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Database: UniProt
Entry: A0A1A3PI78_9MYCO
LinkDB: A0A1A3PI78_9MYCO
Original site: A0A1A3PI78_9MYCO 
ID   A0A1A3PI78_9MYCO        Unreviewed;       125 AA.
AC   A0A1A3PI78;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=A5658_02005 {ECO:0000313|EMBL:OBK33440.1};
OS   Mycobacterium sp. 1245111.1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834073 {ECO:0000313|EMBL:OBK33440.1, ECO:0000313|Proteomes:UP000092232};
RN   [1] {ECO:0000313|EMBL:OBK33440.1, ECO:0000313|Proteomes:UP000092232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1245111.1 {ECO:0000313|EMBL:OBK33440.1,
RC   ECO:0000313|Proteomes:UP000092232};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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}.
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:OBK33440.1}.
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DR   EMBL; LZLV01000143; OBK33440.1; -; Genomic_DNA.
DR   RefSeq; WP_067340608.1; NZ_LZLV01000143.1.
DR   AlphaFoldDB; A0A1A3PI78; -.
DR   STRING; 1834073.A5658_02005; -.
DR   OrthoDB; 9791970at2; -.
DR   Proteomes; UP000092232; 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: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   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..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT   TRANSMEM        67..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT   TRANSMEM        94..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
SQ   SEQUENCE   125 AA;  13906 MW;  5AEDA2F87FF6BB5B CRC64;
     MNLYLPILVL GGIAAAFALG SVALAQITGP SRYNRAKLEA YECGIEPSDQ PANAPHAGSG
     QRFPVKYYLT AMLFIVFDIE IVFLYPWAVS YDQLGLFALI EMVVFMLTVF VAYAYVWRRG
     GLTWD
//
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