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Database: UniProt
Entry: A0A1I6L822_9BACT
LinkDB: A0A1I6L822_9BACT
Original site: A0A1I6L822_9BACT 
ID   A0A1I6L822_9BACT        Unreviewed;       123 AA.
AC   A0A1I6L822;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-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=SAMN05421771_0398 {ECO:0000313|EMBL:SFR99626.1};
OS   Granulicella pectinivorans.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=474950 {ECO:0000313|EMBL:SFR99626.1, ECO:0000313|Proteomes:UP000199024};
RN   [1] {ECO:0000313|EMBL:SFR99626.1, ECO:0000313|Proteomes:UP000199024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21001 {ECO:0000313|EMBL:SFR99626.1,
RC   ECO:0000313|Proteomes:UP000199024};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOZL01000001; SFR99626.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6L822; -.
DR   STRING; 474950.SAMN05421771_0398; -.
DR   OrthoDB; 9791970at2; -.
DR   Proteomes; UP000199024; 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:UP000199024};
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..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   123 AA;  13564 MW;  C35D9307EBF25724 CRC64;
     MGNVSYLPIL VLLLGAVGFA VAPLALAWLW AKKFSPAKPG RSKNAVYECG LESSDDAWVQ
     FKPGYYLYAI LFLVFDVEVV FLLPFATALT GFGLGECLAV FVFLFLLIAG LAWAWHKKVL
     TWT
//
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