[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=11932446 [NCBI, ExPASy, EBI, Israel, Japan] Hoefnagel M.H.N., Starrenburg M.J.C., Martens D.E., Hugenholtz J., Kleerebezem M., Van Swam I.I., Bongers R., Westerhoff H.V., Snoep J.L.; "Metabolic engineering of lactic acid bacteria, the combined approach: kinetic modelling, metabolic control and experimental analysis."; Microbiology 148:1003-1013(2002).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1128/JB.01768-06; PubMed=17307855 [NCBI, ExPASy, EBI, Israel, Japan] Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J.; "The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363."; J. Bacteriol. 189:3256-3270(2007).
[3]	PROTEIN SEQUENCE OF 1-25, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. DOI=10.1016/S0958-6946(01)00031-0; AGRICOLA=IND23261759 Lopez de Felipe F., Hugenholtz J.; "Purification and characterisation of the water forming NADH-oxidase from Lactococcus lactis."; Int. Dairy J. 11:37-44(2001).

Comments

FUNCTION: Catalyzes the four-electron reduction of molecular oxygen to water. Active on beta-NADH, but not on alpha-NADH, beta-NADPH or alpha-NADPH. Under aerobic conditions, oxygen acts as the electron acceptor. Under anaerobic conditions, DCIP and MB can replace oxygen as the electron acceptor.
CATALYTIC ACTIVITY: NADH + acceptor = NAD⁺ + reduced acceptor.
COFACTOR: Binds 1 FAD per subunit.
ENZYME REGULATION: Inhibited by hydrogen peroxide, sulfhydryl reagents and quinine, but not by EDTA.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=4.1 µM for beta-NADH (in the presence of oxygen);
Kinetic parameters:	V_max=83 µmol/min/mg enzyme toward beta-NADH (in the presence of oxygen);
pH dependence:	Optimum pH is 6.0-9.0. Below pH 6.0 the enzyme is reversibly inactivated, above pH 10.0 the enzyme is irreversibly inactivated;

SUBUNIT: Homodimer.
SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY046926; AAL02357.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AM406671; CAL97012.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001031758.1; -.

3D structure databases

ModBase

A2RIB7.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.390.30; Pyr_redox_dim; 1.

Pfam

PF00070; Pyr_redox; 2.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00411; PNDRDTASEI.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

BLOCKS

A2RIB7.

Genome annotation databases

GeneID

4796799; -.

GenomeReviews

AM406671_GR; llmg_0408.

KEGG

llm:llmg_0408; -.

CMR

A2RIB7; llmg_0408.

Other

ProtoNet

A2RIB7.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidation; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 446`	`446`	`NADH oxidase.`	`PRO_0000292941`
`NP_BIND`	`7 11`	`5`	`FAD (By similarity).`
`NP_BIND`	`109 112`	`4`	`FAD (By similarity).`
`ACT_SITE`	`10 10`		`Proton acceptor (By similarity).`
`ACT_SITE`	`42 42`		`Redox-active (By similarity).`
`BINDING`	`42 42`		`FAD (By similarity).`
`BINDING`	`159 159`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`178 178`		`NAD (By similarity).`
`BINDING`	`187 187`		`NAD (By similarity).`
`BINDING`	`244 244`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`282 282`		`FAD (By similarity).`
`BINDING`	`298 298`		`NAD; via carbonyl oxygen (By similarity).`
`BINDING`	`300 300`		`FAD; via amide nitrogen (By similarity).`
`BINDING`	`329 329`		`NAD; via carbonyl oxygen (By similarity).`
`MOD_RES`	`42 42`		`Cysteine sulfenic acid (-SOH) (By similarity).`
`CONFLICT`	`11 11`		`A -> AA (in Ref. 3; AA sequence).`

Sequence information

Length: 446 AA [This is the length of the unprocessed precursor]

Molecular weight: 48872 Da [This is the MW of the unprocessed precursor]

CRC64: 1B1FA2FE313D6C03 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIVVIGTNH AGIATANTLL EQYPGHEIVM IDRNSNMSYL GCGTAIWVGR QIEKPDELFY 

        70         80         90        100        110        120 
AKAEDFEAKG VKILTETEVS EIDFANKKVY AKTKSDDEII EAYDKLVLAT GSRPIIPNLP 

       130        140        150        160        170        180 
GKDLKGIHFL KLFQEGQAID AEFAKEKVKR IAVIGAGYIG TEIAEAAKRR GKEVLLFDAE 

       190        200        210        220        230        240 
NTSLASYYDE EFAKGMDENL AQHGIELHFG ELAKEFKANE EGYVSQIVTN KATYDVDLVI 

       250        260        270        280        290        300 
NCIGFTANSA LASDKLATFK NGAIKVDKHQ QSSDPDVYAV GDVATIYSNA LQDFTYIALA 

       310        320        330        340        350        360 
SNAVRSGIVA GHNIGGKELE SVGVQGSNGI SIFGYNMTST GLSVKAAKKL GLEVSFSDFE 

       370        380        390        400        410        420 
DKQKAWFLHE NNDSVKIRIV YETKSRRIIG AQLASKSEII AGNINMFSLA IQEKKTIDEL 

       430        440 
ALLDLFFLPH FNSPYNYMTV AALNAK

A2RIB7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools