ID A0A9W6LFF8_9ACTN Unreviewed; 443 AA.
AC A0A9W6LFF8;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 18-JUN-2025, entry version 9.
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:GLI40546.1};
GN ORFNames=GALLR39Z86_03960 {ECO:0000313|EMBL:GLI40546.1};
OS Glycomyces algeriensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Glycomycetales;
OC Glycomycetaceae; Glycomyces.
OX NCBI_TaxID=256037 {ECO:0000313|EMBL:GLI40546.1, ECO:0000313|Proteomes:UP001144313};
RN [1] {ECO:0000313|EMBL:GLI40546.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LLR39Z86 {ECO:0000313|EMBL:GLI40546.1};
RA Sekiguchi Y., Tourlousse D.M.;
RT "Reference genome sequencing for broad-spectrum identification of bacterial
RT and archaeal isolates by mass spectrometry.";
RL Submitted (DEC-2022) 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:GLI40546.1}.
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DR EMBL; BSDT01000001; GLI40546.1; -; Genomic_DNA.
DR Proteomes; UP001144313; 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 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; 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; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 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:UP001144313};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 341..386
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 443 AA; 48329 MW; 1F3B42A98DAC1B50 CRC64;
MSVTVPGPRR PREDALNKLK PVITKRWMSP GAWKLDVYEQ LDGYKALRKA LKYSEGDLIS
FMKESGHRGR GGAGFPVGMK WQFVPDDGQE HYLVVNADEG EPGTCKDLPL MMNDPHSLIE
GIIIASYAIK ASRAFVYVRG EAIHAARRLR NAVREAKEAG YLGKDILGSG FDLEVVIHSG
AGAYICGEET ALLDSLEGKR GQPRLRPPFP ATHGLYNKPT CINNVGSIAA VPHIVLGGAQ
WWKDLGSENA AGTMIYSLSG RVKRPGQYEC SLGTTLRELI ELAGGMEEGH ELKFFTPGGS
STPMLAADSI DVPLDFDNVA KAGSILGTTA VMIFSDQDCP VVSCWRWIKF YAHESCGKCT
PCREGNYWMV RVYERLLSGR GQMGDLKLLE SACKNLLGRS FCGLGDGATS CVTSSLKFFR
QDYLDYIEGH KPAVLDAATI GAH
//
