ID   THTR_CHICK              Reviewed;         289 AA.
AC   P25324;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Thiosulfate sulfurtransferase;
DE            EC=2.8.1.1;
DE   AltName: Full=Rhodanese;
GN   Name=TST;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=2275748; DOI=10.1007/bf01024612;
RA   Kohanski R.A., Heinrikson R.L.;
RT   "Primary structure of avian hepatic rhodanese.";
RL   J. Protein Chem. 9:369-377(1990).
CC   -!- FUNCTION: Together with MRPL18, acts as a mitochondrial import factor
CC       for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form
CC       is able to bind to the 5S rRNA (By similarity). Formation of iron-
CC       sulfur complexes and cyanide detoxification. {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   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- TISSUE SPECIFICITY: Expressed in numerous tissues.
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   PIR; A37209; A37209.
DR   AlphaFoldDB; P25324; -.
DR   SMR; P25324; -.
DR   STRING; 9031.ENSGALP00000020374; -.
DR   PaxDb; P25324; -.
DR   VEuPathDB; HostDB:geneid_418049; -.
DR   eggNOG; KOG1529; Eukaryota.
DR   InParanoid; P25324; -.
DR   OrthoDB; 1553525at2759; -.
DR   PhylomeDB; P25324; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0008097; F:5S rRNA binding; ISS:UniProtKB.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IBA:GO_Central.
DR   GO; GO:0035928; P:rRNA import into mitochondrion; ISS:UniProtKB.
DR   GO; GO:0051029; P:rRNA transport; ISS:UniProtKB.
DR   GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Mitochondrion; Reference proteome; Repeat;
KW   RNA-binding; Transferase.
FT   CHAIN           1..289
FT                   /note="Thiosulfate sulfurtransferase"
FT                   /id="PRO_0000139393"
FT   DOMAIN          24..142
FT                   /note="Rhodanese 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          172..284
FT                   /note="Rhodanese 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   REGION          143..158
FT                   /note="Hinge"
FT   ACT_SITE        244
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   289 AA;  32287 MW;  8BFCF671DE0B2BA4 CRC64;
     AAQALGRALV SAKWLSEAVR AGRVGAGLRV LDASWYPPEE RDARQEFKER HIPGASFFNI
     EECRDKSSPY DFMLPSEAHF ADYVGRLGVS NDTHVVVYDG DELGTFYAPR AWWMFRAFGH
     REVSVLNGGF KNWVKEGHPV TAEPSQPAEA VFKAKLDKTL LKTFEQAMEN VGSKKFQVVD
     SRPAGRFQGT ELDQGLESGH IPGAVNMPFS TFLTESGHEK SIEEIQQMFR EKKVDLSKPL
     TATCRKGVTA CHIALAAYLC GKPDVAVYDG SWSEWFHRAP PQYKVTELK