ID A0A1H8UQQ6_9SPHI Unreviewed; 437 AA.
AC A0A1H8UQQ6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN ORFNames=SAMN05428947_106122 {ECO:0000313|EMBL:SEP04908.1};
OS Mucilaginibacter sp. OK283.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1881049 {ECO:0000313|EMBL:SEP04908.1, ECO:0000313|Proteomes:UP000199509};
RN [1] {ECO:0000313|EMBL:SEP04908.1, ECO:0000313|Proteomes:UP000199509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK283 {ECO:0000313|EMBL:SEP04908.1,
RC ECO:0000313|Proteomes:UP000199509};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000864};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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DR EMBL; FODR01000006; SEP04908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8UQQ6; -.
DR STRING; 1881049.SAMN05428947_106122; -.
DR OrthoDB; 9781621at2; -.
DR Proteomes; UP000199509; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR Gene3D; 3.50.50.100; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR43706:SF3; NADH:UBIQUINONE REDUCTASE (NON-ELECTROGENIC); 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 376..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..329
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 437 AA; 48244 MW; D0B61FD4BA54D079 CRC64;
MNTSDSSKFP LVVIVGGGFG GLQVAKKLAD KPVDVLMLDK HNYHTFQPLL YQVAMGGLES
ESIAFSLRKN FSGQKNFRFR IAEVLKVNAE NNTIDTTIGP IAYDYLVIAT GSTTNFFGNH
DIEKFSMPMK SIPEALNLRY SVLQNIEEAL LKTSKDEREA LLTFVLVGAG PTGVELSGSL
AELRNHVLTK DYPELKKEDM KVYLVDFLPK VLGPFSDQAS NAAKDFLTKM GVEVLLGVKV
ESYDGKEIKF EGGKTIRTKN VIWSAGVMGV VPEGIEKGNI ERGNRIKVDS ICRMAGSDNI
FAIGDVAAMI TDETPKGHPG VAQVAIQMGA HVGKTIMQLI NHEPTTPFKY FDKGSLATIG
RNKAVADLGK IRFQGFFAWL VWMFVHLISL LGGRNKVIVF INWVSSYINY NGGTRLIIRK
FEREGLTEDE HLPETVD
//