GLPE_PECAS
ID GLPE_PECAS Reviewed; 105 AA.
AC Q6CZL2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=ECA4139;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG77036.1; -; Genomic_DNA.
DR RefSeq; WP_011095610.1; NC_004547.2.
DR AlphaFoldDB; Q6CZL2; -.
DR SMR; Q6CZL2; -.
DR STRING; 218491.ECA4139; -.
DR EnsemblBacteria; CAG77036; CAG77036; ECA4139.
DR KEGG; eca:ECA4139; -.
DR PATRIC; fig|218491.5.peg.4210; -.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_089574_14_0_6; -.
DR OMA; VCYHGIS; -.
DR OrthoDB; 2056793at2; -.
DR Proteomes; UP000007966; 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 InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..105
FT /note="Thiosulfate sulfurtransferase GlpE"
FT /id="PRO_0000200551"
FT DOMAIN 16..104
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01009"
FT ACT_SITE 64
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01009"
SQ SEQUENCE 105 AA; 11670 MW; 0EB26357B62F9178 CRC64;
MEQFEAISIE QAHSRWQEGG VVVDIRDPQS FAAAHVPGAT HLTNETLPDF VRGADFEAPV
MVICYHGISS RNAAQYLISQ GFDSVYSIDG GFEAWQHRYP QDTQA