ID   THT2_MYCLE              Reviewed;         296 AA.
AC   P46700;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Putative thiosulfate sulfurtransferase SseA;
DE            EC=2.8.1.1;
GN   Name=sseA; OrderedLocusNames=ML0728; ORFNames=B1308_C1_127;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7489918; DOI=10.1016/0378-1119(95)00427-8;
RA   Doukhan L., Predich M., Nair G., Dussurget O., Mandic-Mulec I., Cole S.T.,
RA   Smith D.R., Smith I.;
RT   "Genomic organization of the mycobacterial sigma gene cluster.";
RL   Gene 165:67-70(1995).
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   -!- 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; U00012; AAA85919.1; -; Genomic_DNA.
DR   EMBL; AL583919; CAC30237.1; -; Genomic_DNA.
DR   PIR; A87000; A87000.
DR   RefSeq; NP_301568.1; NC_002677.1.
DR   RefSeq; WP_010907892.1; NC_002677.1.
DR   AlphaFoldDB; P46700; -.
DR   SMR; P46700; -.
DR   STRING; 272631.ML0728; -.
DR   EnsemblBacteria; CAC30237; CAC30237; CAC30237.
DR   KEGG; mle:ML0728; -.
DR   PATRIC; fig|272631.5.peg.1324; -.
DR   Leproma; ML0728; -.
DR   eggNOG; COG2897; Bacteria.
DR   HOGENOM; CLU_031618_1_3_11; -.
DR   OMA; GYPRVKG; -.
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; PS00380; RHODANESE_1; 1.
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..296
FT                   /note="Putative thiosulfate sulfurtransferase SseA"
FT                   /id="PRO_0000139417"
FT   DOMAIN          31..138
FT                   /note="Rhodanese 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          168..286
FT                   /note="Rhodanese 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   ACT_SITE        245
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   296 AA;  33235 MW;  D670A07D501014A4 CRC64;
     MPLPTDPSPS LSAYAHPERL VTGDWLYFHL GKPGLAIVES DENVLLYDVG HIPGAVKVDW
     HTDLNDPKVR DYITGEQFAD LMNRKGIARD DTVVIYGDKS NWWAAYALWV FTLFGHPDVR
     LLNGGRDLWL AERRDTSLAV PNKTSTSYPV VNRNDAPIRA FKDDVLAILG TQPLIDVRSL
     DEYTGKCTEM PDSPEESVLR AGHIPTARSI PWEMTVDKSG RFRSSEELER LYDFITPNDK
     TIVYCRIGER SSHTWFVLTH LLGKPGVRNY DGSWTEWGNT VRVPITAGES PGAVPV