NAOX_LACLM
ID NAOX_LACLM Reviewed; 446 AA.
AC A2RIB7; P81759; Q8KR34;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=NADH oxidase;
DE Short=NOXase;
DE EC=7.1.1.2;
GN Name=noxE {ECO:0000312|EMBL:CAL97012.1}; OrderedLocusNames=llmg_0408;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11932446; DOI=10.1099/00221287-148-4-1003;
RA Hoefnagel M.H.N., Starrenburg M.J.C., Martens D.E., Hugenholtz J.,
RA Kleerebezem M., Van Swam I.I., Bongers R., Westerhoff H.V., Snoep J.L.;
RT "Metabolic engineering of lactic acid bacteria, the combined approach:
RT kinetic modelling, metabolic control and experimental analysis.";
RL Microbiology 148:1003-1013(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-25, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX AGRICOLA=IND23261759; DOI=10.1016/S0958-6946(01)00031-0;
RA Lopez de Felipe F., Hugenholtz J.;
RT "Purification and characterisation of the water forming NADH-oxidase from
RT Lactococcus lactis.";
RL Int. Dairy J. 11:37-44(2001).
CC -!- FUNCTION: Catalyzes the four-electron reduction of molecular oxygen to
CC water. Active on beta-NADH, but not on alpha-NADH, beta-NADPH or alpha-
CC NADPH. Under aerobic conditions, oxygen acts as the electron acceptor.
CC Under anaerobic conditions, DCIP and MB can replace oxygen as the
CC electron acceptor. {ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC Evidence={ECO:0000269|Ref.3};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|Ref.3};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|Ref.3};
CC -!- ACTIVITY REGULATION: Inhibited by hydrogen peroxide, sulfhydryl
CC reagents and quinine, but not by EDTA. {ECO:0000269|Ref.3}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.1 uM for beta-NADH (in the presence of oxygen)
CC {ECO:0000269|Ref.3};
CC Vmax=83 umol/min/mg enzyme toward beta-NADH (in the presence of
CC oxygen) {ECO:0000269|Ref.3};
CC pH dependence:
CC Optimum pH is 6.0-9.0. Below pH 6.0 the enzyme is reversibly
CC inactivated, above pH 10.0 the enzyme is irreversibly inactivated.
CC {ECO:0000269|Ref.3};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000255}.
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DR EMBL; AY046926; AAL02357.1; -; Genomic_DNA.
DR EMBL; AM406671; CAL97012.1; -; Genomic_DNA.
DR RefSeq; WP_011834457.1; NZ_WJVF01000001.1.
DR AlphaFoldDB; A2RIB7; -.
DR SMR; A2RIB7; -.
DR STRING; 416870.llmg_0408; -.
DR EnsemblBacteria; CAL97012; CAL97012; llmg_0408.
DR GeneID; 61108710; -.
DR KEGG; llm:llmg_0408; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_0_9; -.
DR OMA; ACGIPYW; -.
DR PhylomeDB; A2RIB7; -.
DR BioCyc; LLAC416870:LLMG_RS02085-MON; -.
DR BRENDA; 1.6.3.4; 2903.
DR SABIO-RK; A2RIB7; -.
DR Proteomes; UP000000364; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidation;
KW Oxidoreductase; Redox-active center; Translocase.
FT CHAIN 1..446
FT /note="NADH oxidase"
FT /id="PRO_0000292941"
FT ACT_SITE 10
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT ACT_SITE 42
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 7..11
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 109..112
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 178
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 282
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 300
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT BINDING 329
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT MOD_RES 42
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250|UniProtKB:P37062"
FT CONFLICT 11
FT /note="A -> AA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 48872 MW; 1B1FA2FE313D6C03 CRC64;
MKIVVIGTNH AGIATANTLL EQYPGHEIVM IDRNSNMSYL GCGTAIWVGR QIEKPDELFY
AKAEDFEAKG VKILTETEVS EIDFANKKVY AKTKSDDEII EAYDKLVLAT GSRPIIPNLP
GKDLKGIHFL KLFQEGQAID AEFAKEKVKR IAVIGAGYIG TEIAEAAKRR GKEVLLFDAE
NTSLASYYDE EFAKGMDENL AQHGIELHFG ELAKEFKANE EGYVSQIVTN KATYDVDLVI
NCIGFTANSA LASDKLATFK NGAIKVDKHQ QSSDPDVYAV GDVATIYSNA LQDFTYIALA
SNAVRSGIVA GHNIGGKELE SVGVQGSNGI SIFGYNMTST GLSVKAAKKL GLEVSFSDFE
DKQKAWFLHE NNDSVKIRIV YETKSRRIIG AQLASKSEII AGNINMFSLA IQEKKTIDEL
ALLDLFFLPH FNSPYNYMTV AALNAK
