GLPE_ACTP2
ID GLPE_ACTP2 Reviewed; 108 AA.
AC A3MYF1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=APL_0079;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN73187.1; -; Genomic_DNA.
DR RefSeq; WP_005595720.1; NC_009053.1.
DR AlphaFoldDB; A3MYF1; -.
DR SMR; A3MYF1; -.
DR STRING; 416269.APL_0079; -.
DR EnsemblBacteria; ABN73187; ABN73187; APL_0079.
DR GeneID; 66258919; -.
DR KEGG; apl:APL_0079; -.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_089574_14_0_6; -.
DR OMA; VCYHGIS; -.
DR Proteomes; UP000001432; 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; Reference proteome; Transferase.
FT CHAIN 1..108
FT /note="Thiosulfate sulfurtransferase GlpE"
FT /id="PRO_1000062953"
FT DOMAIN 18..106
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01009"
FT ACT_SITE 66
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01009"
SQ SEQUENCE 108 AA; 12403 MW; E31DA8D75B3A4C16 CRC64;
MSETFTEISP HQAWELIENE GATLADIRDG RRYAYSHPQD AFHLTNESYG RFLDEVDYEE
PVIVMCYHGV SSRNTAQFLV EQGFDRVYSV KGGFDGWERS GLPIETAY