ID A0A1B9DPP1_9FLAO Unreviewed; 121 AA.
AC A0A1B9DPP1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=NADH-quinone oxidoreductase subunit A {ECO:0000256|HAMAP-Rule:MF_01394};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01394};
DE AltName: Full=NADH dehydrogenase I subunit A {ECO:0000256|HAMAP-Rule:MF_01394};
DE AltName: Full=NDH-1 subunit A {ECO:0000256|HAMAP-Rule:MF_01394};
DE AltName: Full=NUO1 {ECO:0000256|HAMAP-Rule:MF_01394};
GN Name=nuoA {ECO:0000256|HAMAP-Rule:MF_01394,
GN ECO:0000313|EMBL:GEL10673.1};
GN ORFNames=FBGL_10410 {ECO:0000313|EMBL:OCB71631.1}, FGL01_14120
GN {ECO:0000313|EMBL:GEL10673.1};
OS Flavobacterium glycines.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=551990 {ECO:0000313|EMBL:OCB71631.1, ECO:0000313|Proteomes:UP000093226};
RN [1] {ECO:0000313|Proteomes:UP000093226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105008 {ECO:0000313|Proteomes:UP000093226};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Paenibacillus glacialis DSM 22343.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OCB71631.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 105008 {ECO:0000313|EMBL:OCB71631.1};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GEL10673.1, ECO:0000313|Proteomes:UP000321579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105008 {ECO:0000313|EMBL:GEL10673.1,
RC ECO:0000313|Proteomes:UP000321579};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Flavobacterium glycines NBRC 105008.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be a
CC menaquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_01394}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01394,
CC ECO:0000256|RuleBase:RU003639};
CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H,
CC J, K, L, M, N constitute the membrane sector of the complex.
CC {ECO:0000256|HAMAP-Rule:MF_01394}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01394,
CC ECO:0000256|RuleBase:RU003639}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639}.
CC -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC {ECO:0000256|ARBA:ARBA00008472, ECO:0000256|HAMAP-Rule:MF_01394,
CC ECO:0000256|RuleBase:RU003639}.
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:OCB71631.1}.
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DR EMBL; BJVF01000001; GEL10673.1; -; Genomic_DNA.
DR EMBL; LVEO01000018; OCB71631.1; -; Genomic_DNA.
DR RefSeq; WP_066328339.1; NZ_LVEO01000018.1.
DR AlphaFoldDB; A0A1B9DPP1; -.
DR STRING; 551990.SAMN05192550_0285; -.
DR OrthoDB; 9791970at2; -.
DR Proteomes; UP000093226; Unassembled WGS sequence.
DR Proteomes; UP000321579; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1610; NADH:ubiquinone/plastoquinone oxidoreductase, chain 3; 1.
DR HAMAP; MF_01394; NDH1_NuoA; 1.
DR InterPro; IPR023043; NAD(P)H_OxRDtase_bac/plastid.
DR InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR PANTHER; PTHR11058:SF22; NADH-QUINONE OXIDOREDUCTASE SUBUNIT A; 1.
DR PANTHER; PTHR11058; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1.
DR Pfam; PF00507; Oxidored_q4; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01394};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01394};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_01394};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01394};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01394};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01394}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT TRANSMEM 95..113
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
SQ SEQUENCE 121 AA; 13796 MW; 743FD7C934492F77 CRC64;
MQSEQFNYLP ILMQALLAIG FVVGTIFISG KLGPKRKSAS KDKNFECGIE SVGNARIPFS
VKYFLVAILF VLFDVEVIFL YPWAINFKEL GLEGMIKMIV FMALLLVGFF YIIKKKALEW
E
//
