ID   SDHE_SHEON              Reviewed;          82 AA.
AC   Q8EH90;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=FAD assembly factor SdhE;
GN   Name=sdhE; OrderedLocusNames=SO_1339;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:G4V4G2}.
CC   -!- SIMILARITY: Belongs to the SdhE FAD assembly factor family.
CC       {ECO:0000305}.
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DR   EMBL; AE014299; AAN54404.1; -; Genomic_DNA.
DR   RefSeq; NP_716959.1; NC_004347.2.
DR   RefSeq; WP_011071548.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EH90; -.
DR   SMR; Q8EH90; -.
DR   STRING; 211586.SO_1339; -.
DR   PaxDb; Q8EH90; -.
DR   KEGG; son:SO_1339; -.
DR   PATRIC; fig|211586.12.peg.1289; -.
DR   eggNOG; COG2938; Bacteria.
DR   HOGENOM; CLU_103054_2_2_6; -.
DR   OMA; FEHEYDT; -.
DR   OrthoDB; 2055100at2; -.
DR   PhylomeDB; Q8EH90; -.
DR   BioCyc; SONE211586:G1GMP-1237-MON; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0006105; P:succinate metabolic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..82
FT                   /note="FAD assembly factor SdhE"
FT                   /id="PRO_0000214423"
SQ   SEQUENCE   82 AA;  9641 MW;  49B27470C1A7CAAB CRC64;
     MELMNIARVR WACRRGMLEL DVLFQPFVDN VYQDLSDEDK VLFIRLLECE DPELFAWFMG
     HEVCPDPELA RMVVQVRGRA AP