Reviewed, UniProtKB/Swiss-Prot P00586 (THTR_BOVIN)

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)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › 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	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	The structure consists of 2 domains of very similar conformation, suggesting a common evolutionary origin. However, the sequences of the 2 domains are very different.
Sequence similarities	Contains 2 rhodanese domains.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Repeat
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	sulfate transport Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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

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

1

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297

Helix Strand Turn

Details...

Beta strand

9 – 11

3

Helix

13 – 21

9

Beta strand

29 – 33

5

Helix

44 – 50

7

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

195 – 199

5

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)
	P00586-1 [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: 2002017] [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: 16305752] [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: 711737] [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: 711738] [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: 8132546] [Abstract] Cited for: MUTAGENESIS OF ARG-187 AND LYS-250.
[7]	"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: 691057] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[8]	"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: 6575830] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[9]	"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: 8702871] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS).
[10]	"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: 9761843] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

IPI

IPI00708679.

PIR

ROBO. A23704.

RefSeq

NP_803455.1.
XP_001249946.1.

UniGene

Bt.51597
Bt.89197

3D structure databases

PDBPDBe

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	2-293	[»]
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	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSBTAG00000030650. Bos taurus. [Contig view]
ENSBTAG00000035936. Bos taurus. [Contig view]

GeneID

280946.
783512.

KEGG

bta:280946.
bta:783512.

Phylogenomic databases

HOVERGEN

P00586.

OMA

P00586. ATCRKGV.

Enzyme and pathway databases

BRENDA

2.8.1.1. 251.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.40.250.10. Rhodanese-like. 2 hits.

Pfam

PF00581. Rhodanese. 2 hits.
[Graphical view]

SMART

SM00450. RHOD. 2 hits.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

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:	June 16, 2009
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)