THTR_BOVIN
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 03-AUG-2022, entry version 182.
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}.
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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 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 PDBsum; 1BOH; -.
DR PDBsum; 1BOI; -.
DR PDBsum; 1DP2; -.
DR PDBsum; 1ORB; -.
DR PDBsum; 1RHD; -.
DR PDBsum; 1RHS; -.
DR PDBsum; 2ORA; -.
DR AlphaFoldDB; P00586; -.
DR PCDDB; P00586; -.
DR SMR; P00586; -.
DR IntAct; P00586; 2.
DR MINT; P00586; -.
DR STRING; 9913.ENSBTAP00000040894; -.
DR PaxDb; P00586; -.
DR PeptideAtlas; P00586; -.
DR PRIDE; 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 OrthoDB; 1553525at2759; -.
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 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 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
