SUFE_DICD3
ID SUFE_DICD3 Reviewed; 138 AA.
AC Q9EXP1; E0SGT7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cysteine desulfuration protein SufE;
GN Name=sufE; OrderedLocusNames=Dda3937_03664;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=11251816; DOI=10.1046/j.1365-2958.2001.02288.x;
RA Nachin L., El Hassouni M., Loiseau L., Expert D., Barras F.;
RT "SoxR-dependent response to oxidative stress and virulence of Erwinia
RT chrysanthemi: the key role of SufC, an orphan ABC ATPase.";
RL Mol. Microbiol. 39:960-972(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
RN [3]
RP FUNCTION, HOMODIMERIZATION, AND SUBCELLULAR LOCATION.
RC STRAIN=3937;
RX PubMed=12876288; DOI=10.1074/jbc.m305953200;
RA Loiseau L., Ollagnier-de-Choudens S., Nachin L., Fontecave M., Barras F.;
RT "Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form
RT a new type of cysteine desulfurase.";
RL J. Biol. Chem. 278:38352-38359(2003).
CC -!- FUNCTION: Participates in cysteine desulfuration mediated by SufS.
CC Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-
CC alanine and constitutes an essential step in sulfur metabolism for
CC biosynthesis of a variety of sulfur-containing biomolecules. Functions
CC as a sulfur acceptor for SufS, by mediating the direct transfer of the
CC sulfur atom from the S-sulfanylcysteine of SufS, an intermediate
CC product of cysteine desulfuration process (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:12876288}.
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC -!- SUBUNIT: Homodimer. Interacts with SufS.
CC -!- INTERACTION:
CC Q9EXP1; Q9EXP2: sufS; NbExp=3; IntAct=EBI-2121567, EBI-2121573;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12876288}.
CC -!- SIMILARITY: Belongs to the SufE family. {ECO:0000305}.
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DR EMBL; AJ301654; CAC17129.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM98915.1; -; Genomic_DNA.
DR RefSeq; WP_013318358.1; NC_014500.1.
DR AlphaFoldDB; Q9EXP1; -.
DR SMR; Q9EXP1; -.
DR IntAct; Q9EXP1; 1.
DR STRING; 198628.Dda3937_03664; -.
DR EnsemblBacteria; ADM98915; ADM98915; Dda3937_03664.
DR GeneID; 9734154; -.
DR KEGG; ddd:Dda3937_03664; -.
DR PATRIC; fig|198628.6.peg.2705; -.
DR eggNOG; COG2166; Bacteria.
DR HOGENOM; CLU_124502_1_1_6; -.
DR OMA; DWMQRYE; -.
DR OrthoDB; 1996347at2; -.
DR BioCyc; DDAD198628:DDA3937_RS12755-MON; -.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR HAMAP; MF_01832; SufE; 1.
DR InterPro; IPR023939; Cysteine_desulfuration_SufE.
DR InterPro; IPR003808; Fe-S_metab-assoc_dom.
DR PANTHER; PTHR43597; PTHR43597; 1.
DR Pfam; PF02657; SufE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..138
FT /note="Cysteine desulfuration protein SufE"
FT /id="PRO_0000202127"
FT ACT_SITE 51
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 138 AA; 15165 MW; D89144CCB51154F1 CRC64;
MAQLPDPQKL LRNFSRCSNW EEKYLYIIEL GAGLAPLSDA QRQDGNRVSG CQSQVWIDLA
SNEQGNVVLH GDSDAAIVKG LIAIVFSLYQ GLSVREIVEL DVRPFFASLA LTQHLTPSRS
QGLEAMLRAV RARASALI