ID A0A0M8YB02_9ACTN Unreviewed; 142 AA.
AC A0A0M8YB02;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=NADH-quinone oxidoreductase subunit {ECO:0000256|RuleBase:RU003639};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003639};
GN ORFNames=ADL06_23760 {ECO:0000313|EMBL:KOX22907.1};
OS Streptomyces sp. NRRL F-6491.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX22907.1, ECO:0000313|Proteomes:UP000037743};
RN [1] {ECO:0000313|EMBL:KOX22907.1, ECO:0000313|Proteomes:UP000037743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX22907.1,
RC ECO:0000313|Proteomes:UP000037743};
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:KOX22907.1}.
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DR EMBL; LGEE01000232; KOX22907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8YB02; -.
DR PATRIC; fig|1519495.3.peg.5064; -.
DR Proteomes; UP000037743; 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; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1.
DR PANTHER; PTHR11058:SF9; 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 Quinone {ECO:0000256|RuleBase:RU003639};
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};
KW Ubiquinone {ECO:0000313|EMBL:KOX22907.1}.
FT TRANSMEM 29..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 142 AA; 15485 MW; F509A45AC2A893ED CRC64;
MGHLDRGADV REPTVVAADA ADYFQTYSVV GLLAVVGVLF VAVAFGAGRL LRPVVPTPEK
LLTYECGVDP VGEGWAHTQV RYYVYAFLYV IFAVDSIFLF PWATVFAAPG YGATTLVEMF
VFLGFLAVGL LYAYKKGVLT WT
//
