ID   GLPE_ECO24              Reviewed;         108 AA.
AC   A7ZSV5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 66.
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};
GN   OrderedLocusNames=EcE24377A_3901;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV18402.1; -; Genomic_DNA.
DR   RefSeq; WP_000371928.1; NC_009801.1.
DR   AlphaFoldDB; A7ZSV5; -.
DR   BMRB; A7ZSV5; -.
DR   SMR; A7ZSV5; -.
DR   EnsemblBacteria; ABV18402; ABV18402; EcE24377A_3901.
DR   GeneID; 67417052; -.
DR   KEGG; ecw:EcE24377A_3901; -.
DR   HOGENOM; CLU_089574_14_0_6; -.
DR   OMA; VCYHGIS; -.
DR   Proteomes; UP000001122; 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; Transferase.
FT   CHAIN           1..108
FT                   /note="Thiosulfate sulfurtransferase GlpE"
FT                   /id="PRO_1000062956"
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;  12082 MW;  18D5B461C2A8EF19 CRC64;
     MDQFECINVA DAHQKLQEKE AVLVDIRDPQ SFAMGHAVQA FHLTNDTLGA FMRDNDFDTP
     VMVMCYHGNS SKGAAQYLLQ QGYDVVYSID GGFEAWQRQF PAEVAYGA