SUFE_SALEP
ID SUFE_SALEP Reviewed; 138 AA.
AC B5QVS8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Cysteine desulfuration protein SufE {ECO:0000255|HAMAP-Rule:MF_01832};
GN Name=sufE {ECO:0000255|HAMAP-Rule:MF_01832}; OrderedLocusNames=SEN1671;
OS Salmonella enteritidis PT4 (strain P125109).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P125109;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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; AM933172; CAR33253.1; -; Genomic_DNA.
DR RefSeq; WP_000729468.1; NC_011294.1.
DR AlphaFoldDB; B5QVS8; -.
DR SMR; B5QVS8; -.
DR KEGG; set:SEN1671; -.
DR HOGENOM; CLU_124502_1_1_6; -.
DR OMA; DWMQRYE; -.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000000613; 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.
FT CHAIN 1..138
FT /note="Cysteine desulfuration protein SufE"
FT /id="PRO_1000188332"
FT ACT_SITE 51
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01832"
SQ SEQUENCE 138 AA; 15760 MW; E284BEC1E1682DFB CRC64;
MAALPDKEKL LRNFTRCANW EEKYLYIIEL GQRLAELNPQ DRNPQNTIHG CQSQVWIVMR
RNANGIIELQ GDSDAAIVKG LMAVVFILYH QMTAQDIVHF DVRPWFEKMA LAQHLTPSRS
QGLEAMIRAI RAKAATLS