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Database: UniProt
Entry: A0A0M8XBH5_9ACTN
LinkDB: A0A0M8XBH5_9ACTN
Original site: A0A0M8XBH5_9ACTN 
ID   A0A0M8XBH5_9ACTN        Unreviewed;       110 AA.
AC   A0A0M8XBH5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=NADH-quinone oxidoreductase subunit {ECO:0000256|RuleBase:RU003639};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU003639};
GN   ORFNames=ADL04_13885 {ECO:0000313|EMBL:KOX01385.1};
OS   Streptomyces sp. NRRL B-3648.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOX01385.1, ECO:0000313|Proteomes:UP000037702};
RN   [1] {ECO:0000313|EMBL:KOX01385.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOX01385.1};
RA   Noorani M.;
RL   Submitted (JUL-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.
CC       {ECO:0000256|RuleBase:RU003639}.
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|RuleBase:RU003639};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU003639};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003639}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC       {ECO:0000256|ARBA:ARBA00008472, 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:KOX01385.1}.
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DR   EMBL; LGDZ01000141; KOX01385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8XBH5; -.
DR   PATRIC; fig|1519493.3.peg.2974; -.
DR   Proteomes; UP000037702; 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   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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   NAD {ECO:0000256|RuleBase:RU003639};
KW   Oxidoreductase {ECO:0000313|EMBL:KOX01385.1};
KW   Quinone {ECO:0000256|RuleBase:RU003639};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037702};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003639};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   110 AA;  12287 MW;  2379EE374D3A88B1 CRC64;
     MGALGAGFAI FSVVMATLIG PKRYNRAKLE AYECGIEPTP TPAGGGRFPI KYYLTAMLFI
     VFDIEIVFLY PWAVTFDALG IFGLVEMLLF VLTVFVAYAY VWRRGGLEWD
//
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