NUOA_GEOTN
ID NUOA_GEOTN Reviewed; 122 AA.
AC A4ITI7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=NADH-quinone oxidoreductase subunit A {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 {ECO:0000255|HAMAP-Rule:MF_01394};
DE AltName: Full=NDH-1 subunit A {ECO:0000255|HAMAP-Rule:MF_01394};
DE AltName: Full=NUO1 {ECO:0000255|HAMAP-Rule:MF_01394};
GN Name=nuoA {ECO:0000255|HAMAP-Rule:MF_01394}; OrderedLocusNames=GTNG_3302;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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: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 14 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 membrane {ECO:0000255|HAMAP-Rule:MF_01394};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01394}.
CC -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01394}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000557; ABO68641.1; -; Genomic_DNA.
DR RefSeq; WP_008880691.1; NC_009328.1.
DR AlphaFoldDB; A4ITI7; -.
DR SMR; A4ITI7; -.
DR STRING; 420246.GTNG_3302; -.
DR EnsemblBacteria; ABO68641; ABO68641; GTNG_3302.
DR KEGG; gtn:GTNG_3302; -.
DR eggNOG; COG0838; Bacteria.
DR HOGENOM; CLU_119549_1_1_9; -.
DR OMA; RFPVKYY; -.
DR OrthoDB; 1748431at2; -.
DR Proteomes; UP000001578; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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; PTHR11058; 1.
DR Pfam; PF00507; Oxidored_q4; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; NAD; Quinone; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..122
FT /note="NADH-quinone oxidoreductase subunit A"
FT /id="PRO_0000362688"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
SQ SEQUENCE 122 AA; 14189 MW; 977359A3E19A49A6 CRC64;
MSNIYANSYL IVFVFLCLGV LLPIGALTIG RWLRPNVPDE AKATTYESGN IPFHDSRIQF
QVRYYLFALL FVIFDVETVF LYPWAVVYDQ LGLFALVEMI IFIVLLAIGL IYAWKKKVLR
WM