ID NUOA1_PSEAE Reviewed; 132 AA.
AC Q9I2L4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=NADH-quinone oxidoreductase subunit A 1 {ECO:0000255|HAMAP-Rule:MF_01394};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01394};
DE AltName: Full=NADH dehydrogenase I subunit A 1 {ECO:0000255|HAMAP-Rule:MF_01394};
DE AltName: Full=NDH-1 subunit A 1 {ECO:0000255|HAMAP-Rule:MF_01394};
DE AltName: Full=NUO1 1 {ECO:0000255|HAMAP-Rule:MF_01394};
GN Name=nuoA1 {ECO:0000255|HAMAP-Rule:MF_01394}; OrderedLocusNames=PA1883;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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:0000255|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:0000255|HAMAP-Rule:MF_01394};
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:0000255|HAMAP-Rule:MF_01394}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01394}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01394}.
CC -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01394}.
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DR EMBL; AE004091; AAG05272.1; -; Genomic_DNA.
DR PIR; D83410; D83410.
DR RefSeq; NP_250574.1; NC_002516.2.
DR RefSeq; WP_003088123.1; NZ_QZGE01000003.1.
DR AlphaFoldDB; Q9I2L4; -.
DR SMR; Q9I2L4; -.
DR STRING; 208964.PA1883; -.
DR PaxDb; 208964-PA1883; -.
DR DNASU; 881501; -.
DR GeneID; 881501; -.
DR KEGG; pae:PA1883; -.
DR PATRIC; fig|208964.12.peg.1960; -.
DR PseudoCAP; PA1883; -.
DR HOGENOM; CLU_119549_2_1_6; -.
DR InParanoid; Q9I2L4; -.
DR OrthoDB; 9791970at2; -.
DR PhylomeDB; Q9I2L4; -.
DR BioCyc; PAER208964:G1FZ6-1923-MONOMER; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
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 inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..132
FT /note="NADH-quinone oxidoreductase subunit A 1"
FT /id="PRO_0000362733"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
SQ SEQUENCE 132 AA; 14713 MW; 8DBEE0B84EC59B2F CRC64;
MYASFAPATW ALLAYLFGAL ALCLLMLGLG RVLGGRSHGR AKNLPFESGV DSTGSSRLRF
SVKYALVAML FVIFGIEMPF LYLWAVSLRE NGWAGFVEAT LFVSLLLVGL FYLHRVGALD
WSPERRRKKP HD
//
