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P00586 (THTR_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiosulfate sulfurtransferase

EC=2.8.1.1
Alternative name(s):
Rhodanese
Gene names
Name:TST
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

groLP0A6F52EBI-7900146,EBI-543750From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 297296Thiosulfate sulfurtransferase
PRO_0000139392

Regions

Domain25 – 143119Rhodanese 1
Domain173 – 288116Rhodanese 2
Region144 – 15916Hinge

Sites

Active site2481Cysteine persulfide intermediate Ref.5
Binding site1871Substrate
Binding site2501Substrate

Amino acid modifications

Modified residue141N6-acetyllysine; alternate By similarity
Modified residue141N6-succinyllysine; alternate Ref.7
Modified residue1361N6-acetyllysine; alternate By similarity
Modified residue1361N6-succinyllysine; alternate By similarity
Modified residue1631N6-acetyllysine By similarity
Modified residue1751N6-acetyllysine; alternate By similarity
Modified residue1751N6-succinyllysine; alternate By similarity
Modified residue2241N6-acetyllysine; alternate By similarity
Modified residue2241N6-succinyllysine; alternate By similarity
Modified residue2361N6-acetyllysine By similarity
Modified residue2371N6-acetyllysine; alternate By similarity
Modified residue2371N6-succinyllysine; alternate By similarity

Natural variations

Natural variant2 – 32Missing in some preparations, has no effect on enzyme activity.

Experimental info

Mutagenesis1871R → L: Reduced rhodanese activity. Ref.6
Mutagenesis2501K → A: No rhodanese activity. Ref.6
Sequence conflict1001D → N AA sequence Ref.4
Sequence conflict2151N → D AA sequence Ref.4
Sequence conflict2201D → N AA sequence Ref.4

Secondary structure

............................................................. 297
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00586 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F2F4AA7294F84B1A

FASTA29733,296
        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 

« Hide

References

« Hide '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.
PIRROBO. A23704.
RefSeqNP_803455.1. NM_177489.3.
XP_001249946.1. XM_001249945.5.
UniGeneBt.51597.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOHX-ray2.30A2-296[»]
1BOIX-ray2.20A2-296[»]
1DP2X-ray2.01A2-294[»]
1ORBX-ray2.00A2-297[»]
1RHDX-ray2.50A2-294[»]
1RHSX-ray1.36A2-297[»]
2ORAX-ray1.99A2-297[»]
ProteinModelPortalP00586.
SMRP00586. Positions 2-294.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00586. 2 interactions.
STRING9913.ENSBTAP00000040894.

Proteomic databases

PaxDbP00586.
PRIDEP00586.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000043317; ENSBTAP00000040894; ENSBTAG00000030650.
GeneID280946.
783512.
KEGGbta:280946.
bta:783512.

Organism-specific databases

CTD7263.

Phylogenomic databases

eggNOGCOG2897.
GeneTreeENSGT00510000046773.
HOGENOMHOG000157237.
HOVERGENHBG002345.
InParanoidP00586.
KOK01011.
OMADGFEKSP.
OrthoDBEOG72ZCGB.
TreeFamTF315133.

Family and domain databases

Gene3D3.40.250.10. 2 hits.
InterProIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTSM00450. RHOD. 2 hits.
[Graphical view]
SUPFAMSSF52821. SSF52821. 2 hits.
PROSITEPS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00586.
NextBio20805059.
PMAP-CutDBP00586.

Entry information

Entry nameTHTR_BOVIN
AccessionPrimary (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: April 16, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references