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Database: UniProt
Entry: A0A1T1HJS3_9PSED
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ID   A0A1T1HJS3_9PSED        Unreviewed;       137 AA.
AC   A0A1T1HJS3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=MF4836_31250 {ECO:0000313|EMBL:OOV90114.1};
OS   Pseudomonas sp. MF4836.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1960827 {ECO:0000313|EMBL:OOV90114.1, ECO:0000313|Proteomes:UP000190183};
RN   [1] {ECO:0000313|Proteomes:UP000190183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MF4836 {ECO:0000313|Proteomes:UP000190183};
RA   Fagerlund A.;
RT   "Genome sequencing of bacteria from food industry.";
RL   Submitted (FEB-2017) 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
CC       ubiquinone. 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 13 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:OOV90114.1}.
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DR   EMBL; MVOL01000019; OOV90114.1; -; Genomic_DNA.
DR   RefSeq; WP_003223812.1; NZ_MVOL01000019.1.
DR   AlphaFoldDB; A0A1T1HJS3; -.
DR   SMR; A0A1T1HJS3; -.
DR   STRING; 1960827.MF4836_31250; -.
DR   GeneID; 75525491; -.
DR   Proteomes; UP000190183; 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:SF21; 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|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   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|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_01394};
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};
KW   Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|HAMAP-
KW   Rule:MF_01394}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT   TRANSMEM        66..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT   TRANSMEM        101..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
SQ   SEQUENCE   137 AA;  15090 MW;  4E83EF10E04C504E CRC64;
     MPEATGLMAH NWGFAIFLLG VVGLCAFMLG VSSLLGSKAW GRSKNEPFES GMLPTGGARL
     RLSAKFYLVA MLFVIFDIEA LFLFAWSVSV RESGWTGFVE ALVFIAILLA GLVYLFRVGA
     LDWAPEARRK RQAKLKQ
//
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