ID   THTR_METTH              Reviewed;         286 AA.
AC   O26719;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Putative thiosulfate sulfurtransferase;
DE            EC=2.8.1.1;
GN   OrderedLocusNames=MTH_622;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000666; AAB85128.1; -; Genomic_DNA.
DR   PIR; G69182; G69182.
DR   RefSeq; WP_010876261.1; NC_000916.1.
DR   AlphaFoldDB; O26719; -.
DR   SMR; O26719; -.
DR   STRING; 187420.MTH_622; -.
DR   PaxDb; 187420-MTH_622; -.
DR   EnsemblBacteria; AAB85128; AAB85128; MTH_622.
DR   GeneID; 82297081; -.
DR   KEGG; mth:MTH_622; -.
DR   PATRIC; fig|187420.15.peg.603; -.
DR   HOGENOM; CLU_031618_1_7_2; -.
DR   InParanoid; O26719; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd01448; TST_Repeat_1; 1.
DR   CDD; cd01449; TST_Repeat_2; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 2.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR   PANTHER; PTHR43855; THIOSULFATE SULFURTRANSFERASE; 1.
DR   PANTHER; PTHR43855:SF1; THIOSULFATE SULFURTRANSFERASE SSEA-RELATED; 1.
DR   Pfam; PF00581; Rhodanese; 2.
DR   SMART; SM00450; RHOD; 2.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 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..286
FT                   /note="Putative thiosulfate sulfurtransferase"
FT                   /id="PRO_0000139421"
FT   DOMAIN          22..137
FT                   /note="Rhodanese 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          167..280
FT                   /note="Rhodanese 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   ACT_SITE        239
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
SQ   SEQUENCE   286 AA;  32165 MW;  AE8E020D0DECD523 CRC64;
     MEPYGKGDGR VRWVTPEWLM ENMEDVAIID CQPNIHDYIL EHIPGAVYLN EGLFREPRGK
     APAMYIPEGA VELIFQQAGI ENRPTVVYTG TGGVKGWGDG LEQTMVAYSL ARFGHENILV
     LNGGLAEWKR AGGELTKVFP EVEESGFSAV TKEDFYIEYP EFKRIKDDED VLLLDARPAE
     VYEGQGPWIK PGHIPGAVNL PWADLMDPEN RTLLKPEDEI LELVNSVGAT PDRKIICSCG
     TGREATNEFL LFRWYLGYPD VRIYEGSFTE WTQIEDNPTV TGPDPR
//