ID   NDH_STAAB               Reviewed;         402 AA.
AC   Q2YWP9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Type II NADH:quinone oxidoreductase {ECO:0000250|UniProtKB:Q2FZV7};
DE            EC=1.6.5.9 {ECO:0000250|UniProtKB:Q2FZV7};
DE   AltName: Full=NDH-2 {ECO:0000250|UniProtKB:Q2FZV7};
GN   OrderedLocusNames=SAB0807;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- FUNCTION: Alternative, nonproton pumping NADH:quinone oxidoreductase
CC       that delivers electrons to the respiratory chain by oxidation of NADH
CC       and reduction of quinones, and contributes to the regeneration of
CC       NAD(+). {ECO:0000250|UniProtKB:Q2FZV7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC         Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC         Evidence={ECO:0000250|UniProtKB:Q2FZV7};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q2FZV7};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q2FZV7};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2FZV7}.
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AJ938182; CAI80495.1; -; Genomic_DNA.
DR   RefSeq; WP_000046084.1; NC_007622.1.
DR   AlphaFoldDB; Q2YWP9; -.
DR   SMR; Q2YWP9; -.
DR   KEGG; sab:SAB0807; -.
DR   HOGENOM; CLU_021377_7_2_9; -.
DR   OMA; DHCIFLD; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   3: Inferred from homology;
KW   Cell membrane; FAD; Flavoprotein; Membrane; NAD; Oxidoreductase.
FT   CHAIN           1..402
FT                   /note="Type II NADH:quinone oxidoreductase"
FT                   /id="PRO_0000287364"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT   BINDING         12..16
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT   BINDING         39..40
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT   BINDING         83
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT   BINDING         302
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT   BINDING         319..320
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
FT   BINDING         379
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FZV7"
SQ   SEQUENCE   402 AA;  44134 MW;  8C8494D008805C50 CRC64;
     MAQDRKKVLV LGAGYAGLQT VTKLQKTIST EEAEITLINK NEYHYEATWL HEASAGTLNY
     EDVLYPVESV LKKDKVNFVQ AEVTKIDRDA KKVETNQGIY DFDILVVALG FVSETFGIEG
     MKDHAFQIEN VITARELSRH IEDKFANYAA SKEKDDNDLS ILVGGAGFTG VEFLGELTDR
     IPELCSKYGV DQNKVKITCV EAAPKMLPMF SEELVNHAVS YLEDRGVEFK IATPIVACNE
     KGFVVEVDGE KQQLNAGTSV WAAGVRGSKL MEESFEGVKR GRIVTKQDLT INGYDNIFVI
     GDCSAFIPAG EERPLPTTAQ IAMQQGESVA KNIKRILNGE STEEFEYVDR GTVCSLGSHD
     GVGMVFGKPI AGKKAAFMKK VIDTRAVFKI GGIGLAFKKG KF