ID   SDHE_COXBU              Reviewed;          82 AA.
AC   Q83D70;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=FAD assembly factor SdhE;
GN   Name=sdhE; OrderedLocusNames=CBU_0870;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO90403.1; -; Genomic_DNA.
DR   RefSeq; NP_819889.1; NC_002971.3.
DR   RefSeq; WP_005768810.1; NZ_CDBG01000001.1.
DR   AlphaFoldDB; Q83D70; -.
DR   SMR; Q83D70; -.
DR   STRING; 227377.CBU_0870; -.
DR   DNASU; 1208763; -.
DR   EnsemblBacteria; AAO90403; AAO90403; CBU_0870.
DR   GeneID; 1208763; -.
DR   KEGG; cbu:CBU_0870; -.
DR   PATRIC; fig|227377.7.peg.855; -.
DR   eggNOG; COG2938; Bacteria.
DR   HOGENOM; CLU_103054_2_2_6; -.
DR   OMA; FEHEYDT; -.
DR   Proteomes; UP000002671; 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_0000214393"
SQ   SEQUENCE   82 AA;  9924 MW;  B7917BA1E3FA8457 CRC64;
     MNEPLASKKI RWKCRRGMLE LDILLERFYE EKFRSLTKNE KEIFNQLLDQ PDPLLYDWLL
     GHVTPESSEF KKIIRKIQQL SS