NUOF_AQUAE
ID NUOF_AQUAE Reviewed; 426 AA.
AC O66841;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=aq_573;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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 -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AE000657; AAC06800.1; -; Genomic_DNA.
DR PIR; E70351; E70351.
DR RefSeq; NP_213401.1; NC_000918.1.
DR RefSeq; WP_010880339.1; NC_000918.1.
DR PDB; 6HL2; X-ray; 1.95 A; B/D=1-426.
DR PDB; 6HL3; X-ray; 2.04 A; B/D=1-426.
DR PDB; 6HL4; X-ray; 2.06 A; B/D=1-426.
DR PDB; 6HLA; X-ray; 1.90 A; B/D=1-426.
DR PDB; 6HLI; X-ray; 2.38 A; B/D=1-426.
DR PDB; 6HLJ; X-ray; 2.10 A; B/D=1-426.
DR PDB; 6HLM; X-ray; 1.80 A; B/D=1-426.
DR PDB; 6Q9C; X-ray; 1.78 A; B/D=2-419.
DR PDB; 6Q9G; X-ray; 2.10 A; B/D=1-426.
DR PDB; 6Q9J; X-ray; 1.83 A; B/D=1-426.
DR PDB; 6Q9K; X-ray; 1.99 A; B/D=2-419.
DR PDB; 6R7P; X-ray; 3.22 A; B/D=1-426.
DR PDB; 6SAQ; X-ray; 2.02 A; B/D=1-426.
DR PDBsum; 6HL2; -.
DR PDBsum; 6HL3; -.
DR PDBsum; 6HL4; -.
DR PDBsum; 6HLA; -.
DR PDBsum; 6HLI; -.
DR PDBsum; 6HLJ; -.
DR PDBsum; 6HLM; -.
DR PDBsum; 6Q9C; -.
DR PDBsum; 6Q9G; -.
DR PDBsum; 6Q9J; -.
DR PDBsum; 6Q9K; -.
DR PDBsum; 6R7P; -.
DR PDBsum; 6SAQ; -.
DR AlphaFoldDB; O66841; -.
DR SMR; O66841; -.
DR STRING; 224324.aq_573; -.
DR EnsemblBacteria; AAC06800; AAC06800; aq_573.
DR KEGG; aae:aq_573; -.
DR PATRIC; fig|224324.8.peg.468; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_0_1_0; -.
DR InParanoid; O66841; -.
DR OMA; CREGTDW; -.
DR OrthoDB; 688908at2; -.
DR Proteomes; UP000000798; Chromosome.
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: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; 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 PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding;
KW NAD; Quinone; Reference proteome; Translocase.
FT CHAIN 1..426
FT /note="NADH-quinone oxidoreductase subunit F"
FT /id="PRO_0000118570"
FT BINDING 65..74
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 176..223
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
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 353
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 393
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:6Q9C"
FT TURN 19..24
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:6Q9C"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:6Q9C"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 111..125
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 139..154
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6Q9C"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:6HLM"
FT STRAND 250..260
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:6Q9C"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 331..345
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 351..368
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 374..384
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 394..398
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 401..409
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 411..418
FT /evidence="ECO:0007829|PDB:6Q9C"
SQ SEQUENCE 426 AA; 47508 MW; A876712CBFA2E122 CRC64;
MRSYPAIPRI YAETTLNMLL KRAKKPRVHS IDEYLKDGGY QALEKALNMS PEEIIDWVDK
STLRGRGGAG FPTGKKWKFA VQNPGPRYFI CNADESEPGT FKDRIIIERD PHLLIEGIII
SSYAIGANEA YIYIRGEYPA GYYILRDAIE EAKKKGFLGK NILGSGFDLE IYVARGAGAY
ICGEETALIE SLEGKRGHPR LKPPYPVQKG LWGKPTVVNN VETIANVPFI ISMGWEEYRY
IGPSDYAGPK LFPVSGKVKK PGVYELPMNT TLREVIFKYA GGTLGNKKVK AVFSGALDCF
SSEELDIPMD YSPLGFGGTG TVIVLTEEDD IVEAALKIAE FYEHETCGQC TPCRVGCYEQ
ANLLEKIYKG EATEQDWEGF DFVNRNIQPT SICGLGAVAG RLIRQTLEKF PEEWEKYRKK
SASLPL
