NQRF_PSEHA
ID NQRF_PSEHA Reviewed; 303 AA.
AC Q9LCJ4;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
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 Pseudoalteromonas haloplanktis (Alteromonas haloplanktis).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=228;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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; AB024720; BAA83757.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9LCJ4; -.
DR SMR; Q9LCJ4; -.
DR eggNOG; COG2871; Bacteria.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
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:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
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 Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 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 Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR TIGRFAMs; TIGR01941; nqrF; 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_0000074487"
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; 34463 MW; BA585741D1F86E2A CRC64;
GGSCGQCRVH IKEGGGDILP TELDHISKGE AREGCRLACQ VNVKNDMEIE LEESIFGVKK
WDCEVISNDN KATFIKELKL QIPDGESVPF RAGGYIQIEA PAHHVKYADF DIPEEYRGDW
NHFGFFDLES KVDEETIRAY SMANYPEEEG IIMLNVRIAT PPPRNLSLPC GKMSSYIWSL
KEGDKVTISG PFGEFFAKDT DAEMVFVGGG AGMAPMRSHI FDQLKRLNSK RKISFWYGAR
SKREMFYVED FDGLAEQNEN FVWHTALSDP QPEDNWEGYT GFIHNVLFEN YLKDHEAPED
CEY
