ID   SDHE_ACEP3              Reviewed;         109 AA.
AC   C7JGP5;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=FAD assembly factor SdhE {ECO:0000303|PubMed:26399411};
GN   Name=sdhE {ECO:0000303|PubMed:26399411}; OrderedLocusNames=APA01_11050;
OS   Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=634452;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 105184 / IFO 3283-01;
RX   PubMed=19638423; DOI=10.1093/nar/gkp612;
RA   Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA   Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT   "Whole-genome analyses reveal genetic instability of Acetobacter
RT   pasteurianus.";
RL   Nucleic Acids Res. 37:5768-5783(2009).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 33445 / DSM 3509 / LMD 22.1;
RX   PubMed=26399411; DOI=10.1007/s00253-015-6972-8;
RA   Kiefler I., Bringer S., Bott M.;
RT   "SdhE-dependent formation of a functional Acetobacter pasteurianus
RT   succinate dehydrogenase in Gluconobacter oxydans--a first step toward a
RT   complete tricarboxylic acid cycle.";
RL   Appl. Microbiol. Biotechnol. 99:9147-9160(2015).
CC   -!- FUNCTION: An FAD assembly protein, which accelerates covalent
CC       attachment of the cofactor into other proteins (Probable). Plays an
CC       essential role in the assembly of succinate dehydrogenase (SDH,
CC       respiratory complex II), an enzyme complex that is a component of both
CC       the tricarboxylic acid cycle and the electron transport chain, and
CC       which couples the oxidation of succinate to fumarate with the reduction
CC       of ubiquinone (coenzyme Q) to ubiquinol (By similarity). Required for
CC       flavinylation of SdhA, when the SDH operon and this gene are
CC       overexpressed in G.oxydans. Flavinylation of SdhA is detected only in
CC       the presence of sdhE. {ECO:0000250|UniProtKB:G4V4G2,
CC       ECO:0000269|PubMed:19638423}.
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; AP011121; BAH99254.1; -; Genomic_DNA.
DR   RefSeq; WP_003623435.1; NC_013209.1.
DR   AlphaFoldDB; C7JGP5; -.
DR   SMR; C7JGP5; -.
DR   STRING; 634452.APA01_11050; -.
DR   EnsemblBacteria; BAH99254; BAH99254; APA01_11050.
DR   GeneID; 60376825; -.
DR   GeneID; 66350133; -.
DR   KEGG; apt:APA01_11050; -.
DR   eggNOG; COG2938; Bacteria.
DR   HOGENOM; CLU_103054_1_0_5; -.
DR   OMA; LFRCWHR; -.
DR   BioCyc; APAS634452:APA01_RS05580-MON; -.
DR   Proteomes; UP000000948; 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; Reference proteome.
FT   CHAIN           1..109
FT                   /note="FAD assembly factor SdhE"
FT                   /id="PRO_0000438884"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   109 AA;  12202 MW;  DB4EAE7622DAEC23 CRC64;
     MQDNFTASSP SSSSSASGVA EDNLAARRRR LKFRANHRGT FETDILIGGF VEANADTMTA
     EELTDMENIL EMPDPELTDW LFGRLPLPEE KATPMLRRMV EDSRIRRGG