SDHE_VIBCH
ID SDHE_VIBCH Reviewed; 86 AA.
AC Q9KPA2;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=FAD assembly factor SdhE;
GN Name=sdhE; OrderedLocusNames=VC_2471;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP STRUCTURE BY NMR.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RG Northeast structural genomics consortium (NESG);
RT "Solution structure of UPF0350 protein VC_2471.";
RL Submitted (FEB-2009) to the PDB data bank.
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; AE003852; AAF95613.1; -; Genomic_DNA.
DR PIR; D82074; D82074.
DR RefSeq; NP_232100.1; NC_002505.1.
DR RefSeq; WP_000287742.1; NZ_LT906614.1.
DR PDB; 2JR5; NMR; -; A=1-86.
DR PDBsum; 2JR5; -.
DR AlphaFoldDB; Q9KPA2; -.
DR BMRB; Q9KPA2; -.
DR SMR; Q9KPA2; -.
DR STRING; 243277.VC_2471; -.
DR DNASU; 2613013; -.
DR EnsemblBacteria; AAF95613; AAF95613; VC_2471.
DR GeneID; 57741075; -.
DR KEGG; vch:VC_2471; -.
DR PATRIC; fig|243277.26.peg.2355; -.
DR eggNOG; COG2938; Bacteria.
DR HOGENOM; CLU_103054_2_2_6; -.
DR OMA; FEHEYDT; -.
DR BioCyc; VCHO:VC2471-MON; -.
DR EvolutionaryTrace; Q9KPA2; -.
DR Proteomes; UP000000584; Chromosome 1.
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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..86
FT /note="FAD assembly factor SdhE"
FT /id="PRO_0000214425"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:2JR5"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:2JR5"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:2JR5"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:2JR5"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2JR5"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:2JR5"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:2JR5"
FT HELIX 68..86
FT /evidence="ECO:0007829|PDB:2JR5"
SQ SEQUENCE 86 AA; 9854 MW; C1520248CA032D4C CRC64;
MYTAEQKARI KWACRRGMLE LDVVIMPFFE ECFDSLTESE QDDFVALLES DDPDLFAWVM
GHGRCENLGL AAMVDKIVAH NLSKVR