ID A0A2A2EWI4_9GAMM Unreviewed; 120 AA.
AC A0A2A2EWI4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=NADH-quinone oxidoreductase subunit {ECO:0000256|RuleBase:RU003639};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003639};
GN ORFNames=CK501_15010 {ECO:0000313|EMBL:PAU77028.1};
OS Halovibrio salipaludis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halovibrio.
OX NCBI_TaxID=2032626 {ECO:0000313|EMBL:PAU77028.1, ECO:0000313|Proteomes:UP000218896};
RN [1] {ECO:0000313|EMBL:PAU77028.1, ECO:0000313|Proteomes:UP000218896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL5-2 {ECO:0000313|EMBL:PAU77028.1,
RC ECO:0000313|Proteomes:UP000218896};
RA Dong X., Zhang G.;
RT "Halovibrio sewagensis sp. nov., isolated from wastewater of high
RT salinity.";
RL Submitted (AUG-2017) 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:PAU77028.1}.
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DR EMBL; NSKD01000010; PAU77028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2EWI4; -.
DR OrthoDB; 9791970at2; -.
DR Proteomes; UP000218896; 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:UP000218896};
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 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 120 AA; 13289 MW; 580EAB02058DCAEE CRC64;
MSALEQYSLL LALVAGIAGT VIGLYGLARA MGLTRREQGK DVPASSGVLS RDPVWGRYHA
RYYGYALLFL AFDMEMAFMY PWAVVYKEVG LVALLDMGVF LAILFLGLLY GWSQGALRRQ
//
