NDH_STAEQ
ID NDH_STAEQ Reviewed; 402 AA.
AC Q5HQM1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=SERP0527;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW53923.1; -; Genomic_DNA.
DR RefSeq; WP_002485996.1; NC_002976.3.
DR AlphaFoldDB; Q5HQM1; -.
DR SMR; Q5HQM1; -.
DR STRING; 176279.SERP0527; -.
DR EnsemblBacteria; AAW53923; AAW53923; SERP0527.
DR KEGG; ser:SERP0527; -.
DR eggNOG; COG1252; Bacteria.
DR HOGENOM; CLU_021377_7_2_9; -.
DR OMA; DHCIFLD; -.
DR OrthoDB; 403436at2; -.
DR Proteomes; UP000000531; 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;
KW Reference proteome.
FT CHAIN 1..402
FT /note="Type II NADH:quinone oxidoreductase"
FT /id="PRO_0000287374"
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; 44184 MW; E1E1C4A8D1E314DC CRC64;
MAQDRKKVLV LGAGYAGLQT VTKLQKELSA DAAEITLINK NEYHYESTWL HEASAGTINY
EDLLYPVEKT VNKDKVNFVV AEVTKIDRNA KRVETDKGVY DFDILVVALG FVSETFGIDG
MKEHAFQIEN VLTSRKLSRH IEDKFANYAA SKEKDDKDLS ILVGGAGFTG IEFLGELTDR
IPELCSKYGV DQSKVKLTCV EAAPKMLPMF SDDLVSYAVK YLEDRGVEFK IATPIVACNE
KGFVVEVNGE KQQLEAGTSV WTAGVRGSHL MEESFEGVKR GRVINKQDLT IEGHNDIFVI
GDCSAFIPAG EERPLPTTAQ IAMQQGEHTA SNIKRLLNGE STQDFQYVNR GTVCSLGAND
GVGIVYGRDI AGKKAAFLKK VIDTRAIYKL GGIGLAFKKG KF
