ID   THT2_MYCTO              Reviewed;         297 AA.
AC   P9WHF6; L0TC30; P96888;
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 SseA;
DE            EC=2.8.1.1;
GN   Name=sseA; OrderedLocusNames=MT3382;
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}.
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DR   EMBL; AE000516; AAK47725.1; -; Genomic_DNA.
DR   PIR; D70980; D70980.
DR   RefSeq; WP_003417149.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHF6; -.
DR   SMR; P9WHF6; -.
DR   EnsemblBacteria; AAK47725; AAK47725; MT3382.
DR   GeneID; 45427279; -.
DR   KEGG; mtc:MT3382; -.
DR   PATRIC; fig|83331.31.peg.3640; -.
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; 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..297
FT                   /note="Putative thiosulfate sulfurtransferase SseA"
FT                   /id="PRO_0000428195"
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   297 AA;  33320 MW;  5930AB5F9C63A533 CRC64;
     MPLPADPSPT LSAYAHPERL VTADWLSAHM GAPGLAIVES DEDVLLYDVG HIPGAVKIDW
     HTDLNDPRVR DYINGEQFAE LMDRKGIARD DTVVIYGDKS NWWAAYALWV FTLFGHADVR
     LLNGGRDLWL AERRETTLDV PTKTCTGYPV VQRNDAPIRA FRDDVLAILG AQPLIDVRSP
     EEYTGKRTHM PDYPEEGALR AGHIPTAVHI PWGKAADESG RFRSREELER LYDFINPDDQ
     TVVYCRIGER SSHTWFVLTH LLGKADVRNY DGSWTEWGNA VRVPIVAGEE PGVVPVV