KEGG   ENZYME: 1.6.3.3
Entry
EC 1.6.3.3                  Enzyme                                 
Name
NADH oxidase (H2O2-forming);
NOX-1;
H2O2-forming NADH oxidase
Class
Oxidoreductases;
Acting on NADH or NADPH;
With oxygen as acceptor
Sysname
NADH:oxygen oxidoreductase (H2O2-forming)
Reaction(IUBMB)
NADH + H+ + O2 = NAD+ + H2O2 [RN:R07171]
Reaction(KEGG)
R07171
Substrate
NADH [CPD:C00004];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
NAD+ [CPD:C00003];
H2O2 [CPD:C00027]
Comment
A flavoprotein (FAD). The bacterium Streptococcus mutans contains two distinct NADH oxidases, a H2O2-forming enzyme and a H2O-forming enzyme (cf. EC 1.6.3.4, NADH oxidase (H2O-forming)) [1]. The enzymes from the anaerobic archaea Methanocaldococcus jannaschii [6] and Pyrococcus furiosus [3] also produce low amounts of H2O. Unlike EC 1.6.3.1 (NAD(P)H oxidase) it has no activity towards NADPH.
History
EC 1.6.3.3 created 2013
Orthology
K17870  NADH oxidase (H2O2-forming)
Genes
SULNFJR47_05370
SULCCVO_04135
SUNSUN_0854
NAMNAMH_0952
CPAFC6V80_04875
DPSDP1550
DOLDole_3071
DATHRM2_08060 HRM2_42520(nox2)
DTOTOL2_C37270
DOVDSCO28_64860
DWDDSCW_19890 DSCW_33890
DALKDSCA_32480
HMRHipma_0835
AFRAFE_1803
AFELferr_1480
ACUAtc_1532
ACZAcaty_c1300
AFIAcife_0796 Acife_2017
AFJAFERRID_27740
SWOSwol_1833
MTHOMOTHE_c14430(norW)
MTHZMOTHA_c15290(norW)
PDXPsed_6287
PAUTPdca_54740
PBROHOP40_10155
SPEREW093_11645
THYDTTHT_0457
LEOAMK43_03030
ACOAmico_1237
TLITlie_1355
PPIOCE91St28_05050
MCOSGM418_29440
RSIRunsl_2389
RUNDR864_20705
RUPDTQ70_26860
MLTVC82_1005
MUTGVT53_15020
MAQILDL77_06585
SPONHME9304_01025
FLGLV716_10365
BIAGMA17_10670
IALIALB_3006
TMMTmari_0377
TMITHEMA_02825
TMWTHMA_0386
TMQTHMB_0386
TMXTHMC_0386
TPTTpet_0530
TRQTRQ2_0544
TNACTN_0317
TNPTnap_0182
THQT2812B_02785
THZCELL2_02800
THRTRQ7_03085
PHYAJ81_10050
TMETmel_1229
THPBG95_06955
THERY592_07035
OCYOSSY52_13290
MPZMarpi_1160
MARNLN42_06340
KPFIX53_07750
ASACATHSA_1731
DDFDEFDS_0705 DEFDS_1684
CNICalni_1893
FSIFlexsi_1502
MJAMJ_0649
MFEMefer_0567
MVUMetvu_1320
MFSMFS40622_1061
MIFMetin_1169
MJHJH146_0868
MESGMLAUSG7_0046
MESAMLASG1_1226
MIGMetig_1551
MMPMMP1259
MMQMmarC5_0332
MMXMmarC6_1414
MMZMmarC7_0505
MMDGYY_07130
MMAKMMKA1_14840
MMAOMMOS7_13660
MMADMMJJ_15860
MAEMaeo_0747
MVNMevan_0572
MVOMvol_0824
MOKMetok_0198
METFCFE53_02780
MTHMTH_1354
MMGMTBMA_c17440
METCMTCT_1228
MWOMWSIV6_1738
METEtca_01308(nasD)
METKFVF72_04795
MTHMFZP57_08505
METJFZP68_02220
MSTMsp_1460
MRUmru_0958(nox)
MSIMsm_0046
MEBAbm4_1204(nox)
MMILsm9_1318(nox)
MEYETL18_05295
MOLYLM1_0518
MELMetbo_0139
MEWMSWAN_2349
METHMBMB1_1976
MFCBRM9_2319(nox)
MFIDSM1535_1253
MCUBMCBB_2276
MSUBBK009_09175
METNBK008_04800
METTCIT01_04970
METOCIT02_07625
MEMEHYG87_06000
MFVMfer_0405
MKAMK0881
AFGAFULGI_00021130
APOArcpr_0107
PFUPF1532
PFIPFC_06890
PHOPH1509(PH1509)
PABPAB1931
PYNPNA2_0095
PYAPYCH_10130
PYSPy04_1402
PYCTQ32_09330
TKOTK0304
TONTON_1271
TGATGAM_0364(nox)
TSITSIB_1323
TBATERMP_00960
THEGQS_04555 GQS_04595 GQS_08820
THATAM4_1450 TAM4_348
THMCL1_0572 CL1_1373
TLTOCC_08789
THSTES1_1046
TNUBD01_1539 BD01_2217
TEUTEU_04150 TEU_05415
TGYX802_02720 X802_05670
THVADU37_CDS05620
TCHCHITON_1737
TPEPA0127_02775 A0127_07790
TPIEA7C91_01985
TGGA3K92_06935
TCEA3L02_04460
TBSA3L01_01390 A3L01_07430
THHCDI07_01370 CDI07_08140
TSLA3L11_00575 A3L11_05090 A3L11_05135
TTDA3L14_02805 A3L14_09780
TPRFA3L09_00385 A3L09_02810 A3L09_03565
TRLA3L10_05175 A3L10_06840
TPAFA3L08_00660
THYA3L12_02365
TICFH039_03200 FH039_03270 FH039_10615
TCQTIRI35C_1810
THEMFPV09_10710
PPACPAP_07680
MBAMbar_A0960
MBYMSBRM_0041
MBWMSBRW_0038
MBARMSBR2_0039
MBAKMSBR3_0021
MACMA_4636(ndh)
MMAMM_1296
MMAZMmTuc01_1344
MMJMSMAS_0018
MMACMSMAC_0018
MVCMSVAZ_0055
MEKMSKOL_0051
MLSMSLAZ_0019
METMMSMTP_0021
MEFMSWH1_0021
MEQMSWHS_0021
MSJMSSAC_0027
MSZMSSIH_0025
MSWMSSIT_0025
MTHRMSTHT_1804
MTHEMSTHC_1482
MHORMSHOH_0020
MFZAOB57_008285
MBUMbur_1767
MMETMCMEM_0025
MELOJ7W08_10160
MEVMetev_0030
MPYMpsy_1794
MZIHWN40_01295
MHZMetho_2414
MCJMCON_0597
MPDMCP_2598
MEZMtc_0825(ndh)
RCIRCIX501(ndh)
MELUMTLP_11920
TARTALC_01339
MAXMMALV_14290
MERMMINT_04270
MEARMpt1_c09730
MARCAR505_0212
ABIAboo_0959
ACFAciM339_1012
SHCShell_0843
DKADKAM_0441
DFDDesfe_0617
DMUDesmu_0634
THFMA03_01995
KCRKcr_1220
BARCAOA65_1542
 » show all
Reference
1  [PMID:8254304]
  Authors
Higuchi M, Shimada M, Yamamoto Y, Hayashi T, Koga T, Kamio Y
  Title
Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans.
  Journal
J Gen Microbiol 139:2343-51 (1993)
DOI:10.1099/00221287-139-10-2343
  Sequence
[smu:SMU_765]
Reference
2  [PMID:11722568]
  Authors
Ward DE, Donnelly CJ, Mullendore ME, van der Oost J, de Vos WM, Crane EJ 3rd
  Title
The NADH oxidase from Pyrococcus furiosus. Implications for the protection of anaerobic hyperthermophiles against oxidative stress.
  Journal
Eur J Biochem 268:5816-23 (2001)
DOI:10.1046/j.0014-2956.2001.02526.x
  Sequence
[pfu:PF1532]
Reference
3  [PMID:12823559]
  Authors
Kengen SW, van der Oost J, de Vos WM
  Title
Molecular characterization of H2O2-forming NADH oxidases from Archaeoglobus fulgidus.
  Journal
Eur J Biochem 270:2885-94 (2003)
DOI:10.1046/j.1432-1033.2003.03668.x
  Sequence
Reference
4  [PMID:17293421]
  Authors
Yang X, Ma K
  Title
Characterization of an exceedingly active NADH oxidase from the anaerobic hyperthermophilic bacterium Thermotoga maritima.
  Journal
J Bacteriol 189:3312-7 (2007)
DOI:10.1128/JB.01525-06
  Sequence
Reference
5  [PMID:18521590]
  Authors
Hirano J, Miyamoto K, Ohta H
  Title
Purification and characterization of thermostable H2O2-forming NADH oxidase from  2-phenylethanol-assimilating Brevibacterium sp. KU1309.
  Journal
Appl Microbiol Biotechnol 80:71-8 (2008)
DOI:10.1007/s00253-008-1535-x
Reference
6  [PMID:19118348]
  Authors
Case CL, Rodriguez JR, Mukhopadhyay B
  Title
Characterization of an NADH oxidase of the flavin-dependent disulfide reductase family from Methanocaldococcus jannaschii.
  Journal
Microbiology 155:69-79 (2009)
DOI:10.1099/mic.0.024265-0
  Sequence
[mja:MJ_0649]
Other DBs
ExplorEnz - The Enzyme Database: 1.6.3.3
IUBMB Enzyme Nomenclature: 1.6.3.3
ExPASy - ENZYME nomenclature database: 1.6.3.3
BRENDA, the Enzyme Database: 1.6.3.3

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