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NDH_STAHJ
ID   NDH_STAHJ               Reviewed;         402 AA.
AC   Q4L4V6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=SH2010;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(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; AP006716; BAE05319.1; -; Genomic_DNA.
DR   RefSeq; WP_011276277.1; NC_007168.1.
DR   AlphaFoldDB; Q4L4V6; -.
DR   SMR; Q4L4V6; -.
DR   STRING; 279808.SH2010; -.
DR   EnsemblBacteria; BAE05319; BAE05319; SH2010.
DR   KEGG; sha:SH2010; -.
DR   eggNOG; COG1252; Bacteria.
DR   HOGENOM; CLU_021377_7_2_9; -.
DR   OMA; DHCIFLD; -.
DR   OrthoDB; 403436at2; -.
DR   Proteomes; UP000000543; 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_0000287375"
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;  44352 MW;  DC71055505F16C43 CRC64;
     MAQDRKKVLV LGAGYAGLQT VTKLQKELSA DEADITLINK NKYHYEATWL HEASAGTLNY
     EDLIYPIESV IKEDKVKFIN AEVTKIDRNA KKVETNHGIY DYDILVVALG FESETFGING
     MKDYAFQIEN IETARKLSRH IEDKFANYAA SKEKDDKDLA ILVGGAGFTG IEFLGELTER
     IPELCNKYGV DQNKVRVTCV EAAPKMLPMF SDELVNYAVN YLEDRGVEFK IATPIVACNE
     KGFVVKINDQ EQQLEAGTAI WAAGVRGSKL MEESFEGVKR GRIVTKQDLT IEGHDDIFVI
     GDVSAFIPAG EERPLPTTAQ IAMQQGEHVA KSIKNILNGQ AATDFEYVDR GTVCSLGAHD
     GVGIVYGRDI TGKKAAFMKK VIDTRAVFKI GGVGLAFKKG KF
 
 
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