ID   THTR_MYCLE              Reviewed;         277 AA.
AC   Q50036;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Putative thiosulfate sulfurtransferase;
DE            EC=2.8.1.1;
DE   AltName: Full=Rhodanese-like protein;
GN   Name=cysA; Synonyms=cysA3; OrderedLocusNames=ML2198;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: May be a sulfotransferase involved in the formation of
CC       thiosulfate.
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;
CC   -!- DOMAIN: Contains two rhodanese domains with different primary
CC       structures but with near identical secondary structure conformations
CC       suggesting a common evolutionary origin. Only the C-terminal rhodanese
CC       domain contains the catalytic cysteine residue (By similarity).
CC       {ECO:0000250}.
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DR   EMBL; U15182; AAA62982.1; -; Genomic_DNA.
DR   EMBL; AL583924; CAC31153.1; -; Genomic_DNA.
DR   PIR; A87184; A87184.
DR   RefSeq; NP_302440.1; NC_002677.1.
DR   RefSeq; WP_010908760.1; NC_002677.1.
DR   AlphaFoldDB; Q50036; -.
DR   SMR; Q50036; -.
DR   STRING; 272631.ML2198; -.
DR   EnsemblBacteria; CAC31153; CAC31153; CAC31153.
DR   KEGG; mle:ML2198; -.
DR   PATRIC; fig|272631.5.peg.4165; -.
DR   Leproma; ML2198; -.
DR   eggNOG; COG2897; Bacteria.
DR   HOGENOM; CLU_031618_1_3_11; -.
DR   OMA; QRPGHVP; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.250.10; -; 2.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR   Pfam; PF00581; Rhodanese; 2.
DR   SMART; SM00450; RHOD; 2.
DR   SUPFAM; SSF52821; SSF52821; 2.
DR   PROSITE; PS00683; RHODANESE_2; 1.
DR   PROSITE; PS50206; RHODANESE_3; 2.
PE   3: Inferred from homology;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..277
FT                   /note="Putative thiosulfate sulfurtransferase"
FT                   /id="PRO_0000139414"
FT   DOMAIN          18..125
FT                   /note="Rhodanese 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          154..274
FT                   /note="Rhodanese 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   ACT_SITE        233
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   277 AA;  31095 MW;  527E05C9FE93969D CRC64;
     MARSDVLVSA DWAESNLDSA NIVFVEVDED TSTYDGDHIA GAIKLDWRAD LQDPIKRDFI
     DTQQFSKLLG DRGISNDNTV ILYGGNNNWF AAYAYWYFKL YRHDKVKLLD GGRKKWELDG
     RPLSTDTVTR PATSYAAAAP DNTIRAFRDE VIASIKIKNL VDVRSPDEFS GKLLAPAHLP
     QEQSQRPGHI PSAINIPWSK AANEDGTFKS DEQLAKLYAD AGLDRLKETI VYCRIGERSS
     HTWFVLRELL GYQNVKNYDG SWTEYGSLVG VPIELGS