(data stored in ACNUC7421 zone)

SWISSPROT: GLPE_PSEAB

ID   GLPE_PSEAB              Reviewed;         110 AA.
AC   Q02TH4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   08-MAY-2019, entry version 61.
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=PA14_07690;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Catalyzes, although with low efficiency, the sulfur
CC       transfer 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}.
DR   EMBL; CP000438; ABJ15553.1; -; Genomic_DNA.
DR   RefSeq; WP_003099577.1; NC_008463.1.
DR   SMR; Q02TH4; -.
DR   EnsemblBacteria; ABJ15553; ABJ15553; PA14_07690.
DR   KEGG; pau:PA14_07690; -.
DR   HOGENOM; HOG000247776; -.
DR   KO; K02439; -.
DR   OMA; VCYHGIS; -.
DR   BioCyc; PAER208963:G1G74-634-MONOMER; -.
DR   Proteomes; UP000000653; 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;
DR   PRODOM; Q02TH4.
DR   SWISS-2DPAGE; Q02TH4.
KW   Complete proteome; Cytoplasm; Transferase.
FT   CHAIN         1    110       Thiosulfate sulfurtransferase GlpE.
FT                                /FTId=PRO_1000062968.
FT   DOMAIN       17    105       Rhodanese. {ECO:0000255|HAMAP-
FT                                Rule:MF_01009}.
FT   ACT_SITE     65     65       Cysteine persulfide intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01009}.
SQ   SEQUENCE   110 AA;  11935 MW;  ABDEF7AE1D31DF02 CRC64;
     MSDTFQRIAP EQARQLRENG AQVVDIRDPQ SFAVGHISGS RHIDNHSVAD FIAAADLDAP
     LVVVCYHGNS SQSAAAYFIQ QGFSDVYSLD GGFELWRSVY PADTSSGEAE
//

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