GLPE_ECOLU
ID GLPE_ECOLU Reviewed; 108 AA.
AC B7NE29;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 55.
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=ECUMN_3883;
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / 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; CU928163; CAR15029.1; -; Genomic_DNA.
DR RefSeq; WP_000371928.1; NC_011751.1.
DR RefSeq; YP_002414534.1; NC_011751.1.
DR AlphaFoldDB; B7NE29; -.
DR SMR; B7NE29; -.
DR STRING; 585056.ECUMN_3883; -.
DR EnsemblBacteria; CAR15029; CAR15029; ECUMN_3883.
DR GeneID; 67417052; -.
DR KEGG; eum:ECUMN_3883; -.
DR PATRIC; fig|585056.7.peg.4057; -.
DR HOGENOM; CLU_089574_14_0_6; -.
DR OMA; VCYHGIS; -.
DR Proteomes; UP000007097; 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_1000134853"
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
