ID   THT3_MYCTO              Reviewed;         284 AA.
AC   P9WHF4; L0TAR9; Q59570;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Putative thiosulfate sulfurtransferase SseB;
DE            EC=2.8.1.1;
GN   Name=sseB; OrderedLocusNames=MT2348;
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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK46633.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46633.1; ALT_INIT; Genomic_DNA.
DR   PIR; G70732; G70732.
DR   RefSeq; WP_003899253.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHF4; -.
DR   SMR; P9WHF4; -.
DR   EnsemblBacteria; AAK46633; AAK46633; MT2348.
DR   KEGG; mtc:MT2348; -.
DR   PATRIC; fig|83331.31.peg.2527; -.
DR   HOGENOM; CLU_031618_0_0_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   InterPro; IPR045078; TST/MPST-like.
DR   PANTHER; PTHR11364; PTHR11364; 1.
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   Repeat; Transferase.
FT   CHAIN           1..284
FT                   /note="Putative thiosulfate sulfurtransferase SseB"
FT                   /id="PRO_0000428196"
FT   DOMAIN          20..138
FT                   /note="Rhodanese 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          169..280
FT                   /note="Rhodanese 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   ACT_SITE        241
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   284 AA;  29400 MW;  DF6D44E63EB6BD90 CRC64;
     MQARGQVLIT AAELAGMIQA GDPVSILDVR WRLDEPDGHA AYLQGHLPGA VFVSLEDELS
     DHTIAGRGRH PLPSGASLQA TVRRCGIRHD VPVVVYDDWN RAGSARAWWV LTAAGIANVR
     ILDGGLPAWR SAGGSIETGQ VSPQLGNVTV LHDDLYAGQR LTLTAQQAGA GGVTLLDARV
     PERFRGDVEP VDAVAGHIPG AINVPSGSVL ADDGTFLGNG ALNALLSDHG IDHGGRVGVY
     CGSGVSAAVI VAALAVIGQD AELFPGSWSE WSSDPTRPVG RGTA