KEGG ENZYME: 1.6.3.3

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

MIWA:

SS37A_37330

DAT:	HRM2_42520(nox2)

DOV:	DSCO28_64860

SWO:

Swol_1833

KSL:	OG809_34960

PDX:

Psed_6287

PAUT:

Pdca_54740

PBRO:

HOP40_10155

LEO:	AMK43_03030

ACO:	Amico_1237

TLI:

Tlie_1355

PPIO:

CE91St28_05050

PYY:	RAH42_02965

ARAM:

KAR29_04550 KAR29_13580

RSI:	Runsl_2389

RUN:	DR864_20705

RUP:	DTQ70_26860

HSB:	MWH26_07060

HCU:	MUN79_17865

HCF:	MUN80_16305

RCG:	N7E81_11745

PSYD:

IMZ30_07330

FLG:	LV716_10365

MLT:

VC82_1005

MUT:	GVT53_15020

MAQI:

LDL77_06585

SPON:

HME9304_01025

DDF:	DEFDS_0705

FSI:	Flexsi_1502

MJA:

MJ_0649

MFE:	Mefer_0567

MVU:	Metvu_1320

MFS:	MFS40622_1061

MIF:	Metin_1169

MJH:	JH146_0868

MESG:

MLAUSG7_0046

MESA:

MLASG1_1226

MIG:	Metig_1551

MMP:

MMP1259

MMQ:	MmarC5_0332

MMX:	MmarC6_1414

MMZ:	MmarC7_0505

MMD:

GYY_07130

MMAK:

MMKA1_14840

MMAO:

MMOS7_13660

MMAD:

MMJJ_15860

MAE:

Maeo_0747

MVN:	Mevan_0572

MVO:

Mvol_0824

MOK:	Metok_0198

METF:

CFE53_02780

MTH:

MTH_1354

MMG:	MTBMA_c17440

MWO:	MWSIV6_1738

METC:

MTCT_1228

METE:

tca_01308(nasD)

METK:

FVF72_04795

MTHM:

FZP57_08505

METJ:

FZP68_02220

MST:

Msp_1460

MEIS:

PXD04_03050 PXD04_08275

MRU:	mru_0958(nox)

MSI:

Msm_0046

MEB:	Abm4_1204(nox)

MMIL:

sm9_1318(nox)

MEYE:

TL18_05295

MOL:

YLM1_0518

METV:

K4897_00635

MEL:	Metbo_0139

MEW:	MSWAN_2349

METH:

MBMB1_1976

MFC:	BRM9_2319(nox)

MFI:	DSM1535_1253

MCUB:

MCBB_2276

MSUB:

BK009_09175

METN:

BK008_04800

METT:

CIT01_04970

METO:

CIT02_07625

MEME:

HYG87_06000

MFEG:

GCM10025860_19120

MFV:

Mfer_0405

MKA:

MK0881

APO:	Arcpr_0107

PFU:

PF1532

PFI:

PFC_06890

PHO:	PH1509(PH1509)

PAB:

PAB1931

PYN:

PNA2_0095

PYA:	PYCH_10130

PYS:

Py04_1402

PYC:	TQ32_09330

TKO:

TK0304

TON:

TON_1271

TGA:	TGAM_0364(nox)

TSI:

TSIB_1323

TBA:	TERMP_00960

THE:	GQS_04555 GQS_08820

THA:

TAM4_1450

THM:

CL1_1373

TLT:

OCC_08789

THS:

TES1_1046

TNU:

BD01_1539

TEU:

TEU_04150

TGY:	X802_05670

THV:	ADU37_CDS05620

TCH:	CHITON_1737

TPEP:

A0127_02775

TPIE:

A7C91_01985

TGG:	A3K92_06935

TCE:	A3L02_04460

TBS:	A3L01_01390 A3L01_07430

THH:	CDI07_01370 CDI07_08140

TSL:	A3L11_00575 A3L11_05135

TTD:	A3L14_09780

TPRF:

A3L09_00385 A3L09_03565

TRL:	A3L10_05175 A3L10_06840

TPAF:

A3L08_00660

THY:	A3L12_02365

TIC:	FH039_03270 FH039_10615

TCQ:	TIRI35C_1810

THEM:

FPV09_10710

THEI:

K1720_09725

PPAC:

PAP_07680

MBA:	Mbar_A0960

MBY:	MSBRM_0041

MBW:	MSBRW_0038

MBAR:

MSBR2_0039

MBAK:

MSBR3_0021

MAC:	MA_4636(ndh)

MMA:

MM_1296

MMAZ:

MmTuc01_1344

MMJ:	MSMAS_0018

MMAC:

MSMAC_0018

MVC:	MSVAZ_0055

MEK:	MSKOL_0051

MLS:	MSLAZ_0019

METM:

MSMTP_0021

MEF:	MSWH1_0021

MEQ:	MSWHS_0021

MSJ:	MSSAC_0027

MSZ:	MSSIH_0025

MSW:	MSSIT_0025

MTHR:

MSTHT_1804

MTHE:

MSTHC_1482

MHOR:

MSHOH_0020

MFZ:	AOB57_008285

MBU:

Mbur_1767

MMET:

MCMEM_0025

MELO:

J7W08_10160

MEV:	Metev_0030

MPY:

Mpsy_1794

MZI:	HWN40_01295

MMAV:

RE476_10395

MSEB:

RE474_07000

MHZ:	Metho_2414

MCJ:

MCON_0597

MPD:

MCP_2598

MEZ:	Mtc_0825(ndh)

RCI:	RCIX501(ndh)

MELU:

MTLP_11920

TAR:	TALC_01339

MAX:	MMALV_14290

MER:	MMINT_04270

MEAR:

Mpt1_c09730

MEUZ:

KRP56_06960

MARC:

AR505_0212

ABI:

Aboo_0959

ACF:	AciM339_1012

SHC:	Shell_0843

KCR:

Kcr_1220

BARC:

AOA65_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

[afu:AF_0254 AF_0455]

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

[tma:TM1432 TM1433]

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

All links

Chemical substance (5)   
   KEGG COMPOUND (5)   
Chemical reaction (2)   
   KEGG REACTION (1)   
   KEGG RCLASS (1)   
Gene (253)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (180)   
   KEGG MGENES (49)   
   RefGene (23)   
Protein sequence (25)   
   UniProt (25)   
DNA sequence (20)   
   GenBank (10)   
   EMBL (10)   
All databases (305)   

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