ID A0A1F5WF32_9BACT Unreviewed; 415 AA.
AC A0A1F5WF32;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN ORFNames=A3J56_02725 {ECO:0000313|EMBL:OGF74194.1};
OS Candidatus Giovannonibacteria bacterium RIFCSPHIGHO2_02_FULL_46_20.
OC Bacteria; Candidatus Giovannonibacteria.
OX NCBI_TaxID=1798338 {ECO:0000313|EMBL:OGF74194.1, ECO:0000313|Proteomes:UP000178406};
RN [1] {ECO:0000313|EMBL:OGF74194.1, ECO:0000313|Proteomes:UP000178406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGF74194.1}.
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DR EMBL; MFHQ01000028; OGF74194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5WF32; -.
DR STRING; 1798338.A3J56_02725; -.
DR Proteomes; UP000178406; 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:SF3; EXTERNAL NADH-UBIQUINONE OXIDOREDUCTASE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 202..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..330
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 415 AA; 45761 MW; 335DB3B6A148F7F4 CRC64;
MVKEVVIIGG GFGGVRVAQN LARRARGIHI TLIDKEYYHT FHPALYEIAT ADLPETFRHS
PIEFHKLRSA ASYPLVDIFL RDLNVTVVRG TVTGIDFKNQ KALLESGVMY PYDALVLAVG
SETNYFGIEG LSPHALPLKT LWDALSVRNA LDEAFARTPK QKRLSIVIGG GGFTGCEFAG
ELAFFVKKLE EKHGRQKKST EIIVVEASAA LIGGARVWVR RAAKKRLEAL GITLMLERPI
TKVADSSLFL QDSSAVPFDV LIWTAGVRAN SFTKTCAGIQ LQKNFCMCVD QYLRALPHEN
VFGVGDATYC INDATGTSHP MTATVALKEA EIAAYNIERL FAKKLLIAFV YTPPGFIVPL
GGKYALFDSR LVKISGVLAW ALKHLVALHY WVSLIGLRRG YKVWRGSMGI FIKND
//
