NUOE_BUCAI
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 03-AUG-2022, entry version 122.
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; Proteobacteria; 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; 107806.10038840; -.
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 OMA; HIIRYCD; -.
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; 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 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