ID   GLPE_KLEP3              Reviewed;         109 AA.
AC   B5XTR4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 56.
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=KPK_0323;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(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; CP000964; ACI10450.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XTR4; -.
DR   SMR; B5XTR4; -.
DR   EnsemblBacteria; ACI10450; ACI10450; KPK_0323.
DR   KEGG; kpe:KPK_0323; -.
DR   HOGENOM; CLU_089574_14_0_6; -.
DR   OMA; VCYHGIS; -.
DR   OrthoDB; 2056793at2; -.
DR   Proteomes; UP000001734; 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..109
FT                   /note="Thiosulfate sulfurtransferase GlpE"
FT                   /id="PRO_1000190100"
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   109 AA;  12273 MW;  D7FD64CA1EBFCD21 CRC64;
     MEQFECINVE EAHQKLHQQT AVLVDIRDPQ SYAMGHTPGA FHLTNDTLGA FMRDHDFDTA
     VMVMCYHGNS SKGAAQYLLQ QGFDKVYSVD GGFDAWHRHF PAEVAHGTF