguous);
NADH-ubiquinone oxidoreductase (ambiguous);
reduced nicotinamide adenine dinucleotide-coenzyme Q reductase (ambiguous);
NADH-Q6 oxidoreductase (ambiguous);
NADH2 dehydrogenase (ubiquinone) (ambiguous);
NADH:ubiquinone oxidoreductase;
NADH:ubiquinone reductase (non-electrogenic)
Class
Oxidoreductases;
Acting on NADH or NADPH;
With a quinone or similar compound as acceptor
Sysname
NADH:quinone oxidoreductase
Reaction(IUBMB)
NADH + H+ + a quinone = NAD+ + a quinol [RN:R07358]
Reaction(KEGG)
R07358 > R02163
Substrate
NADH [CPD:C00004];
H+ [CPD:C00080];
quinone [CPD:C15602]
Product
NAD+ [CPD:C00003];
quinol [CPD:C15603]
Comment
A flavoprotein (FAD or FMN). Occurs in mitochondria of yeast and plants, and in aerobic bacteria. Has low activity with NADPH. Unlike EC 7.1.1.2, NADH:ubiquinone reductase (H+-translocating), this enzyme does not pump proteons of sodium ions across the membrane. It is also not sensitive to rotenone.
History
EC 1.6.5.9 created 2011 (EC 1.6.5.11 created 1972 as EC 1.6.99.5, transferred 2015 to EC 1.6.5.11, incorporated 2019), modified 2019
Orthology
K17871  NADH:ubiquinone reductase (non-electrogenic)
K23948  NADH:quinone reductase (non-electrogenic)
Genes
CIN: 100182249
SPU: 100888391
APLC: 110986378
SKO: 100373395
DPTE: 113796723
CSCU: 111641683
PTEP: 107438858
LGI: LOTGIDRAFT_224073
PCAN: 112563361
CRG: 105321592
MYI: 110463105
LAK: 106166048
NVE: 5508664
EPA: 110235097
ADF: 107342464
AMIL: 114960565
PDAM: 113687155
SPIS: 111337860
ATH: AT1G07180(NDA1) AT2G20800(NDB4) AT2G29990(NDA2) AT4G05020(NDB2) AT4G21490(NDB3) AT4G28220(NDB1)
LJA: Lj0g3v0132519.1(Lj0g3v0132519.1) Lj2g3v2279580.1(Lj2g3v2279580.1) Lj2g3v2279580.2(Lj2g3v2279580.2) Lj2g3v2279580.3(Lj2g3v2279580.3) Lj3g3v2873580.1(Lj3g3v2873580.1) Lj4g3v0445550.1(Lj4g3v0445550.1) Lj4g3v0447890.1(Lj4g3v0447890.1) Lj6g3v2083620.1(Lj6g3v2083620.1)
DOSA: Os01t0830100-01(Os01g0830100) Os05t0331200-01(Os05g0331200) Os07t0564500-01(Os07g0564500) Os08t0141400-01(Os08g0141400)
ATS: 109733687(LOC109733687) 109747592(LOC109747592) 109769370(LOC109769370) 109779678(LOC109779678) 109783120(LOC109783120)
APRO: F751_6396
SCE: YDL085W(NDE2) YML120C(NDI1) YMR145C(NDE1)
KMX: KLMA_10279(NDI1) KLMA_10695(NDE1)
NCS: NCAS_0A03930(NCAS0A03930) NCAS_0B00240(NCAS0B00240) NCAS_0D01150(NCAS0D01150)
NDI: NDAI_0E00230(NDAI0E00230) NDAI_0E01660(NDAI0E01660) NDAI_0H03010(NDAI0H03010)
TPF: TPHA_0C04800(TPHA0C04800) TPHA_0G02580(TPHA0G02580)
TBL: TBLA_0B08910(TBLA0B08910) TBLA_0D03320(TBLA0D03320)
TDL: TDEL_0B00230(TDEL0B00230) TDEL_0G03120(TDEL0G03120)
KAF: KAFR_0A02890(KAFR0A02890) KAFR_0B05060(KAFR0B05060) KAFR_0F02920(KAFR0F02920)
PIC: PICST_66598(NDE1)
SPAA: SPAPADRAFT_140814(NDE1)
SLB: AWJ20_3145(NDE2) AWJ20_806(NDE1)
NCR: NCU04803(npd-2) NCU08980(nde-2)
NTE: NEUTE1DRAFT122492(NEUTE1DRAFT_122492) NEUTE1DRAFT68534(NEUTE1DRAFT_68534)
ANG: ANI_1_408064(An07g03290) ANI_1_610074(An08g04240)
TASA: A1Q1_01474
ABP: AGABI1DRAFT74487(AGABI1DRAFT_74487) AGABI1DRAFT77116(NDE1)
ABV: AGABI2DRAFT224327(AGABI2DRAFT_224327) AGABI2DRAFT227697(NDE2)
MGL: MGL_3253
MRT: MRET_2441
TGO: TGME49_209150(NDH2-I)
SMIN: v1.2.003453.t1(symbB.v1.2.003453.t1) v1.2.023058.t1(symbB.v1.2.023058.t1) v1.2.027571.t1(symbB.v1.2.027571.t1) v1.2.027967.t1(symbB.v1.2.027967.t1) v1.2.035097.t1(symbB.v1.2.035097.t1) v1.2.040380.t1(symbB.v1.2.040380.t1)
NGD: NGA_0209201(NDH) NGA_0211800(NDH)
PAE: PA1024
PAEV: N297_1060
PAEI: N296_1060
PAEP: PA1S_20835
PAEM: U769_20680
PAEL: T223_21960
PAEG: AI22_13105
PAEC: M802_1057
PAEO: M801_1060
ABY: ABAYE2310
ABN: AB57_1579
ABX: ABK1_1836
ABH: M3Q_1745
ABAZ: P795_10460
ABAU: IX87_03535
ABAA: IX88_08705
ACC: BDGL_000729(ncd-2)
ACI: ACIAD1570
AGU: AS4_15870
AUG: URS_1963
MARJ: MARI_09980
ADI: B5T_00972
APAC: S7S_14955
AXE: P40_04635
REH: H16_B0757(h16_B0757)
CGD: CR3_3261(npd)
BCT: GEM_4688
BSTG: WT74_06310
BXE: Bxe_B2734
BXB: DR64_5067
ODI: ODI_R3969
RFR: Rfer_1008
POL: Bpro_3833
AJS: Ajs_3732
VEI: Veis_3873
DAC: Daci_1401
CTES: O987_22750
HYB: Q5W_03345
PBH: AAW51_0436(ncd2)
METR: BSY238_141
AZA: AZKH_1985(ncd2)
DOL: Dole_1182
DOV: DSCO28_51240(ncd-2)
DWD: DSCW_19220 DSCW_40460(ncd-2)
DALK: DSCA_39670(ncd-2)
DBR: Deba_2264
BPP: BPI_II568
BBT: BBta_5146
RPA: RPA1941
RPB: RPB_3433
RPD: RPD_2021
RPT: Rpal_2151
NWI: Nwi_3001
NHA: Nham_1075
RBM: TEF_16875
CCR: CC_2990
CAK: Caul_0738
CSE: Cseg_3484
LAQU: R2C4_20260
ZMO: ZMO1861
ZMN: Za10_1302
NAR: Saro_3073
SPHU: SPPYR_1920
SPHM: G432_19900
SPKC: KC8_02230
SECH: B18_16765
SPMI: K663_19748
SPHR: BSY17_3803
SINB: SIDU_10930
SMIC: SmB9_19560(ncd-2)
ELI: ELI_05175
SHUM: STHU_38860
MAG: amb2607
MAGX: XM1_3418
MAGN: WV31_06225
TMO: TMO_0840
BMQ: BMQ_3940
BMD: BMD_3924
BMEG: BG04_854
BAG: Bcoa_0811
BCOA: BF29_2888
BACO: OXB_0772
BEO: BEH_15100
BHA: BH2639
GKA: GK1066
GTN: GTNG_0930
AFL: Aflv_1885
AAMY: GFC30_1363
ANL: GFC29_246
LSP: Bsph_1377
HLI: HLI_02465
PASA: BAOM_1501(fabK)
PSYO: PB01_05555
ASOC: CB4_01628
SIV: SSIL_3147
LSN: LSA_03220
STH: STH2571
TMR: Tmar_1960
SAY: TPY_2453
MMC: Mmcs_4067
MKM: Mkms_4142
MJL: Mjls_4296
MVA: Mvan_4576
MGI: Mflv_2128
MVQ: MYVA_4354
MHAS: MHAS_02926
MMIN: MMIN_27600
MHIB: MHIB_06560
NFA: NFA_55910
NSR: NS506_00518(ncd2)
REQ: REQ_04030
SLE: sle_61270(sle_61270) sle_64350(sle_64350)
AMD: AMED_3837
AMN: RAM_19545
AMM: AMES_3792
AMZ: B737_3792
PSEA: WY02_09230
PSEE: FRP1_20815
PSEH: XF36_18405
AMI: Amir_4367
STI: Sthe_2924
TTK: TST_0731
 » show all
Reference
1  [PMID:6800784]
  Authors
Bergsma J, Strijker R, Alkema JY, Seijen HG, Konings WN
  Title
NADH dehydrogenase and NADH oxidation in membrane vesicle from Bacillus subtilis.
  Journal
Eur J Biochem 120:599-606 (1981)
DOI:10.1111/j.1432-1033.1981.tb05742.x
Reference
2
  Authors
Moller, I.M, and Palmer, J.M.
  Title
Direct evidence for the presence of a rotenone-resistant NADH dehydrogenase on the inner surface of plant mitochondria.
  Journal
Physiol Plant 54:267-274 (1982)
Reference
3  [PMID:3138118]
  Authors
de Vries S, Grivell LA
  Title
Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae.
  Journal
Eur J Biochem 176:377-84 (1988)
DOI:10.1111/j.1432-1033.1988.tb14292.x
  Sequence
[sce:YML120C]
Reference
4  [PMID:10381390]
  Authors
Kerscher SJ, Okun JG, Brandt U
  Title
A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica.
  Journal
J Cell Sci 112 ( Pt 14):2347-54 (1999)
  Sequence
Reference
5  [PMID:15725055]
  Authors
Rasmusson AG, Soole KL, Elthon TE
  Title
Alternative NAD(P)H dehydrogenases of plant mitochondria.
  Journal
Annu Rev Plant Biol 55:23-39 (2004)
DOI:10.1146/annurev.arplant.55.031903.141720
Reference
6  [PMID:15590775]
  Authors
Melo AM, Bandeiras TM, Teixeira M
  Title
New insights into type II NAD(P)H:quinone oxidoreductases.
  Journal
Microbiol Mol Biol Rev 68:603-16 (2004)
DOI:10.1128/MMBR.68.4.603-616.2004
Other DBs
ExplorEnz - The Enzyme Database: 1.6.5.9
IUBMB Enzyme Nomenclature: 1.6.5.9
ExPASy - ENZYME nomenclature database: 1.6.5.9
BRENDA, the Enzyme Database: 1.6.5.9
CAS: 9028-04-0

DBGET integrated database retrieval system