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Database: UniProt
Entry: A0A1J0VRB2_9NOCA
LinkDB: A0A1J0VRB2_9NOCA
Original site: A0A1J0VRB2_9NOCA 
ID   A0A1J0VRB2_9NOCA        Unreviewed;       126 AA.
AC   A0A1J0VRB2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=BOX37_12170 {ECO:0000313|EMBL:APE34587.1};
OS   Nocardia mangyaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=2213200 {ECO:0000313|EMBL:APE34587.1, ECO:0000313|Proteomes:UP000183810};
RN   [1] {ECO:0000313|EMBL:APE34587.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y48 {ECO:0000313|EMBL:APE34587.1};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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 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; CP018082; APE34587.1; -; Genomic_DNA.
DR   RefSeq; WP_071927770.1; NZ_JAUMIP010000014.1.
DR   AlphaFoldDB; A0A1J0VRB2; -.
DR   KEGG; nsl:BOX37_12170; -.
DR   OrthoDB; 9791970at2; -.
DR   Proteomes; UP000183810; 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:UP000183810};
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        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT   TRANSMEM        68..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT   TRANSMEM        95..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
SQ   SEQUENCE   126 AA;  13702 MW;  57A29E9A9782A4A2 CRC64;
     MNTEVPALVL GAIAAAFAVF SVAMAALVGP KRYNRAKLEP YECGIEPTPH AIAGGPGNAG
     GQRFPVKYYL TAMLFIIFDI EIVFLYPWAV HFDALGLFGL AAMALFIVNV SVAYAYEWRR
     GGLSWE
//
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