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Database: UniProt
Entry: M1LUH1_9PROT
LinkDB: M1LUH1_9PROT
Original site: M1LUH1_9PROT 
ID   M1LUH1_9PROT            Unreviewed;       115 AA.
AC   M1LUH1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   03-MAY-2023, entry version 38.
DE   RecName: Full=NADH-quinone oxidoreductase subunit {ECO:0000256|RuleBase:RU003639};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU003639};
GN   ORFNames=ST1E_0885 {ECO:0000313|EMBL:AGF49207.1};
OS   Candidatus Kinetoplastibacterium galatii TCC219.
OC   Bacteria; Pseudomonadota; Betaproteobacteria;
OC   Candidatus Kinetoplastibacterium.
OX   NCBI_TaxID=1208921 {ECO:0000313|EMBL:AGF49207.1, ECO:0000313|Proteomes:UP000011658};
RN   [1] {ECO:0000313|EMBL:AGF49207.1, ECO:0000313|Proteomes:UP000011658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCC219 {ECO:0000313|EMBL:AGF49207.1,
RC   ECO:0000313|Proteomes:UP000011658};
RX   PubMed=23345457;
RA   Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA   Teixeira M.M., Camargo E.P., Buck G.A.;
RT   "Genome evolution and phylogenomic analysis of candidatus
RT   kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT   and angomonas.";
RL   Genome Biol. Evol. 5:338-350(2013).
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}.
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DR   EMBL; CP003806; AGF49207.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1LUH1; -.
DR   STRING; 1208921.ST1E_0885; -.
DR   KEGG; kga:ST1E_0885; -.
DR   PATRIC; fig|1208921.3.peg.493; -.
DR   eggNOG; COG0838; Bacteria.
DR   HOGENOM; CLU_119549_3_1_4; -.
DR   Proteomes; UP000011658; Chromosome.
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   Oxidoreductase {ECO:0000313|EMBL:AGF49207.1};
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}.
FT   TRANSMEM        6..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        61..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   115 AA;  13346 MW;  3C897B62F049613E CRC64;
     MNLQQYFSVL LFILVSIIIG LGLLLVGYLL SPKKYTEEKS SPYECGFENF GDARMQFDIR
     YYLVAILFIL FDLEIAFLFP WAIVQDLIGM EGFIAVMLFL FILFIGFFMN GRKVL
//
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