NDH_STAES
ID NDH_STAES Reviewed; 402 AA.
AC Q8CPV5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=SE_0635;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04232.1; -; Genomic_DNA.
DR RefSeq; NP_764190.1; NC_004461.1.
DR RefSeq; WP_011082633.1; NZ_WBME01000044.1.
DR AlphaFoldDB; Q8CPV5; -.
DR SMR; Q8CPV5; -.
DR STRING; 176280.SE_0635; -.
DR EnsemblBacteria; AAO04232; AAO04232; SE_0635.
DR KEGG; sep:SE_0635; -.
DR PATRIC; fig|176280.10.peg.608; -.
DR eggNOG; COG1252; Bacteria.
DR HOGENOM; CLU_021377_7_2_9; -.
DR OMA; DHCIFLD; -.
DR Proteomes; UP000001411; Chromosome.
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_0000287373"
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; 44255 MW; 662B59D0D7AD1281 CRC64;
MAQDRKKVLV LGAGYAGLQT VTKLQKELSA DAAEITLINK NEYHYESTWL HEASAGTINY
EDLLYPVEKT VNKNKVNFVV AEVTKIDRNA KRVETDKGVY DFDILVVALG FVSETFGIDG
MKEHAFQIEN VLTSRKLSRH IEDKFANYAA SKEKDDKDLS ILVGGAGFTG IEFLGELTDR
IPELCSKYGV DQSKVKLTCV EAAPKMLPMF SDDLVSYAVK YLEDRGVEFK IATPIVACNE
KGFVVEVNGE KQQLEAGTSV WTAGVRGSHL MEESFEGVKR GRIINKQDLT IEGHNDIFVI
GDCSAFIPAD EERPLPTTAQ IAMQQGEHTA SNIKRLLNGE STQDFQYVNR GTVCSLGAND
GVGIVYGRDI AGKKAAFLKK VIDTRAIYKL GGIGLAFKKG KF