ID A0A0X3RXA3_9ACTN Unreviewed; 145 AA.
AC A0A0X3RXA3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, 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=ADL25_42645 {ECO:0000313|EMBL:KUJ34051.1};
OS Streptomyces sp. NRRL F-5122.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ34051.1, ECO:0000313|Proteomes:UP000054048};
RN [1] {ECO:0000313|Proteomes:UP000054048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-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:KUJ34051.1}.
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DR EMBL; LMWH01000293; KUJ34051.1; -; Genomic_DNA.
DR RefSeq; WP_059133375.1; NZ_LMWH01000293.1.
DR AlphaFoldDB; A0A0X3RXA3; -.
DR OrthoDB; 3747048at2; -.
DR Proteomes; UP000054048; 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 Reference proteome {ECO:0000313|Proteomes:UP000054048};
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:KUJ34051.1}.
FT TRANSMEM 30..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 145 AA; 15519 MW; 5AD9A86CBFFB816A CRC64;
MAETGNVGNG STAGAVHTGN VVAADYFQSY SVVGLLAVVG VLFVAVAFGA GRLLRPVVPT
PEKLLTYECG VDPVGEGWAH TQVRYYVYAF LYVIFAVDSI FLFPWATVFA APGYGATTLV
EMFIFLGFLA VGLLYAYKKG VLTWT
//
