GLPE_YERPG
ID GLPE_YERPG Reviewed; 109 AA.
AC A9R4D5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=YpAngola_A3755;
OS Yersinia pestis bv. Antiqua (strain Angola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Angola;
RX PubMed=20061468; DOI=10.1128/jb.01518-09;
RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA Achtman M., Lindler L.E., Ravel J.;
RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT new insights into the evolution and pangenome of the plague bacterium.";
RL J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX86389.1; -; Genomic_DNA.
DR RefSeq; WP_002218928.1; NZ_CP009935.1.
DR AlphaFoldDB; A9R4D5; -.
DR SMR; A9R4D5; -.
DR GeneID; 66843799; -.
DR KEGG; ypg:YpAngola_A3755; -.
DR PATRIC; fig|349746.12.peg.463; -.
DR OMA; VCYHGIS; -.
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_1000190113"
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; 12316 MW; 4932B008865B1869 CRC64;
MEQFEAISVE QAYLRWKEGK TALVDIRDPQ SYEAGHAPGA FHLTNSSLHT FMQQTDFDQP
VMVMCYHGNS SKGAAQYLLQ QGFDVVYSID GGFEAWARSY PQDITSESR