ID   SDHE_ECOL6              Reviewed;          88 AA.
AC   P64560; Q46825;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=FAD assembly factor SdhE;
GN   Name=sdhE; Synonyms=ygfY; OrderedLocusNames=c3477;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: An FAD assembly protein, which accelerates covalent
CC       attachment of the cofactor into other proteins. Plays an essential role
CC       in the assembly of succinate dehydrogenase (SDH, respiratory complex
CC       II), an enzyme complex that is a component of both the tricarboxylic
CC       acid cycle and the electron transport chain, and which couples the
CC       oxidation of succinate to fumarate with the reduction of ubiquinone
CC       (coenzyme Q) to ubiquinol. Required for flavinylation (covalent
CC       attachment of FAD) of the flavoprotein subunit SdhA of SDH and other
CC       flavinylated proteins as well. {ECO:0000250|UniProtKB:G4V4G2}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P64559}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:G4V4G2}.
CC   -!- SIMILARITY: Belongs to the SdhE FAD assembly factor family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014075; AAN81925.1; -; Genomic_DNA.
DR   RefSeq; WP_000354046.1; NC_004431.1.
DR   AlphaFoldDB; P64560; -.
DR   SMR; P64560; -.
DR   STRING; 199310.c3477; -.
DR   EnsemblBacteria; AAN81925; AAN81925; c3477.
DR   GeneID; 67415218; -.
DR   KEGG; ecc:c3477; -.
DR   eggNOG; COG2938; Bacteria.
DR   HOGENOM; CLU_103054_2_2_6; -.
DR   OMA; FEHEYDT; -.
DR   BioCyc; ECOL199310:C3477-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.10.150.250; -; 1.
DR   InterPro; IPR005631; SDH.
DR   InterPro; IPR036714; SDH_sf.
DR   Pfam; PF03937; Sdh5; 1.
DR   SUPFAM; SSF109910; SSF109910; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm.
FT   CHAIN           1..88
FT                   /note="FAD assembly factor SdhE"
FT                   /id="PRO_0000214396"
SQ   SEQUENCE   88 AA;  10547 MW;  B7047D93220989DE CRC64;
     MDINNKARIH WACRRGMREL DISIMPFFEH EYDSLSDDEK RIFIRLLECD DPDLFNWLMN
     HGKPADAELE MMVRLIQTRN RERGPVAI