THTR_CRIGR
ID THTR_CRIGR Reviewed; 297 AA.
AC P46635;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Thiosulfate sulfurtransferase;
DE EC=2.8.1.1;
DE AltName: Full=Rhodanese;
GN Name=TST;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=8535164; DOI=10.1006/prep.1995.1091;
RA Trevino R.J., Hunt J., Horowitz P.M., Chirgwin J.M.;
RT "Chinese hamster rhodanese cDNA: activity of the expressed protein is not
RT blocked by a C-terminal extension.";
RL Protein Expr. Purif. 6:693-699(1995).
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. Binds molecular oxygen and
CC sulfur. {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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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; U23943; AAB84305.1; -; mRNA.
DR RefSeq; NP_001233676.1; NM_001246747.1.
DR AlphaFoldDB; P46635; -.
DR SMR; P46635; -.
DR STRING; 10029.NP_001233676.1; -.
DR GeneID; 100689314; -.
DR KEGG; cge:100689314; -.
DR CTD; 7263; -.
DR eggNOG; KOG1529; Eukaryota.
DR OrthoDB; 1553525at2759; -.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0008097; F:5S rRNA binding; ISS:UniProtKB.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0035928; P:rRNA import into mitochondrion; ISS:UniProtKB.
DR GO; GO:0051029; P:rRNA transport; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Glycoprotein; Mitochondrion; Phosphoprotein; Repeat;
KW RNA-binding; Transferase.
FT CHAIN 1..297
FT /note="Thiosulfate sulfurtransferase"
FT /id="PRO_0000139394"
FT DOMAIN 25..143
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 173..288
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 144..159
FT /note="Hinge"
FT ACT_SITE 248
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 14
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16762"
FT MOD_RES 14
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00586"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24329"
FT MOD_RES 136
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 136
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 163
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 175
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 175
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 224
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 224
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 236
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 237
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 237
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT CARBOHYD 35
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 297 AA; 33337 MW; B2933ECF97285C6D CRC64;
MVHQVLYRAL VSTKWLAESI RSGSLGPGLR VLDASWYSPG TRQARKEYQE RHVPGASFFD
IEECRDTTSP YEMMLPSEAH FADYVGSLGI SNDTHVVVYD GDNLGSFYAP RVWWMFRVFG
HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP AVFKATLDRS LLKTYEQVLE NLQSKRFQLV
DSRAQGRYLG TEPEPDIVGL DSGHIRGSAN MPFMNFLTED GFEKSPEELR AIFQDKKVDL
SQPLIATCRK GVTACHIALA AYLCGKPDVA VYDGSWSEWF HQAPPETRVS QGKSGKA
