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