ID F3G4S1_PSESJ Unreviewed; 106 AA.
AC F3G4S1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Thiosulfate sulfurtransferase GlpE {ECO:0000256|HAMAP-Rule:MF_01009};
DE EC=2.8.1.1 {ECO:0000256|HAMAP-Rule:MF_01009};
GN Name=glpE {ECO:0000256|HAMAP-Rule:MF_01009,
GN ECO:0000313|EMBL:EGH42071.1};
GN ORFNames=PSYPI_06493 {ECO:0000313|EMBL:EGH42071.1};
OS Pseudomonas syringae pv. pisi str. 1704B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH42071.1, ECO:0000313|Proteomes:UP000004986};
RN [1] {ECO:0000313|EMBL:EGH42071.1, ECO:0000313|Proteomes:UP000004986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1704B {ECO:0000313|EMBL:EGH42071.1,
RC ECO:0000313|Proteomes:UP000004986};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
CC -!- FUNCTION: Catalyzes, although with low efficiency, the sulfur transfer
CC reaction from thiosulfate to cyanide. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01009};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01009}.
CC -!- SIMILARITY: Belongs to the GlpE family. {ECO:0000256|HAMAP-
CC Rule:MF_01009}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGH42071.1}.
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DR EMBL; AEAI01000313; EGH42071.1; -; Genomic_DNA.
DR AlphaFoldDB; F3G4S1; -.
DR PATRIC; fig|629263.4.peg.1078; -.
DR HOGENOM; CLU_089574_14_0_6; -.
DR Proteomes; UP000004986; Unassembled WGS sequence.
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; Rhodanese-like domain; 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 PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF6; THIOSULFATE SULFURTRANSFERASE GLPE; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01009};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01009, ECO:0000313|EMBL:EGH42071.1}.
FT DOMAIN 16..104
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT ACT_SITE 64
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01009"
SQ SEQUENCE 106 AA; 11748 MW; FBB5F9A2BD6EE08F CRC64;
MTEFKRIPPE QAQALREQGA VLVDVRDPQA FESNHIPDSV HLDNHSIADF IREADLDKPL
VVVCYHGNSS QSAAAYLVGQ GFSDVYSVDG GFELWRATYP QETVQG
//
