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NUOF_PSEAE
ID   NUOF_PSEAE              Reviewed;         448 AA.
AC   Q9I0J7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=NADH-quinone oxidoreductase subunit F;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit F;
DE   AltName: Full=NDH-1 subunit F;
GN   Name=nuoF; OrderedLocusNames=PA2641;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305};
CC       Note=Binds 1 FMN. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC   -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F, and G
CC       constitute the peripheral sector of the complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AE004091; AAG06029.1; -; Genomic_DNA.
DR   PIR; F83316; F83316.
DR   RefSeq; NP_251331.1; NC_002516.2.
DR   RefSeq; WP_003097674.1; NZ_QZGE01000008.1.
DR   AlphaFoldDB; Q9I0J7; -.
DR   SMR; Q9I0J7; -.
DR   STRING; 287.DR97_5321; -.
DR   PaxDb; Q9I0J7; -.
DR   PRIDE; Q9I0J7; -.
DR   EnsemblBacteria; AAG06029; AAG06029; PA2641.
DR   GeneID; 882348; -.
DR   KEGG; pae:PA2641; -.
DR   PATRIC; fig|208964.12.peg.2763; -.
DR   PseudoCAP; PA2641; -.
DR   HOGENOM; CLU_014881_0_1_6; -.
DR   InParanoid; Q9I0J7; -.
DR   OMA; CDDVIMD; -.
DR   PhylomeDB; Q9I0J7; -.
DR   BioCyc; PAER208964:G1FZ6-2681-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:InterPro.
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; IBA:GO_Central.
DR   Gene3D; 1.20.1440.230; -; 1.
DR   Gene3D; 3.40.50.11540; -; 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   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   SMART; SM00928; NADH_4Fe-4S; 1.
DR   SUPFAM; SSF140490; SSF140490; 1.
DR   SUPFAM; SSF142019; SSF142019; 1.
DR   TIGRFAMs; TIGR01959; nuoF_fam; 1.
DR   PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; NAD; Quinone;
KW   Reference proteome; Translocase; Ubiquinone.
FT   CHAIN           1..448
FT                   /note="NADH-quinone oxidoreductase subunit F"
FT                   /id="PRO_0000287849"
FT   BINDING         69..78
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         182..229
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         361
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         364
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         367
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         408
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   448 AA;  48679 MW;  6820CA50DA9A656A CRC64;
     MTLTSIGPAN RMARSAETHP LTWRLREDAQ PVWLEEYQSK DGYAAARKAL TQMAQDDIVQ
     TVKDSGLKGR GGAGFPTGVK WGLMPKDESL NIRYLLCNAD EMEPNTWKDR MLMEQLPHLL
     VEGMLISARA LKAYRGYIFL RGEYVDAARN LNRAIDEAKA AGLLGKNILG SGFDFELFVH
     TGAGRYICGE ETALINSLEG RRANPRSKPP FPAAVGVWGK PTCVNNVETL CNVPAIVGNG
     VDWYKTLARP GSEDMGTKLM GFSGKVKNPG LWELPFGVSA RELFEDYAGG MRDGFQLKAW
     QPGGAGTGFL LPEHLDAQMF AGGIAKVGTR MGTGLAMAVD DSINMVSLLR NMEEFFARES
     CGWCTPCRDG LPWSVKLLRA LERGEGQPGD LETLEQLVNF LGPGKTFCAH APGAVEPLGS
     ALKYFRAEFE AGISRQPSAA PRPATVGA
 
 
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