P00586 (THTR_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thiosulfate sulfurtransferase
EC=2.8.1.1

Alternative name(s):
Rhodanese

Gene names

Name:

TST

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA By similarity. Formation of iron-sulfur complexes and cyanide detoxification. Binds molecular oxygen and sulfur.
Catalytic activity	Thiosulfate + cyanide = sulfite + thiocyanate.
Subunit structure	Monomer.
Subcellular location	Mitochondrion matrix.
Tissue specificity	Expressed in numerous tissues.
Domain	Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (Ref.8).
Sequence similarities	Contains 2 rhodanese domains.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	RNA-binding
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	rRNA import into mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: Compara mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	5S rRNA binding Inferred from sequence or structural similarity. Source: UniProtKB thiosulfate sulfurtransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 297

296

Thiosulfate sulfurtransferase

PRO_0000139392

Regions

Domain

25 – 143

119

Rhodanese 1

Domain

173 – 288

116

Rhodanese 2

Region

144 – 159

16

Hinge

Sites

Active site

248

1

Cysteine persulfide intermediate Ref.5

Binding site

187

1

Substrate

Binding site

250

1

Substrate

Amino acid modifications

Modified residue

14

1

N6-acetyllysine By similarity

Modified residue

14

1

N6-succinyllysine Ref.7

Modified residue

136

1

N6-acetyllysine By similarity

Modified residue

164

1

Phosphothreonine By similarity

Modified residue

165

1

Phosphotyrosine By similarity

Natural variations

Natural variant

2 – 3

2

Missing in some preparations, has no effect on enzyme activity.

Experimental info

Mutagenesis

187

1

R → L: Reduced rhodanese activity. Ref.6

Mutagenesis

250

1

K → A: No rhodanese activity. Ref.6

Sequence conflict

100

1

D → N AA sequence Ref.4

Sequence conflict

215

1

N → D AA sequence Ref.4

Sequence conflict

220

1

D → N AA sequence Ref.4

Secondary structure

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297

Helix Strand Turn

Details...

Turn

3 – 6

4

Beta strand

9 – 11

3

Helix

13 – 21

9

Turn

26 – 28

3

Beta strand

29 – 33

5

Turn

39 – 41

3

Helix

44 – 50

7

Beta strand

56 – 58

3

Turn

61 – 63

3

Beta strand

69 – 73

5

Helix

78 – 87

10

Beta strand

95 – 99

5

Beta strand

103 – 105

3

Helix

109 – 118

10

Beta strand

124 – 127

4

Helix

130 – 136

7

Helix

159 – 161

3

Helix

165 – 174

10

Beta strand

177 – 181

5

Helix

185 – 189

5

Beta strand

190 – 192

3

Beta strand

195 – 199

5

Beta strand

208 – 210

3

Helix

213 – 216

4

Helix

226 – 235

10

Beta strand

244 – 247

4

Beta strand

249 – 252

4

Helix

254 – 263

10

Beta strand

270 – 274

5

Helix

275 – 282

8

Helix

285 – 287

3

Beta strand

288 – 290

3

Sequences

	Sequence		Length	Mass (Da)
	P00586 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F2F4AA7294F84B1A	FASTA	297	33,296
	10 20 30 40 50 60 MVHQVLYRAL VSTKWLAESV RAGKVGPGLR VLDASWYSPG TREARKEYLE RHVPGASFFD 70 80 90 100 110 120 IEECRDKASP YEVMLPSEAG FADYVGSLGI SNDTHVVVYD GDDLGSFYAP RVWWMFRVFG 130 140 150 160 170 180 HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP AIFKATLNRS LLKTYEQVLE NLESKRFQLV 190 200 210 220 230 240 DSRAQGRYLG TQPEPDAVGL DSGHIRGSVN MPFMNFLTED GFEKSPEELR AMFEAKKVDL 250 260 270 280 290 TKPLIATCRK GVTACHIALA AYLCGKPDVA IYDGSWFEWF HRAPPETWVS QGKGGKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of cloned bovine adrenal rhodanese." Miller D.M., Delgado R., Chirgwin J.M., Hardies S.C., Horowitz P.M. J. Biol. Chem. 266:4686-4691(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Testis.
[4]	"The covalent structure of bovine liver rhodanese. Isolation and partial structural analysis of cyanogen bromide fragements and the complete sequence of the enzyme." Russell J., Weng L., Keim P.S., Heinrikson R.L. J. Biol. Chem. 253:8102-8108(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-295. Tissue: Liver.
[5]	"Active site cysteinyl and arginyl residues of rhodanese. A novel formation of disulfide bonds in the active site promoted by phenylglyoxal." Weng L., Heinrikson R.L., Westley J. J. Biol. Chem. 253:8109-8119(1978) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVE SITE.
[6]	"The sulfurtransferase activity and structure of rhodanese are affected by site-directed replacement of Arg-186 or Lys-249." Luo G.-X., Horowitz P.M. J. Biol. Chem. 269:8220-8225(1994) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ARG-187 AND LYS-250.
[7]	"Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase." Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., Hao Q., Lin H. Science 334:806-809(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUCCINYLATION AT LYS-14.
[8]	"Structure of bovine liver rhodanese. I. Structure determination at 2.5-A resolution and a comparison of the conformation and sequence of its two domains." Ploegman J.H., Drent G., Kalk K.H., Hol W.G.J. J. Mol. Biol. 123:557-594(1978) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[9]	"Binding of metal cyanide complexes to bovine liver rhodanese in the crystalline state." Lijk L.J., Kalk K.H., Brandenburg N.P., Hol W.G.J. Biochemistry 22:2952-2957(1983) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[10]	"Active site structural features for chemically modified forms of rhodanese." Gliubich F., Gazerro M., Zanotti G., Delbono S., Bombieri G., Berni R. J. Biol. Chem. 271:21054-21061(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS).
[11]	"Structure of sulfur-substituted rhodanese at 1.36-A resolution." Gliubich F., Berni R., Colapietro M., Barba L., Zanotti G. Acta Crystallogr. D 54:481-486(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M58561 mRNA. Translation: AAA30753.1.
BT020995 mRNA. Translation: AAX09012.1.
BC112580 mRNA. Translation: AAI12581.1.

IPI

IPI00708679.

PIR

ROBO. A23704.

RefSeq

NP_803455.1. NM_177489.3.
XP_001249946.1. XM_001249945.4.

UniGene

Bt.51597.
Bt.89197.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BOH	X-ray	2.30	A	2-296	[»]
1BOI	X-ray	2.20	A	2-296	[»]
1DP2	X-ray	2.01	A	2-294	[»]
1ORB	X-ray	2.00	A	2-297	[»]
1RHD	X-ray	2.50	A	2-294	[»]
1RHS	X-ray	1.36	A	2-297	[»]
2ORA	X-ray	1.99	A	2-297	[»]

ProteinModelPortal

P00586.

SMR

P00586. Positions 2-294.

ModBase

Search...

Protein-protein interaction databases

STRING

9913.ENSBTAP00000040894.

Proteomic databases

PaxDb

P00586.

PRIDE

P00586.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000043317; ENSBTAP00000040894; ENSBTAG00000030650.

GeneID

280946.
783512.

KEGG

bta:280946.
bta:783512.

Organism-specific databases

CTD

7263.

Phylogenomic databases

eggNOG

COG2897.

GeneTree

ENSGT00510000046773.

HOGENOM

HOG000157237.

HOVERGEN

HBG002345.

InParanoid

P00586.

KO

K01011.

OMA

SRAQGRY.

OrthoDB

EOG466VMJ.

Enzyme and pathway databases

BioCyc

CATTLE:280946-MONOMER.
CATTLE:783512-MONOMER.

Family and domain databases

Gene3D

3.40.250.10. 2 hits.

InterPro

IPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]

Pfam

PF00581. Rhodanese. 2 hits.
[Graphical view]

SMART

SM00450. RHOD. 2 hits.
[Graphical view]

SUPFAM

SSF52821. Rhodanese-like. 2 hits.

PROSITE

PS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00586.

NextBio

20805059.

PMAP-CutDB

P00586.

Entry information

Entry name

THTR_BOVIN

Accession

Primary (citable) accession number: P00586
Secondary accession number(s): Q2KIM8, Q5E9C5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 120 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program