ID R1H554_9GAMM Unreviewed; 107 AA.
AC R1H554;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 ORFNames=G113_07742 {ECO:0000313|EMBL:EOD55671.1};
OS Aeromonas molluscorum 848.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1268236 {ECO:0000313|EMBL:EOD55671.1, ECO:0000313|Proteomes:UP000013526};
RN [1] {ECO:0000313|EMBL:EOD55671.1, ECO:0000313|Proteomes:UP000013526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=848 {ECO:0000313|EMBL:EOD55671.1,
RC ECO:0000313|Proteomes:UP000013526};
RX PubMed=23788549;
RA Spataro N., Farfan M., Albarral V., Sanglas A., Loren J.G., Fuste M.C.,
RA Bosch E.;
RT "Draft Genome Sequence of Aeromonas molluscorum Strain 848TT, Isolated from
RT Bivalve Molluscs.";
RL Genome Announc. 1:E00382-13(2013).
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:EOD55671.1}.
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DR EMBL; AQGQ01000035; EOD55671.1; -; Genomic_DNA.
DR RefSeq; WP_005897984.1; NZ_AQGQ01000035.1.
DR AlphaFoldDB; R1H554; -.
DR PATRIC; fig|1268236.3.peg.1537; -.
DR OrthoDB; 9811849at2; -.
DR Proteomes; UP000013526; 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:EOD55671.1}.
FT DOMAIN 17..101
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT ACT_SITE 65
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01009"
SQ SEQUENCE 107 AA; 11789 MW; D6F37B7CA3E65EA2 CRC64;
MDQFAHISAQ DAYAKLAAGE ARLVDIRDPQ SFETSHAVGA FHLTNGSLVR FMDEVDFDTP
VIVICYHGNS SQGAAQYLLQ QGYDEVYSLD GGFEAWRKEF PIQAGDA
//
