ID   GLPE_PASMU              Reviewed;         107 AA.
AC   Q9CL12;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   28-JAN-2026, entry version 116.
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=PM1436;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Transferase that catalyzes the transfer of sulfur from
CC       thiosulfate to thiophilic acceptors such as cyanide or dithiols. May
CC       function in a CysM-independent thiosulfate assimilation pathway by
CC       catalyzing the conversion of thiosulfate to sulfite, which can then be
CC       used for L-cysteine biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01009}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=thiosulfate + hydrogen cyanide = thiocyanate + sulfite + 2
CC         H(+); Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC         ChEBI:CHEBI:18022, ChEBI:CHEBI:18407, ChEBI:CHEBI:33542; EC=2.8.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01009};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=thiosulfate + [thioredoxin]-dithiol = [thioredoxin]-disulfide
CC         + hydrogen sulfide + sulfite + 2 H(+); Xref=Rhea:RHEA:83859,
CC         Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:33542, ChEBI:CHEBI:50058; 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; AE004439; AAK03520.1; -; Genomic_DNA.
DR   RefSeq; WP_005724096.1; NC_002663.1.
DR   AlphaFoldDB; Q9CL12; -.
DR   SMR; Q9CL12; -.
DR   STRING; 272843.PM1436; -.
DR   EnsemblBacteria; AAK03520; AAK03520; PM1436.
DR   KEGG; pmu:PM1436; -.
DR   HOGENOM; CLU_089574_14_0_6; -.
DR   OrthoDB; 9811849at2; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004792; F:thiosulfate-cyanide sulfurtransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0103041; F:thiosulfate-thioredoxin sulfurtransferase activity; IEA:RHEA.
DR   CDD; cd01444; GlpE_ST; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   HAMAP; MF_01009; Thiosulf_sulfurtr; 1.
DR   InterPro; IPR050229; GlpE_sulfurtransferase.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR023695; Thiosulf_sulfurTrfase.
DR   NCBIfam; NF001195; PRK00162.1; 1.
DR   PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR43031:SF6; THIOSULFATE SULFURTRANSFERASE GLPE; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..107
FT                   /note="Thiosulfate sulfurtransferase GlpE"
FT                   /id="PRO_0000200556"
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   107 AA;  12081 MW;  7332CE1E00886E9F CRC64;
     MSAFSEISPQ QAWQLVQQHA AALLDIRNET HFALAHPAQA FHLSHQSYGE FEMQYEDDHP
     VIVICYHGVS SRGAAMYLIE QGYTQVYSVT GGFEAWERDG LPIERIG
//