ID   THTR_SACER              Reviewed;         281 AA.
AC   P16385;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Putative thiosulfate sulfurtransferase;
DE            EC=2.8.1.1;
DE   AltName: Full=Rhodanese-like protein;
GN   Name=cysA;
OS   Saccharopolyspora erythraea (Streptomyces erythraeus).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=1836;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 3-16.
RC   STRAIN=WHM22;
RX   PubMed=2294090; DOI=10.1128/jb.172.1.350-360.1990;
RA   Donadio S., Shafiee A., Hutchinson C.R.;
RT   "Disruption of a rhodaneselike gene results in cysteine auxotrophy in
RT   Saccharopolyspora erythraea.";
RL   J. Bacteriol. 172:350-360(1990).
CC   -!- FUNCTION: May be a sulfotransferase involved in the formation of
CC       thiosulfate.
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: The structure consists of 2 domains of very similar
CC       conformation, suggesting a common evolutionary origin. However, the
CC       sequences of the 2 domains are very different.
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; M29612; AAA88535.1; -; Genomic_DNA.
DR   RefSeq; WP_009949184.1; NZ_CP069353.1.
DR   AlphaFoldDB; P16385; -.
DR   SMR; P16385; -.
DR   PRIDE; P16385; -.
DR   OMA; QRPGHVP; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Repeat; Transferase.
FT   CHAIN           1..281
FT                   /note="Putative thiosulfate sulfurtransferase"
FT                   /id="PRO_0000139420"
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   281 AA;  31425 MW;  92CAB84EF69F26AE CRC64;
     MSREEVLVST DWAEQNLNTD GVVFAEVDED TTAYDGGHIP GAIKLDWKNE LQDHVRRDFV
     NREGFEKLLS AKGIGNDDTV ILYGGNNNWF AAYAYWYFKL YGHSDVKLLD GGRKKWELDG
     RELTKEEPNR AATAYKAQEP DASIRAFRDE VVDAIGNKNL VDVRSPDEFA GKLLAPAHLP
     QESAQRAGHI PSAINVPWSK AANEDGTFKS DEELKQVYGE AGLDTDKDTI AYCRIGERSS
     HTWFVLRELL GHTNVKNYDG SWTEYGSLVG VPIENPQEQG A