ID   GLPE_SHIDS              Reviewed;         108 AA.
AC   Q32AN7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Thiosulfate sulfurtransferase GlpE {ECO:0000255|HAMAP-Rule:MF_01009};
DE            EC=2.8.1.1 {ECO:0000255|HAMAP-Rule:MF_01009};
GN   Name=glpE {ECO:0000255|HAMAP-Rule:MF_01009}; OrderedLocusNames=SDY_3650;
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: Catalyzes, although with low efficiency, the sulfur transfer
CC       reaction from thiosulfate to cyanide. {ECO:0000255|HAMAP-
CC       Rule:MF_01009}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen cyanide + thiosulfate = 2 H(+) + sulfite +
CC         thiocyanate; Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:18022, ChEBI:CHEBI:18407,
CC         ChEBI:CHEBI:33542; EC=2.8.1.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01009};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01009}.
CC   -!- SIMILARITY: Belongs to the GlpE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01009}.
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DR   EMBL; CP000034; ABB63618.1; -; Genomic_DNA.
DR   RefSeq; WP_000371932.1; NC_007606.1.
DR   RefSeq; YP_405109.1; NC_007606.1.
DR   AlphaFoldDB; Q32AN7; -.
DR   SMR; Q32AN7; -.
DR   STRING; 300267.SDY_3650; -.
DR   EnsemblBacteria; ABB63618; ABB63618; SDY_3650.
DR   KEGG; sdy:SDY_3650; -.
DR   PATRIC; fig|300267.13.peg.4332; -.
DR   HOGENOM; CLU_089574_14_0_6; -.
DR   OMA; VCYHGIS; -.
DR   Proteomes; UP000002716; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01444; GlpE_ST; 1.
DR   Gene3D; 3.40.250.10; -; 1.
DR   HAMAP; MF_01009; Thiosulf_sulfurtr; 1.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR023695; Thiosulf_sulfurTrfase.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; SSF52821; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..108
FT                   /note="Thiosulfate sulfurtransferase GlpE"
FT                   /id="PRO_1000062978"
FT   DOMAIN          17..105
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01009"
FT   ACT_SITE        65
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01009"
SQ   SEQUENCE   108 AA;  12112 MW;  49D4B461DEC49F05 CRC64;
     MDQFECINVA DAHQKLQEKE AVLVDIRDPQ SFAMGHAVQT FHLTNDTLGA FMRDNDFDTP
     VMVMCYHGNS SKGAAQYLLQ QGYDVVYSID GGFEAWQRQF PAEVAYGA