ID A0A0M9CDL0_9ACTN Unreviewed; 489 AA.
AC A0A0M9CDL0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN ORFNames=ISGA_05880 {ECO:0000313|EMBL:KOY50089.1};
OS Gordonia sp. NB41Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=875808 {ECO:0000313|EMBL:KOY50089.1, ECO:0000313|Proteomes:UP000011989};
RN [1] {ECO:0000313|EMBL:KOY50089.1, ECO:0000313|Proteomes:UP000011989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB4-1Y {ECO:0000313|EMBL:KOY50089.1,
RC ECO:0000313|Proteomes:UP000011989};
RX PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL Microbiology 159:1618-1628(2013).
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:KOY50089.1}.
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DR EMBL; APHK02000002; KOY50089.1; -; Genomic_DNA.
DR RefSeq; WP_053776008.1; NZ_CP132196.1.
DR AlphaFoldDB; A0A0M9CDL0; -.
DR STRING; 1241906.ISGA_05880; -.
DR OrthoDB; 9781621at2; -.
DR Proteomes; UP000011989; 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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000011989};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 392..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..336
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT REGION 458..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 52079 MW; 29B2AFA2E7CD3838 CRC64;
MSSPTPTSAR PHVVIIGSGF GGLFAAQRLA KADVDVTLIA KTTHHLFQPM LYQVATGIVA
EGEIAPATRV VLRKQKNATV LMGDVFGIDL AGKKVTSRLL ERITVTPFDK LILAAGADQS
YFGNDHFAEY APGMKTIDHA LELRGRILGA FEQAELSDDP EERARLLTFV VVGAGPTGVE
LAGQIAEMSD KTLKGAFRNI DPTEARVILL DAAPAVLPPF GPKLGQKAAA RLEKLGVEIQ
LNAMVVDLDY DGLVVKEKDG STRRIESQCK VWSAGVQASP LGKQLSEQSG VELDRAGRVK
VGPDLTIPGN PDVFVVGDMM AVDGVPGVAQ GAIQGGRYAA DAIKAELKGQ TPDQRKPFSY
YDKGSMATIS RFSAVMQVPI PGTKKKFETE GYFAWLGWLA LHLVYLVGFR NRLNTLVNWF
FAFSTRGRTQ LAVTEQQVYA RTAIGQLSEL ERKTIAEVEA DSAGADDPTG SGPDGAGAKG
AASKDAAAG
//
