ID   THTR2_MYCBO             Reviewed;         320 AA.
AC   Q7TX80; A0A1R3Y373; X2BMN5;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Putative thiosulfate sulfurtransferase 2;
DE            EC=2.8.1.1;
DE   AltName: Full=Rhodanese-like protein 2;
GN   Name=cysA2; OrderedLocusNames=BQ2027_MB3144;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU01770.1; -; Genomic_DNA.
DR   RefSeq; NP_856789.1; NC_002945.3.
DR   RefSeq; WP_010950830.1; NC_002945.4.
DR   AlphaFoldDB; Q7TX80; -.
DR   SMR; Q7TX80; -.
DR   EnsemblBacteria; SIU01770; SIU01770; BQ2027_MB3144.
DR   PATRIC; fig|233413.5.peg.3456; -.
DR   OMA; FCPRKGR; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.250.10; -; 2.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   Pfam; PF00581; Rhodanese; 2.
DR   SMART; SM00450; RHOD; 2.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   SUPFAM; SSF52821; SSF52821; 2.
DR   PROSITE; PS50206; RHODANESE_3; 2.
PE   3: Inferred from homology;
KW   Repeat; Transferase.
FT   CHAIN           1..320
FT                   /note="Putative thiosulfate sulfurtransferase 2"
FT                   /id="PRO_0000139413"
FT   DOMAIN          18..125
FT                   /note="Rhodanese 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          154..267
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   320 AA;  35999 MW;  4D6427752BDB7B1D 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 GHQNVNIAFG YGPHACPASA YSRMCLTTFF TSLTQRFPQL QLARPFEDLE
     RRGKGLHSVG IKELLVTWPT