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Database: UniProt
Entry: A0A0G3CUC5_9GAMM
LinkDB: A0A0G3CUC5_9GAMM
Original site: A0A0G3CUC5_9GAMM 
ID   A0A0G3CUC5_9GAMM        Unreviewed;       140 AA.
AC   A0A0G3CUC5;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=QQ39_12120 {ECO:0000313|EMBL:AKJ42737.1};
OS   Pragia fontium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Pragia.
OX   NCBI_TaxID=82985 {ECO:0000313|EMBL:AKJ42737.1, ECO:0000313|Proteomes:UP000068021};
RN   [1] {ECO:0000313|EMBL:AKJ42737.1, ECO:0000313|Proteomes:UP000068021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=24613 {ECO:0000313|EMBL:AKJ42737.1,
RC   ECO:0000313|Proteomes:UP000068021};
RX   PubMed=26159528;
RA   Snopkova K., Sedlar K., Bosak J., Chaloupkova E., Provaznik I., Smajs D.;
RT   "Complete Genome Sequence of Pragia fontium 24613, an Environmental
RT   Bacterium from the Family Enterobacteriaceae.";
RL   Genome Announc. 3:e00740-15(2015).
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}.
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DR   EMBL; CP010423; AKJ42737.1; -; Genomic_DNA.
DR   RefSeq; WP_047781470.1; NZ_UGTK01000001.1.
DR   STRING; 82985.QQ39_12120; -.
DR   KEGG; pfq:QQ39_12120; -.
DR   PATRIC; fig|82985.3.peg.2536; -.
DR   OrthoDB; 9791970at2; -.
DR   Proteomes; UP000068021; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000068021};
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        95..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
SQ   SEQUENCE   140 AA;  15584 MW;  42F6D0113E6887B4 CRC64;
     MPTSTEVAAH HWAFAVFIVV ALGLCAVMLT AAYFLGGRAR ARTKNTPYES GIDAVGSARL
     RLSAKFYLVA MFFVIFDVEA LYLFAWSVSV RESGWIGFIE AAIFIFVLLA GLFYLVRIGA
     LDWTPQRSKR QIKNNPSNLQ
//
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