ID   NUOE_BUCAI              Reviewed;         162 AA.
AC   P57255;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   27-MAR-2024, entry version 128.
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=BU157;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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   -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F, and G
CC       constitute the peripheral sector of the complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; BA000003; BAB12875.1; -; Genomic_DNA.
DR   RefSeq; NP_239989.1; NC_002528.1.
DR   RefSeq; WP_009874113.1; NC_002528.1.
DR   AlphaFoldDB; P57255; -.
DR   SMR; P57255; -.
DR   STRING; 563178.BUAP5A_155; -.
DR   EnsemblBacteria; BAB12875; BAB12875; BAB12875.
DR   KEGG; buc:BU157; -.
DR   PATRIC; fig|107806.10.peg.167; -.
DR   eggNOG; COG1905; Bacteria.
DR   HOGENOM; CLU_054362_2_0_6; -.
DR   Proteomes; UP000001806; Chromosome.
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; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.10.10.1590; NADH-quinone oxidoreductase subunit E; 1.
DR   InterPro; IPR002023; NuoE-like.
DR   InterPro; IPR042128; NuoE_dom.
DR   InterPro; IPR041921; NuoE_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR01958; nuoE_fam; 1.
DR   PANTHER; PTHR10371:SF3; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10371; NADH DEHYDROGENASE UBIQUINONE FLAVOPROTEIN 2, MITOCHONDRIAL; 1.
DR   Pfam; PF01257; 2Fe-2S_thioredx; 1.
DR   PIRSF; PIRSF000216; NADH_DH_24kDa; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS01099; COMPLEX1_24K; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Iron; Iron-sulfur; Metal-binding; NAD; Quinone; Reference proteome;
KW   Translocase.
FT   CHAIN           1..162
FT                   /note="NADH-quinone oxidoreductase subunit E"
FT                   /id="PRO_0000118688"
FT   BINDING         88
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
FT   BINDING         93
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
FT   BINDING         129
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
FT   BINDING         133
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   162 AA;  18598 MW;  428DC8DBA0B463F1 CRC64;
     MQEISIKFKL TNEEINAIEN QKKYYEDFRA ISIEALKIVQ KKRGWVSDQA IYAIAEILHI
     NPSDVEGVAT FYSQIFRKPV GRNIIRYCDS VVCFLTGYKR IQIALENYLK IKIGETTKDD
     RFTLLPVCCL GNCDKGPTIM INEDTYSVLT PESIPSLLES YK
//