NUOE1_RHIME
ID NUOE1_RHIME Reviewed; 275 AA.
AC P56909;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=NADH-quinone oxidoreductase subunit E 1;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit E 1;
DE AltName: Full=NDH-1 subunit E 1;
GN Name=nuoE1; Synonyms=nuoE; OrderedLocusNames=R01269; ORFNames=SMc01917;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=41;
RA Putnoky P., Jady B., Chellapilla K.P., Barta F., Kiss E.;
RT "Rhizobium meliloti carries two sets of nuo genes.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient (By 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; AJ245398; CAB51625.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45848.1; -; Genomic_DNA.
DR RefSeq; NP_385375.1; NC_003047.1.
DR RefSeq; WP_010969146.1; NC_003047.1.
DR AlphaFoldDB; P56909; -.
DR SMR; P56909; -.
DR STRING; 266834.SMc01917; -.
DR EnsemblBacteria; CAC45848; CAC45848; SMc01917.
DR GeneID; 61602730; -.
DR KEGG; sme:SMc01917; -.
DR PATRIC; fig|266834.11.peg.2683; -.
DR eggNOG; COG1905; Bacteria.
DR HOGENOM; CLU_054362_0_1_5; -.
DR OMA; VGKFHVQ; -.
DR Proteomes; UP000001976; 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; Ubiquinone.
FT CHAIN 1..275
FT /note="NADH-quinone oxidoreductase subunit E 1"
FT /id="PRO_0000118698"
FT REGION 200..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 140
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 144
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT CONFLICT 211
FT /note="S -> KP (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 29906 MW; CD403B196E541382 CRC64;
MSVRRLAEDT VQPAAFAFSK ENAAWAEATI KKYPEGREQS AVIPLLMRAQ EQDGWVTRAA
IESVADMLGM AYIRVLEVAT FYTQFQLQPV GTRAHVQVCG TTPCMLRGAE DLIKICKKKI
ASEPFTLNEG GTLSWEEVEC QGACVNAPMV MIFKDTFEDL TPERLEEIID RFEAGKGSEV
VPGPQIDRVY SAPIGGLTTL QAPEPVEEKK SVRASKAKDE QAVSVPPSNA AKPSTATDVT
NPTLKTPATA RKAAAKNVKI EGETVDKSKP AKKPR
