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GLPE_AERHH
ID   GLPE_AERHH              Reviewed;         107 AA.
AC   A0KEH8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=AHA_0106;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC   2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK36237.1; -; Genomic_DNA.
DR   RefSeq; WP_011704135.1; NC_008570.1.
DR   RefSeq; YP_854635.1; NC_008570.1.
DR   AlphaFoldDB; A0KEH8; -.
DR   SMR; A0KEH8; -.
DR   STRING; 380703.AHA_0106; -.
DR   EnsemblBacteria; ABK36237; ABK36237; AHA_0106.
DR   GeneID; 64356548; -.
DR   KEGG; aha:AHA_0106; -.
DR   PATRIC; fig|380703.7.peg.98; -.
DR   eggNOG; COG0607; Bacteria.
DR   HOGENOM; CLU_089574_14_0_6; -.
DR   OMA; VCYHGIS; -.
DR   Proteomes; UP000000756; 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..107
FT                   /note="Thiosulfate sulfurtransferase GlpE"
FT                   /id="PRO_1000062954"
FT   DOMAIN          17..101
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01009"
FT   ACT_SITE        65
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01009"
SQ   SEQUENCE   107 AA;  11814 MW;  F799290D6AAE215D CRC64;
     MDQFAHISAH DAHQKLAAGA ARLVDIRDPQ SFETAHAVGA FHLTNGTLVR FMNEVDFDTP
     VIVMCYHGNS SQGAAQYLLQ QGYDEVYSLD GGFEAWRREF PIQAGDA
 
 
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