SUFE_SALPA
ID SUFE_SALPA Reviewed; 138 AA.
AC Q5PH69;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Cysteine desulfuration protein SufE {ECO:0000255|HAMAP-Rule:MF_01832};
GN Name=sufE {ECO:0000255|HAMAP-Rule:MF_01832}; OrderedLocusNames=SPA1480;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV77417.1; -; Genomic_DNA.
DR RefSeq; WP_000729470.1; NC_006511.1.
DR AlphaFoldDB; Q5PH69; -.
DR SMR; Q5PH69; -.
DR EnsemblBacteria; AAV77417; AAV77417; SPA1480.
DR KEGG; spt:SPA1480; -.
DR HOGENOM; CLU_124502_1_1_6; -.
DR OMA; DWMQRYE; -.
DR UniPathway; UPA00266; -.
DR Proteomes; UP000008185; 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_1000070445"
FT ACT_SITE 51
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01832"
SQ SEQUENCE 138 AA; 15790 MW; E284AA90A4682DFB CRC64;
MAALPDKEKL LRNFTRCANW EEKYLYIIEL GQRLAELNPQ DRNPQNTIHG CQSQVWIVMR
RNANGIIELQ GDSDAAIVKG LMAVVFILYH QMTAQDIVHF DVRPWFEKMA LTQHLTPSRS
QGLEAMIRAI RAKAATLS