ID A0A512T160_9MICO Unreviewed; 437 AA.
AC A0A512T160;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 18-JUN-2025, entry version 18.
DE RecName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000256|ARBA:ARBA00019901, ECO:0000256|RuleBase:RU364066};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU364066};
GN Name=nuoF {ECO:0000313|EMBL:GEQ13909.1};
GN ORFNames=KLO01_19560 {ECO:0000313|EMBL:GEQ13909.1};
OS Knoellia locipacati.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Intrasporangiaceae; Knoellia.
OX NCBI_TaxID=882824 {ECO:0000313|EMBL:GEQ13909.1, ECO:0000313|Proteomes:UP000321793};
RN [1] {ECO:0000313|EMBL:GEQ13909.1, ECO:0000313|Proteomes:UP000321793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 109775 {ECO:0000313|EMBL:GEQ13909.1,
RC ECO:0000313|Proteomes:UP000321793};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Knoellia locipacati NBRC 109775.";
RL Submitted (JUL-2019) 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:RU364066}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4
CC H(+)(out); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:132124; Evidence={ECO:0000256|ARBA:ARBA00047712,
CC ECO:0000256|RuleBase:RU364066};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|RuleBase:RU364066};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU364066};
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523, ECO:0000256|RuleBase:RU364066}.
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:GEQ13909.1}.
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DR EMBL; BKBA01000008; GEQ13909.1; -; Genomic_DNA.
DR RefSeq; WP_147064539.1; NZ_BAABDN010000001.1.
DR AlphaFoldDB; A0A512T160; -.
DR OrthoDB; 9805533at2; -.
DR Proteomes; UP000321793; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0045333; P:cellular respiration; IEA:TreeGrafter.
DR FunFam; 1.20.1440.230:FF:000001; Mitochondrial NADH dehydrogenase flavoprotein 1; 1.
DR FunFam; 3.40.50.11540:FF:000001; NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial; 1.
DR FunFam; 3.10.20.600:FF:000003; NADH-quinone oxidoreductase subunit F; 1.
DR Gene3D; 3.10.20.600; -; 1.
DR Gene3D; 6.10.250.1450; -; 1.
DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR InterPro; IPR050837; ComplexI_51kDa_subunit.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR NCBIfam; TIGR01959; nuoF_fam; 1.
DR NCBIfam; NF010120; PRK13596.1; 1.
DR PANTHER; PTHR11780:SF10; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11780; NADH-UBIQUINONE OXIDOREDUCTASE FLAVOPROTEIN 1 NDUFV1; 1.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF10531; SLBB; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU364066};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU364066};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|RuleBase:RU364066};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364066};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364066};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364066};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU364066};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|RuleBase:RU364066};
KW Reference proteome {ECO:0000313|Proteomes:UP000321793};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 329..374
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 437 AA; 47740 MW; EC4D1984681D9A69 CRC64;
MSTTLTPILT KFWDDPQSWT LETYEKNEGY QALKKALAMA PADLVQMTKD SGLRGRGGAG
FPTGMKWGFL PPPDGGPRYL VVNADESEPG TCKDIPLMMA APQFLIEGVA ITSFAIGCNH
AFIYLRGEVV HVYRRLLRAV EEAYAAGHLG KNIHGSGFDL DVTVHAGAGA YICGEETALL
DSLEGRRGQP RLKPPFPAVA GLYARPTVVN NVESIASVPP ILLHGSEWFG DMGTEKSQGF
GIFSLSGHVK NPGQYEAPLG ITLRELLDMA GGMRDPDKAL KFWTPGGSST PLFTAEHLDT
PLDFESVAAA GSMLGTRALQ IFDETTCVVR AVDRWTDFYK HESCGKCTPC REGTWWLKQI
LGRLEHGQGS EEDLDKLLDI CDNILGRSFC ALGDGATSPI TSSIQYFRDE YRAHLTEGRC
PFDSRESTLF HKDRVTA
//
