SUFE_SHIDS
ID SUFE_SHIDS Reviewed; 138 AA.
AC Q32F89;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Cysteine desulfuration protein SufE {ECO:0000255|HAMAP-Rule:MF_01832};
GN Name=sufE {ECO:0000255|HAMAP-Rule:MF_01832}; OrderedLocusNames=SDY_1910;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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. {ECO:0000255|HAMAP-
CC Rule:MF_01832}.
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01832}.
CC -!- SUBUNIT: Homodimer. Interacts with SufS. {ECO:0000255|HAMAP-
CC Rule:MF_01832}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01832}.
CC -!- SIMILARITY: Belongs to the SufE family. {ECO:0000255|HAMAP-
CC Rule:MF_01832}.
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DR EMBL; CP000034; ABB62016.1; -; Genomic_DNA.
DR RefSeq; WP_000279738.1; NC_007606.1.
DR RefSeq; YP_403507.1; NC_007606.1.
DR AlphaFoldDB; Q32F89; -.
DR SMR; Q32F89; -.
DR STRING; 300267.SDY_1910; -.
DR EnsemblBacteria; ABB62016; ABB62016; SDY_1910.
DR KEGG; sdy:SDY_1910; -.
DR PATRIC; fig|300267.13.peg.2299; -.
DR HOGENOM; CLU_124502_1_1_6; -.
DR OMA; DWMQRYE; -.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000002716; 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 3: Inferred from homology;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..138
FT /note="Cysteine desulfuration protein SufE"
FT /id="PRO_1000070447"
FT ACT_SITE 51
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01832"
SQ SEQUENCE 138 AA; 15758 MW; 92F58475B1B988B8 CRC64;
MAVLPDKEKL LRNFLRCANW EEKYLYIIEL GQRLPELRDE GRSPQNSIQG CQSQVWIVMR
QNAQGIIELQ GDSDAAIVKG LIAVVFILYD QMMPQDIVNF DVRPWFEKMA LTQHLTPSRS
QGLEAMIRAI RAKAAALS