ID THTR_BOVIN Reviewed; 297 AA. AC P00586; Q2KIM8; Q5E9C5; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 188. DE RecName: Full=Thiosulfate sulfurtransferase; DE EC=2.8.1.1 {ECO:0000269|PubMed:711738}; DE AltName: Full=Rhodanese; GN Name=TST; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2002017; DOI=10.1016/s0021-9258(19)67703-3; RA Miller D.M., Delgado R., Chirgwin J.M., Hardies S.C., Horowitz P.M.; RT "Expression of cloned bovine adrenal rhodanese."; RL J. Biol. Chem. 266:4686-4691(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Testis; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEIN SEQUENCE OF 2-295. RC TISSUE=Liver; RX PubMed=711737; DOI=10.1016/s0021-9258(17)34368-5; RA Russell J., Weng L., Keim P.S., Heinrikson R.L.; RT "The covalent structure of bovine liver rhodanese. Isolation and partial RT structural analysis of cyanogen bromide fragements and the complete RT sequence of the enzyme."; RL J. Biol. Chem. 253:8102-8108(1978). RN [5] RP CATALYTIC ACTIVITY, AND ACTIVE SITE. RX PubMed=711738; DOI=10.1016/s0021-9258(17)34369-7; RA Weng L., Heinrikson R.L., Westley J.; RT "Active site cysteinyl and arginyl residues of rhodanese. A novel formation RT of disulfide bonds in the active site promoted by phenylglyoxal."; RL J. Biol. Chem. 253:8109-8119(1978). RN [6] RP MUTAGENESIS OF ARG-187 AND LYS-250. RX PubMed=8132546; DOI=10.1016/s0021-9258(17)37182-x; RA Luo G.-X., Horowitz P.M.; RT "The sulfurtransferase activity and structure of rhodanese are affected by RT site-directed replacement of Arg-186 or Lys-249."; RL J. Biol. Chem. 269:8220-8225(1994). RN [7] RP SUCCINYLATION AT LYS-14. RX PubMed=22076378; DOI=10.1126/science.1207861; RA Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., RA Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., RA Hao Q., Lin H.; RT "Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase."; RL Science 334:806-809(2011). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=691057; DOI=10.1016/0022-2836(78)90207-3; RA Ploegman J.H., Drent G., Kalk K.H., Hol W.G.J.; RT "Structure of bovine liver rhodanese. I. Structure determination at 2.5-A RT resolution and a comparison of the conformation and sequence of its two RT domains."; RL J. Mol. Biol. 123:557-594(1978). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=6575830; DOI=10.1021/bi00281a026; RA Lijk L.J., Kalk K.H., Brandenburg N.P., Hol W.G.J.; RT "Binding of metal cyanide complexes to bovine liver rhodanese in the RT crystalline state."; RL Biochemistry 22:2952-2957(1983). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS). RX PubMed=8702871; DOI=10.1074/jbc.271.35.21054; RA Gliubich F., Gazerro M., Zanotti G., Delbono S., Bombieri G., Berni R.; RT "Active site structural features for chemically modified forms of RT rhodanese."; RL J. Biol. Chem. 271:21054-21061(1996). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS). RX PubMed=9761843; DOI=10.1107/s090744499701216x; RA Gliubich F., Berni R., Colapietro M., Barba L., Zanotti G.; RT "Structure of sulfur-substituted rhodanese at 1.36-A resolution."; RL Acta Crystallogr. D 54:481-486(1998). 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; Evidence={ECO:0000269|PubMed:711738}; CC -!- SUBUNIT: Monomer. CC -!- INTERACTION: CC P00586; P0A6F5: groEL; Xeno; NbExp=2; IntAct=EBI-7900146, EBI-543750; 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 (PubMed:691057). CC {ECO:0000269|PubMed:691057}. 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; M58561; AAA30753.1; -; mRNA. DR EMBL; BT020995; AAX09012.1; -; mRNA. DR EMBL; BC112580; AAI12581.1; -; mRNA. DR PIR; A23704; ROBO. DR RefSeq; NP_803455.1; NM_177489.3. DR RefSeq; XP_010803625.2; XM_010805323.2. DR PDB; 1BOH; X-ray; 2.30 A; A=2-297. DR PDB; 1BOI; X-ray; 2.20 A; A=2-297. DR PDB; 1DP2; X-ray; 2.01 A; A=2-294. DR PDB; 1ORB; X-ray; 2.00 A; A=2-297. DR PDB; 1RHD; X-ray; 2.50 A; A=2-294. DR PDB; 1RHS; X-ray; 1.36 A; A=2-297. DR PDB; 2ORA; X-ray; 1.99 A; A=2-297. DR PDB; 8Q5Z; X-ray; 1.50 A; A=1-297. DR PDBsum; 1BOH; -. DR PDBsum; 1BOI; -. DR PDBsum; 1DP2; -. DR PDBsum; 1ORB; -. DR PDBsum; 1RHD; -. DR PDBsum; 1RHS; -. DR PDBsum; 2ORA; -. DR PDBsum; 8Q5Z; -. DR AlphaFoldDB; P00586; -. DR PCDDB; P00586; -. DR SMR; P00586; -. DR IntAct; P00586; 2. DR MINT; P00586; -. DR STRING; 9913.ENSBTAP00000040894; -. DR GlyCosmos; P00586; 1 site, No reported glycans. DR PaxDb; 9913-ENSBTAP00000040894; -. DR PeptideAtlas; P00586; -. DR GeneID; 280946; -. DR KEGG; bta:280946; -. DR CTD; 7263; -. DR eggNOG; KOG1529; Eukaryota. DR HOGENOM; CLU_031618_3_1_1; -. DR InParanoid; P00586; -. DR TreeFam; TF315133; -. DR BRENDA; 2.8.1.1; 908. DR EvolutionaryTrace; P00586; -. DR Proteomes; UP000009136; 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 CDD; cd01445; TST_Repeats; 2. 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 InterPro; IPR045078; TST/MPST-like. DR PANTHER; PTHR11364; THIOSULFATE SULFERTANSFERASE; 1. DR PANTHER; PTHR11364:SF6; THIOSULFATE SULFURTRANSFERASE; 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 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Glycoprotein; KW Mitochondrion; Phosphoprotein; Reference proteome; Repeat; RNA-binding; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:711737" FT CHAIN 2..297 FT /note="Thiosulfate sulfurtransferase" FT /id="PRO_0000139392" 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 ECO:0000269|PubMed:711738" FT BINDING 187 FT /ligand="substrate" FT BINDING 250 FT /ligand="substrate" 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:0000269|PubMed:22076378" 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" FT VARIANT 2..3 FT /note="Missing (in some preparations, has no effect on FT enzyme activity)" FT MUTAGEN 187 FT /note="R->L: Reduced rhodanese activity." FT /evidence="ECO:0000269|PubMed:8132546" FT MUTAGEN 250 FT /note="K->A: No rhodanese activity." FT /evidence="ECO:0000269|PubMed:8132546" FT CONFLICT 100 FT /note="D -> N (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 215 FT /note="N -> D (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 220 FT /note="D -> N (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT TURN 3..6 FT /evidence="ECO:0007829|PDB:1BOH" FT STRAND 9..11 FT /evidence="ECO:0007829|PDB:1RHS" FT HELIX 13..21 FT /evidence="ECO:0007829|PDB:1RHS" FT TURN 26..28 FT /evidence="ECO:0007829|PDB:1RHD" FT STRAND 29..33 FT /evidence="ECO:0007829|PDB:1RHS" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:1ORB" FT HELIX 44..50 FT /evidence="ECO:0007829|PDB:1RHS" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:1BOH" FT TURN 61..63 FT /evidence="ECO:0007829|PDB:1RHS" FT STRAND 69..73 FT /evidence="ECO:0007829|PDB:1RHS" FT HELIX 78..87 FT /evidence="ECO:0007829|PDB:1RHS" FT STRAND 95..99 FT /evidence="ECO:0007829|PDB:1RHS" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:1RHS" FT HELIX 109..118 FT /evidence="ECO:0007829|PDB:1RHS" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:1RHS" FT HELIX 130..136 FT /evidence="ECO:0007829|PDB:1RHS" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:1RHS" FT HELIX 165..174 FT /evidence="ECO:0007829|PDB:1RHS" FT STRAND 177..181 FT /evidence="ECO:0007829|PDB:1RHS" FT HELIX 185..189 FT /evidence="ECO:0007829|PDB:1RHS" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:2ORA" FT STRAND 195..199 FT /evidence="ECO:0007829|PDB:1RHS" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:1ORB" FT HELIX 213..216 FT /evidence="ECO:0007829|PDB:1RHS" FT HELIX 226..235 FT /evidence="ECO:0007829|PDB:1RHS" FT STRAND 244..247 FT /evidence="ECO:0007829|PDB:1RHS" FT STRAND 249..252 FT /evidence="ECO:0007829|PDB:1RHS" FT HELIX 254..263 FT /evidence="ECO:0007829|PDB:1RHS" FT STRAND 270..274 FT /evidence="ECO:0007829|PDB:1RHS" FT HELIX 275..282 FT /evidence="ECO:0007829|PDB:1RHS" FT HELIX 285..287 FT /evidence="ECO:0007829|PDB:1RHS" FT STRAND 288..290 FT /evidence="ECO:0007829|PDB:1RHS" SQ SEQUENCE 297 AA; 33296 MW; F2F4AA7294F84B1A CRC64; MVHQVLYRAL VSTKWLAESV RAGKVGPGLR VLDASWYSPG TREARKEYLE RHVPGASFFD IEECRDKASP YEVMLPSEAG FADYVGSLGI SNDTHVVVYD GDDLGSFYAP RVWWMFRVFG HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP AIFKATLNRS LLKTYEQVLE NLESKRFQLV DSRAQGRYLG TQPEPDAVGL DSGHIRGSVN MPFMNFLTED GFEKSPEELR AMFEAKKVDL TKPLIATCRK GVTACHIALA AYLCGKPDVA IYDGSWFEWF HRAPPETWVS QGKGGKA //