NQRF_ALTMA
ID NQRF_ALTMA Reviewed; 303 AA.
AC Q9LCJ3;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 Alteromonas macleodii (Pseudoalteromonas macleodii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=28108;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27126 / DSM 6062 / IAM 12920 / JCM 20772 / LMG 2843 / NBRC
RC 102226 / 107;
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; AB024721; BAA83758.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9LCJ3; -.
DR SMR; Q9LCJ3; -.
DR STRING; 28108.ACZ81_16680; -.
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; 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_0000074488"
FT DOMAIN <1..45
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; 34506 MW; 56CD2E5CB5931131 CRC64;
GGSCGQCRVD VHSGGGEILP TELDHITKGE AREGCRLSCQ VAIKQDMEIE LEESVFGVKK
WDCEVISNDN KATFIKELKL KIPNGESVPF RAGGYIQIEA PAHHVKYKEF DIPEEYRGDW
ERFGFFDIES KVDEETIRAY SMANYPEEEG IIMLNVRIAT PPPNNLSLPA GKMSSYIWSL
KEGDKATISG PFGEFFAKET ENEMVFVGGG AGMAPMRSHI FDQLRRLKSK RKMSFWYGAR
SLREMFYTED FDELAAENDN FEWHVALSDP QPEDNWEGYT GFIHQVLLEN YLKDHPAPED
CEY
