NUOF_RICRS
ID NUOF_RICRS Reviewed; 421 AA.
AC A8GQT6; Q8GE74;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=A1G_00895;
OS Rickettsia rickettsii (strain Sheila Smith).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=392021;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TRANSCRIPT ANALYSIS (OPERON
RP STRUCTURE).
RX PubMed=12867468; DOI=10.1128/jb.185.15.4578-4584.2003;
RA Rahman M.S., Simser J.A., Macaluso K.R., Azad A.F.;
RT "Molecular and functional analysis of the lepB gene, encoding a type I
RT signal peptidase from Rickettsia rickettsii and Rickettsia typhi.";
RL J. Bacteriol. 185:4578-4584(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheila Smith;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia rickettsii.";
RL Submitted (SEP-2007) 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. Couples the redox
CC reaction to proton translocation (for every two electrons transferred,
CC four hydrogen ions are translocated across the cytoplasmic membrane),
CC and thus conserves the redox energy in a proton gradient (By
CC 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 -!- MISCELLANEOUS: Belongs to an operon consisting of at least secF-nuoF-
CC lepB-rnc.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AY134668; AAO00970.1; -; Genomic_DNA.
DR EMBL; CP000848; ABV75761.1; -; Genomic_DNA.
DR RefSeq; WP_012150373.1; NC_009882.1.
DR AlphaFoldDB; A8GQT6; -.
DR SMR; A8GQT6; -.
DR EnsemblBacteria; ABV75761; ABV75761; A1G_00895.
DR GeneID; 45538751; -.
DR KEGG; rri:A1G_00895; -.
DR HOGENOM; CLU_014881_0_1_5; -.
DR OMA; CREGTDW; -.
DR Proteomes; UP000006832; Chromosome.
DR GO; GO:0045271; C:respiratory chain complex I; IEA:UniProt.
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 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 InterPro; IPR019554; Soluble_ligand-bd.
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; 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 2: Evidence at transcript level;
KW 4Fe-4S; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; NAD; Quinone;
KW Translocase.
FT CHAIN 1..421
FT /note="NADH-quinone oxidoreductase subunit F"
FT /id="PRO_0000316288"
FT BINDING 54..63
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 166..213
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 347
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 350
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 390
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
SQ SEQUENCE 421 AA; 46102 MW; D57700F4C0755749 CRC64;
MLKEEDKIFT NLHGQQSHDL KSSKKRGDWE NTKALLDKGR DFIVEEVKKS GLRGRGGAGF
STGMKWSFMP KNLEKSCYLV VNADESEPGT CKDRDILRFE PHKLIEGCLL ASFAIGANNC
YIYIRGEFYN EASNIQRALD EAYKEGLIGK NSCGSGFDCN IYLHRGAGAY ICGEETALLE
SLEGKKGMPR LKPPFPAGFG LYGCPTTINN VESIAVVPTI LRRGASWFAG IGKPNNTGTK
IFCISGHVNK PCNVEEAMGI SLKELIEKYA GGVRGGWDNL KAIIPGGSSV PLLPKSLCEV
DMDFDSLRTA GSGLGTGGII VMDQSTDIIY AIARLSKFYM HESCGQCTPC REGTGWMWRV
MMRLVKGNVT KSEIDELLNV TKAIEGHTIC ALGDAAAWPI QGLIRHFRSE IEARIKSYSV
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