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Database: UniProt
Entry: A0A0D1L038_9MYCO
LinkDB: A0A0D1L038_9MYCO
Original site: A0A0D1L038_9MYCO 
ID   A0A0D1L038_9MYCO        Unreviewed;       124 AA.
AC   A0A0D1L038;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-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=TL10_24485 {ECO:0000313|EMBL:KIU14440.1};
OS   Mycolicibacterium llatzerense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=280871 {ECO:0000313|EMBL:KIU14440.1, ECO:0000313|Proteomes:UP000032221};
RN   [1] {ECO:0000313|EMBL:KIU14440.1, ECO:0000313|Proteomes:UP000032221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLUC14 {ECO:0000313|EMBL:KIU14440.1,
RC   ECO:0000313|Proteomes:UP000032221};
RA   Greninger A.L., Langelier C., Cunningham G., Chiu C.Y., Miller S.;
RT   "Genome sequence of Mycobacterium llatzerense and Mycobacterium immunogenum
RT   recovered from brain abscess.";
RL   Submitted (JAN-2015) 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:KIU14440.1}.
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DR   EMBL; JXST01000044; KIU14440.1; -; Genomic_DNA.
DR   RefSeq; WP_043400785.1; NZ_LXSC01000040.1.
DR   AlphaFoldDB; A0A0D1L038; -.
DR   STRING; 280871.TL10_24485; -.
DR   PATRIC; fig|280871.6.peg.5075; -.
DR   OrthoDB; 9791970at2; -.
DR   Proteomes; UP000032221; 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   Oxidoreductase {ECO:0000313|EMBL:KIU14440.1};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032221};
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        66..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
FT   TRANSMEM        93..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01394"
SQ   SEQUENCE   124 AA;  13806 MW;  89CF0B6B32D8266E CRC64;
     MNVYIPILVL GAIAAAFAVG SVGIALVIGP RRYNRAKLEA YECGIEPMAP GSPGHETTGQ
     RFPVKYYLTA MLFIVFDIEI VFLYPWAVSF ESLGVFAVVE MLLFMLTVFV AYAYIWRRGG
     LSWD
//
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