ID NQRF_PHOPO Reviewed; 303 AA.
AC Q9LCJ1;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit F;
DE Short=Na(+)-NQR subunit F;
DE Short=Na(+)-translocating NQR subunit F;
DE EC=7.2.1.1 {ECO:0000250|UniProtKB:Q56584};
DE AltName: Full=NQR complex subunit F;
DE AltName: Full=NQR-1 subunit F;
DE Flags: Fragment;
GN Name=nqrF; Synonyms=nqr6;
OS Photobacterium phosphoreum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=659;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 20393 / IAM 12085;
RX PubMed=10779868; DOI=10.1139/w00-006;
RA Kato S., Yumoto I.;
RT "Detection of the Na(+)-translocating NADH-quinone reductase in marine
RT bacteria using a PCR technique.";
RL Can. J. Microbiol. 46:325-332(2000).
CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to
CC ubiquinol by two successive reactions, coupled with the transport of
CC Na(+) ions from the cytoplasm to the periplasm. The first step is
CC catalyzed by NqrF, which accepts electrons from NADH and reduces
CC ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway.
CC {ECO:0000250|UniProtKB:Q56584}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n
CC Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-COMP:9565,
CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389,
CC ChEBI:CHEBI:17976, ChEBI:CHEBI:29101, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=7.2.1.1;
CC Evidence={ECO:0000250|UniProtKB:Q56584};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:A5F5Y4};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:A5F5Y4};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:A5F5Y4};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000250|UniProtKB:Q56584}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NqrF family. {ECO:0000305}.
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DR EMBL; AB024724; BAA83761.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9LCJ1; -.
DR SMR; Q9LCJ1; -.
DR STRING; 659.AYY26_05535; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06188; NADH_quinone_reductase; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR010205; NqrF.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR NCBIfam; TIGR01941; nqrF; 1.
DR PANTHER; PTHR43644; NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR43644:SF1; NAD(P)H-FLAVIN REDUCTASE; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Cell inner membrane; Cell membrane; FAD; Flavoprotein;
KW Ion transport; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; Sodium;
KW Sodium transport; Translocase; Transport; Ubiquinone.
FT CHAIN <1..>303
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT F"
FT /id="PRO_0000074500"
FT DOMAIN <1..55
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 58..198
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 201..>303
FT /note="Catalytic"
FT BINDING 4
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 7
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 39
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT NON_TER 1
FT NON_TER 303
SQ SEQUENCE 303 AA; 34516 MW; 57396CC41F020FC5 CRC64;
GGSCGQCRVK VKSGGGDILP TELDHISKGE AREGERLACQ VNVKSDMDIE LPEEIFGVKK
WECSVISNDN KATFIKELKL QIPDGETVPF RAGGYIQIEA PAHHIKYSDF DVPEEYRGDW
DKFNLFRYES KVDEDIIRAY SMANYPEEFG IIMLNVRIAT PPPNNPDVAP GQMSSFIWSL
KEGDKCTISG PFGEFFAKDT DNEMVFVGGG AGMAPMRSHI FDQLKRLHSK RKMSYWYGAR
SKREMFYEED FDALAAENPN FVWHCALSDP QPEDNWDGYT GFIHNVLYEN YLRDHEAPED
CEY
//
