NQRF_VIBC3
ID NQRF_VIBC3 Reviewed; 408 AA.
AC A5F5Y4; C3M414;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit F {ECO:0000255|HAMAP-Rule:MF_00430};
DE Short=Na(+)-NQR subunit F {ECO:0000255|HAMAP-Rule:MF_00430};
DE Short=Na(+)-translocating NQR subunit F {ECO:0000255|HAMAP-Rule:MF_00430};
DE EC=7.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000269|PubMed:11888296};
DE AltName: Full=NQR complex subunit F {ECO:0000255|HAMAP-Rule:MF_00430};
DE AltName: Full=NQR-1 subunit F {ECO:0000255|HAMAP-Rule:MF_00430};
GN Name=nqrF {ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000303|PubMed:11888296};
GN OrderedLocusNames=VC0395_A1879, VC395_2406;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
RN [3]
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=11888296; DOI=10.1021/bi011873o;
RA Barquera B., Hellwig P., Zhou W., Morgan J.E., Haese C.C., Gosink K.K.,
RA Nilges M., Bruesehoff P.J., Roth A., Lancaster C.R., Gennis R.B.;
RT "Purification and characterization of the recombinant Na(+)-translocating
RT NADH:quinone oxidoreductase from Vibrio cholerae.";
RL Biochemistry 41:3781-3789(2002).
RN [4]
RP COFACTOR, AND MUTAGENESIS OF CYS-70; CYS-76; CYS-79; CYS-111; ARG-210;
RP TYR-212 AND SER-246.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=15379571; DOI=10.1021/bi048689y;
RA Barquera B., Nilges M.J., Morgan J.E., Ramirez-Silva L., Zhou W.,
RA Gennis R.B.;
RT "Mutagenesis study of the 2Fe-2S center and the FAD binding site of the
RT Na(+)-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae.";
RL Biochemistry 43:12322-12330(2004).
RN [5]
RP SUBUNIT.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=20558724; DOI=10.1074/jbc.m109.071126;
RA Casutt M.S., Huber T., Brunisholz R., Tao M., Fritz G., Steuber J.;
RT "Localization and function of the membrane-bound riboflavin in the Na+-
RT translocating NADH:quinone oxidoreductase (Na+-NQR) from Vibrio cholerae.";
RL J. Biol. Chem. 285:27088-27099(2010).
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:0000255|HAMAP-Rule:MF_00430}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00430, ECO:0000269|PubMed:11888296};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00430,
CC ECO:0000269|PubMed:15379571};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|HAMAP-Rule:MF_00430,
CC ECO:0000269|PubMed:15379571};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00430,
CC ECO:0000269|PubMed:15379571};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000269|PubMed:11888296,
CC ECO:0000269|PubMed:20558724}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00430, ECO:0000305}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00430}.
CC -!- SIMILARITY: Belongs to the NqrF family. {ECO:0000255|HAMAP-
CC Rule:MF_00430, ECO:0000305}.
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DR EMBL; CP000627; ABQ21559.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10396.1; -; Genomic_DNA.
DR RefSeq; WP_000103964.1; NZ_JAACZH010000008.1.
DR PDB; 4UAJ; X-ray; 2.70 A; A=129-408.
DR PDBsum; 4UAJ; -.
DR AlphaFoldDB; A5F5Y4; -.
DR SMR; A5F5Y4; -.
DR STRING; 345073.VC395_2406; -.
DR EnsemblBacteria; ABQ21559; ABQ21559; VC0395_A1879.
DR GeneID; 57740911; -.
DR KEGG; vco:VC0395_A1879; -.
DR KEGG; vcr:VC395_2406; -.
DR PATRIC; fig|345073.21.peg.2319; -.
DR eggNOG; COG2871; Bacteria.
DR HOGENOM; CLU_003827_7_2_6; -.
DR OMA; FIKEFVV; -.
DR BRENDA; 7.2.1.1; 15862.
DR Proteomes; UP000000249; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; IDA:UniProtKB.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_00430; NqrF; 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; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF000044; Cis_Diol_DH_RD; 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 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Cell inner membrane; Cell membrane; FAD;
KW Flavoprotein; Ion transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW NAD; Sodium; Sodium transport; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..408
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT F"
FT /id="PRO_1000080595"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT DOMAIN 33..127
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT DOMAIN 130..270
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT BINDING 70
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430,
FT ECO:0000269|PubMed:15379571"
FT BINDING 76
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430,
FT ECO:0000269|PubMed:15379571"
FT BINDING 79
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430,
FT ECO:0000269|PubMed:15379571"
FT BINDING 111
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430,
FT ECO:0000269|PubMed:15379571"
FT MUTAGEN 70
FT /note="C->A: Loss of the 2Fe-2S center, but does not affect
FT flavin content. Exhibits very low NADH:quinone
FT oxidoreductase activity."
FT /evidence="ECO:0000269|PubMed:15379571"
FT MUTAGEN 76
FT /note="C->A: Loss of the 2Fe-2S center, but does not affect
FT flavin content. Exhibits very low NADH:quinone
FT oxidoreductase activity."
FT /evidence="ECO:0000269|PubMed:15379571"
FT MUTAGEN 79
FT /note="C->A: Loss of the 2Fe-2S center, but does not affect
FT flavin content. Exhibits very low NADH:quinone
FT oxidoreductase activity."
FT /evidence="ECO:0000269|PubMed:15379571"
FT MUTAGEN 111
FT /note="C->A: Loss of the 2Fe-2S center, but does not affect
FT flavin content. Exhibits very low NADH:quinone
FT oxidoreductase activity."
FT /evidence="ECO:0000269|PubMed:15379571"
FT MUTAGEN 210
FT /note="R->L: Decreases flavin content, but does not affect
FT the 2Fe-2S center. Exhibits very low NADH:quinone
FT oxidoreductase activity."
FT /evidence="ECO:0000269|PubMed:15379571"
FT MUTAGEN 212
FT /note="Y->L: Decreases flavin content, but does not affect
FT the 2Fe-2S center. Exhibits very low NADH:quinone
FT oxidoreductase activity."
FT /evidence="ECO:0000269|PubMed:15379571"
FT MUTAGEN 246
FT /note="S->A: Decreases flavin content, but does not affect
FT the 2Fe-2S center. Exhibits very low NADH:quinone
FT oxidoreductase activity."
FT /evidence="ECO:0000269|PubMed:15379571"
FT STRAND 131..153
FT /evidence="ECO:0007829|PDB:4UAJ"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4UAJ"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:4UAJ"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:4UAJ"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4UAJ"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:4UAJ"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:4UAJ"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:4UAJ"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:4UAJ"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:4UAJ"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:4UAJ"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:4UAJ"
FT STRAND 272..281
FT /evidence="ECO:0007829|PDB:4UAJ"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:4UAJ"
FT HELIX 285..296
FT /evidence="ECO:0007829|PDB:4UAJ"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:4UAJ"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:4UAJ"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:4UAJ"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:4UAJ"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:4UAJ"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:4UAJ"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:4UAJ"
FT TURN 363..366
FT /evidence="ECO:0007829|PDB:4UAJ"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:4UAJ"
FT HELIX 381..392
FT /evidence="ECO:0007829|PDB:4UAJ"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:4UAJ"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:4UAJ"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:4UAJ"
SQ SEQUENCE 408 AA; 45067 MW; F5665E9623CAAD7B CRC64;
MSTIIFGVVM FTLIILALVL VILFAKSKLV PTGDITISIN GDPEKAIVTQ PGGKLLTALA
GAGVFVSSAC GGGGSCGQCR VKIKSGGGDI LPTELDHISK GEAREGERLA CQVAVKADMD
LELPEEIFGV KKWECTVISN DNKATFIKEL KLAIPDGESV PFRAGGYIQI EAPAHHVKYA
DFDVPEKYRG DWDKFNLFRY ESKVDEPIIR AYSMANYPEE FGIIMLNVRI ATPPPNNPNV
PPGQMSSYIW SLKAGDKCTI SGPFGEFFAK DTDAEMVFIG GGAGMAPMRS HIFDQLKRLK
SKRKMSYWYG ARSKREMFYV EDFDGLAAEN DNFVWHCALS DPQPEDNWTG YTGFIHNVLY
ENYLKDHEAP EDCEYYMCGP PMMNAAVINM LKNLGVEEEN ILLDDFGG
