ID   A0A1G2DAY8_9BACT        Unreviewed;       419 AA.
AC   A0A1G2DAY8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE            EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN   ORFNames=A3C93_01235 {ECO:0000313|EMBL:OGZ10703.1};
OS   Candidatus Lloydbacteria bacterium RIFCSPHIGHO2_02_FULL_54_17.
OC   Bacteria; Candidatus Lloydbacteria.
OX   NCBI_TaxID=1798664 {ECO:0000313|EMBL:OGZ10703.1, ECO:0000313|Proteomes:UP000178636};
RN   [1] {ECO:0000313|EMBL:OGZ10703.1, ECO:0000313|Proteomes:UP000178636}
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:OGZ10703.1}.
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DR   EMBL; MHLO01000047; OGZ10703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2DAY8; -.
DR   STRING; 1798664.A3C93_01235; -.
DR   Proteomes; UP000178636; Unassembled WGS sequence.
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; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          5..304
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   419 AA;  46406 MW;  340CB98D1C9DB4B4 CRC64;
     MEHKRILIVG GGFAGISAAL VLDRKRLPGV TVTLITERPH FEYHAALYRL VTGSSPLEVC
     IPLREIFAEK NVEVVEDRIT ELRRDQRTVV GFSGAEYRYD HLVLALGSET NYFGIPGLKE
     YSHGMKSVTE ALRLKQHITE ALLTCKVDFA NKVEQICDAN FVVVGAGATG VEMAGELIVY
     ARKLALEHGV DPSLISVELI EGAGKILPAL PAAFTGRIEH HLRGLGVNIF LNRTIEREEC
     EEIFLRDMKM RTKTVIWTAG VRAAHLYEAW GLPIDKRGKV AVDGYLRLKD DARVFVAGDG
     AATIYSGWAQ TALYDGKYIA HVIATHLRSD LGMSHETNVT LPLYRPKPPV NAIPAGPEWA
     GVLWGGMRFY GRVGWWLRRL ADLQIFLRLL PVSKAWKAFK NGSSICETCS VCSVEKTAP
//