GLPE_ECO7I
ID GLPE_ECO7I Reviewed; 108 AA.
AC B7NMI9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 59.
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=ECIAI39_3905;
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI39 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928164; CAR20017.1; -; Genomic_DNA.
DR RefSeq; WP_000371924.1; NC_011750.1.
DR RefSeq; YP_002409798.1; NC_011750.1.
DR AlphaFoldDB; B7NMI9; -.
DR SMR; B7NMI9; -.
DR STRING; 585057.ECIAI39_3905; -.
DR EnsemblBacteria; CAR20017; CAR20017; ECIAI39_3905.
DR KEGG; ect:ECIAI39_3905; -.
DR PATRIC; fig|585057.6.peg.4043; -.
DR HOGENOM; CLU_089574_14_0_6; -.
DR OMA; VCYHGIS; -.
DR Proteomes; UP000000749; 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_1000134850"
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; 12054 MW; 03C72DEAC2A8F016 CRC64;
MDQFECINVA DAHQKLQEKE AVLVDIRDPQ SFAMGHAAQA FHLTNDTLGA FMRDNDFDTP
VMVMCYHGNS SKGAAQYLLQ QGYDVVYSID GGFEAWQRQF PAEVAYGA
