NUOE_AQUAE
ID NUOE_AQUAE Reviewed; 160 AA.
AC O66842;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=NADH-quinone oxidoreductase subunit E;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit E;
DE AltName: Full=NDH-1 subunit E;
GN Name=nuoE; OrderedLocusNames=aq_574;
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AE000657; AAC06799.1; -; Genomic_DNA.
DR PIR; F70351; F70351.
DR RefSeq; NP_213402.1; NC_000918.1.
DR RefSeq; WP_010880340.1; NC_000918.1.
DR PDB; 6HL2; X-ray; 1.95 A; A/C=1-160.
DR PDB; 6HL3; X-ray; 2.04 A; A/C=1-160.
DR PDB; 6HL4; X-ray; 2.06 A; A/C=1-160.
DR PDB; 6HLA; X-ray; 1.90 A; A/C=1-160.
DR PDB; 6HLI; X-ray; 2.38 A; A/C=1-160.
DR PDB; 6HLJ; X-ray; 2.10 A; A/C=1-160.
DR PDB; 6HLM; X-ray; 1.80 A; A/C=1-160.
DR PDB; 6Q9C; X-ray; 1.78 A; A/C=6-160.
DR PDB; 6Q9G; X-ray; 2.10 A; A/C=1-160.
DR PDB; 6Q9J; X-ray; 1.83 A; A/C=1-160.
DR PDB; 6Q9K; X-ray; 1.99 A; A/C=6-160.
DR PDB; 6R7P; X-ray; 3.22 A; A/C=1-160.
DR PDB; 6SAQ; X-ray; 2.02 A; A/C=1-160.
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; O66842; -.
DR SMR; O66842; -.
DR STRING; 224324.aq_574; -.
DR EnsemblBacteria; AAC06799; AAC06799; aq_574.
DR KEGG; aae:aq_574; -.
DR eggNOG; COG1905; Bacteria.
DR HOGENOM; CLU_054362_2_1_0; -.
DR InParanoid; O66842; -.
DR OMA; CHVQGAE; -.
DR OrthoDB; 1206880at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR CDD; cd03064; TRX_Fd_NuoE; 1.
DR Gene3D; 1.10.10.1590; -; 1.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR042128; NuoE_dom.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01958; nuoE_fam; 1.
DR PROSITE; PS01099; COMPLEX1_24K; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Iron; Iron-sulfur; Metal-binding; NAD; Quinone;
KW Reference proteome; Translocase.
FT CHAIN 1..160
FT /note="NADH-quinone oxidoreductase subunit E"
FT /id="PRO_0000118687"
FT BINDING 86
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 91
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 127
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 131
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:6Q9C"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:6Q9C"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:6Q9C"
SQ SEQUENCE 160 AA; 18551 MW; 425D81995A491B3B CRC64;
MFKTEFEFPE ELKTKLQEHI NYFPKKRQAI LLCLHEIQNY YGYIPPESLK PLADMLELPL
NHVEGVVAFY DMFDREDKAK YRIRVCVSIV CHLMGTNKLL KALENILGIK PGEVTPDGKF
KIVPVQCLGA CSEAPVFMVN DDEYKFESEV QLNEILSRYT
