ID A0A172TV04_9BACT Unreviewed; 136 AA.
AC A0A172TV04;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 ORFNames=SY85_11005 {ECO:0000313|EMBL:ANE50951.1};
OS Flavisolibacter tropicus.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavisolibacter.
OX NCBI_TaxID=1492898 {ECO:0000313|EMBL:ANE50951.1, ECO:0000313|Proteomes:UP000077177};
RN [1] {ECO:0000313|Proteomes:UP000077177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCS9 {ECO:0000313|Proteomes:UP000077177};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Flavisolibacter sp./LCS9/ whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANE50951.1, ECO:0000313|Proteomes:UP000077177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCS9 {ECO:0000313|EMBL:ANE50951.1,
RC ECO:0000313|Proteomes:UP000077177};
RX PubMed=27259556; DOI=10.1099/ijsem.0.001207;
RA Lee J.J., Kang M.S., Kim G.S., Lee C.S., Lim S., Lee J., Roh S.H., Kang H.,
RA Ha J.M., Bae S., Jung H.Y., Kim M.K.;
RT "Flavisolibacter tropicus sp. nov., isolated from tropical soil.";
RL Int. J. Syst. Evol. Microbiol. 66:3413-3419(2016).
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}.
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DR EMBL; CP011390; ANE50951.1; -; Genomic_DNA.
DR RefSeq; WP_066404453.1; NZ_CP011390.1.
DR AlphaFoldDB; A0A172TV04; -.
DR STRING; 1492898.SY85_11005; -.
DR KEGG; fla:SY85_11005; -.
DR PATRIC; fig|1492898.3.peg.2374; -.
DR OrthoDB; 9791970at2; -.
DR Proteomes; UP000077177; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000077177};
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 25..46
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT TRANSMEM 104..127
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
SQ SEQUENCE 136 AA; 15203 MW; FB7F3FFE091439E0 CRC64;
MFHLLQADVT RAVANVNSAE SYLPVGLQLL FAIGMIGLLM VVTHLLGPKR QTSDKLATFT
SGIESHGEAR QPVAIKYFLV AILFVLFDVE VIFFYPYAVN FKGLGWSGFW AVLMFVGFFL
CGFIYIIKKG ALDWED
//