ID   THTR_MYCTO              Reviewed;         277 AA.
AC   P9WHF8; L0TBW4; O05793;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Putative thiosulfate sulfurtransferase;
DE            EC=2.8.1.1;
DE   AltName: Full=Rhodanese-like protein;
GN   Name=cysA1; Synonyms=cysA; OrderedLocusNames=MT3199;
GN   and
GN   Name=cysA2; OrderedLocusNames=MT0837;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: May be a sulfotransferase involved in the formation of
CC       thiosulfate. {ECO:0000250}.
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; AE000516; AAK45079.1; -; Genomic_DNA.
DR   EMBL; AE000516; AAK47539.1; -; Genomic_DNA.
DR   PIR; G70809; G70809.
DR   RefSeq; WP_003404293.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHF8; -.
DR   SMR; P9WHF8; -.
DR   EnsemblBacteria; AAK45079; AAK45079; MT0837.
DR   EnsemblBacteria; AAK47539; AAK47539; MT3199.
DR   KEGG; mtc:MT0837; -.
DR   KEGG; mtc:MT3199; -.
DR   PATRIC; fig|83331.31.peg.3449; -.
DR   HOGENOM; CLU_031618_1_3_11; -.
DR   Proteomes; UP000001020; 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   Repeat; Transferase.
FT   CHAIN           1..277
FT                   /note="Putative thiosulfate sulfurtransferase"
FT                   /id="PRO_0000428194"
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;  31015 MW;  AC37B715D99565A9 CRC64;
     MARCDVLVSA DWAESNLHAP KVVFVEVDED TSAYDRDHIA GAIKLDWRTD LQDPVKRDFV
     DAQQFSKLLS ERGIANEDTV ILYGGNNNWF AAYAYWYFKL YGHEKVKLLD GGRKKWELDG
     RPLSSDPVSR PVTSYTASPP DNTIRAFRDE VLAAINVKNL IDVRSPDEFS GKILAPAHLP
     QEQSQRPGHI PGAINVPWSR AANEDGTFKS DEELAKLYAD AGLDNSKETI AYCRIGERSS
     HTWFVLRELL GHQNVKNYDG SWTEYGSLVG APIELGS