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P00586

- THTR_BOVIN

UniProt

P00586 - THTR_BOVIN

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Protein
Thiosulfate sulfurtransferase
Gene
TST
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

Thiosulfate + cyanide = sulfite + thiocyanate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei187 – 1871Substrate
Active sitei248 – 2481Cysteine persulfide intermediate1 Publication
Binding sitei250 – 2501Substrate

GO - Molecular functioni

  1. 5S rRNA binding Source: UniProtKB
  2. protein binding Source: IntAct
  3. thiosulfate sulfurtransferase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. rRNA import into mitochondrion Source: UniProtKB
  2. rRNA transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_213617. Sulfide oxidation to sulfate.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiosulfate sulfurtransferase (EC:2.8.1.1)
Alternative name(s):
Rhodanese
Gene namesi
Name:TST
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 5

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Ensembl
  2. mitochondrial matrix Source: UniProtKB-SubCell
  3. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi187 – 1871R → L: Reduced rhodanese activity. 1 Publication
Mutagenesisi250 – 2501K → A: No rhodanese activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 297296Thiosulfate sulfurtransferase
PRO_0000139392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141N6-acetyllysine; alternate By similarity
Modified residuei14 – 141N6-succinyllysine; alternate1 Publication
Glycosylationi35 – 351O-linked (GlcNAc) By similarity
Modified residuei136 – 1361N6-acetyllysine; alternate By similarity
Modified residuei136 – 1361N6-succinyllysine; alternate By similarity
Modified residuei163 – 1631N6-acetyllysine By similarity
Modified residuei175 – 1751N6-acetyllysine; alternate By similarity
Modified residuei175 – 1751N6-succinyllysine; alternate By similarity
Modified residuei224 – 2241N6-acetyllysine; alternate By similarity
Modified residuei224 – 2241N6-succinyllysine; alternate By similarity
Modified residuei236 – 2361N6-acetyllysine By similarity
Modified residuei237 – 2371N6-acetyllysine; alternate By similarity
Modified residuei237 – 2371N6-succinyllysine; alternate By similarity

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

PaxDbiP00586.
PRIDEiP00586.

Miscellaneous databases

PMAP-CutDBP00586.

Expressioni

Tissue specificityi

Expressed in numerous tissues.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
groLP0A6F52EBI-7900146,EBI-543750From a different organism.

Protein-protein interaction databases

IntActiP00586. 2 interactions.
STRINGi9913.ENSBTAP00000040894.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 64
Beta strandi9 – 113
Helixi13 – 219
Turni26 – 283
Beta strandi29 – 335
Turni39 – 413
Helixi44 – 507
Beta strandi56 – 583
Turni61 – 633
Beta strandi69 – 735
Helixi78 – 8710
Beta strandi95 – 995
Beta strandi103 – 1053
Helixi109 – 11810
Beta strandi124 – 1274
Helixi130 – 1367
Helixi159 – 1613
Helixi165 – 17410
Beta strandi177 – 1815
Helixi185 – 1895
Beta strandi190 – 1923
Beta strandi195 – 1995
Beta strandi208 – 2103
Helixi213 – 2164
Helixi226 – 23510
Beta strandi244 – 2474
Beta strandi249 – 2524
Helixi254 – 26310
Beta strandi270 – 2745
Helixi275 – 2828
Helixi285 – 2873
Beta strandi288 – 2903

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOHX-ray2.30A2-297[»]
1BOIX-ray2.20A2-297[»]
1DP2X-ray2.01A2-294[»]
1ORBX-ray2.00A2-297[»]
1RHDX-ray2.50A2-294[»]
1RHSX-ray1.36A2-297[»]
2ORAX-ray1.99A2-297[»]
ProteinModelPortaliP00586.
SMRiP00586. Positions 2-294.

Miscellaneous databases

EvolutionaryTraceiP00586.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 143119Rhodanese 1
Add
BLAST
Domaini173 – 288116Rhodanese 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 15916Hinge
Add
BLAST

Domaini

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 (PubMed:691057).

Sequence similaritiesi

Contains 2 rhodanese domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2897.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiP00586.
KOiK01011.
OMAiAPPEYPN.
OrthoDBiEOG72ZCGB.
TreeFamiTF315133.

Family and domain databases

Gene3Di3.40.250.10. 2 hits.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTiSM00450. RHOD. 2 hits.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 2 hits.
PROSITEiPS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00586-1 [UniParc]FASTAAdd to Basket

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MVHQVLYRAL VSTKWLAESV RAGKVGPGLR VLDASWYSPG TREARKEYLE    50
RHVPGASFFD IEECRDKASP YEVMLPSEAG FADYVGSLGI SNDTHVVVYD 100
GDDLGSFYAP RVWWMFRVFG HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP 150
AIFKATLNRS LLKTYEQVLE NLESKRFQLV DSRAQGRYLG TQPEPDAVGL 200
DSGHIRGSVN MPFMNFLTED GFEKSPEELR AMFEAKKVDL TKPLIATCRK 250
GVTACHIALA AYLCGKPDVA IYDGSWFEWF HRAPPETWVS QGKGGKA 297
Length:297
Mass (Da):33,296
Last modified:January 23, 2007 - v3
Checksum:iF2F4AA7294F84B1A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 32Missing in some preparations, has no effect on enzyme activity.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001D → N AA sequence 1 Publication
Sequence conflicti215 – 2151N → D AA sequence 1 Publication
Sequence conflicti220 – 2201D → N AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M58561 mRNA. Translation: AAA30753.1.
BT020995 mRNA. Translation: AAX09012.1.
BC112580 mRNA. Translation: AAI12581.1.
PIRiA23704. ROBO.
RefSeqiNP_803455.1. NM_177489.3.
XP_001249946.1. XM_001249945.5.
UniGeneiBt.51597.

Genome annotation databases

EnsembliENSBTAT00000043317; ENSBTAP00000040894; ENSBTAG00000030650.
GeneIDi280946.
783512.
KEGGibta:280946.
bta:783512.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M58561 mRNA. Translation: AAA30753.1 .
BT020995 mRNA. Translation: AAX09012.1 .
BC112580 mRNA. Translation: AAI12581.1 .
PIRi A23704. ROBO.
RefSeqi NP_803455.1. NM_177489.3.
XP_001249946.1. XM_001249945.5.
UniGenei Bt.51597.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BOH X-ray 2.30 A 2-297 [» ]
1BOI X-ray 2.20 A 2-297 [» ]
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 [» ]
ProteinModelPortali P00586.
SMRi P00586. Positions 2-294.
ModBasei Search...

Protein-protein interaction databases

IntActi P00586. 2 interactions.
STRINGi 9913.ENSBTAP00000040894.

Proteomic databases

PaxDbi P00586.
PRIDEi P00586.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000043317 ; ENSBTAP00000040894 ; ENSBTAG00000030650 .
GeneIDi 280946.
783512.
KEGGi bta:280946.
bta:783512.

Organism-specific databases

CTDi 7263.

Phylogenomic databases

eggNOGi COG2897.
GeneTreei ENSGT00510000046773.
HOGENOMi HOG000157237.
HOVERGENi HBG002345.
InParanoidi P00586.
KOi K01011.
OMAi APPEYPN.
OrthoDBi EOG72ZCGB.
TreeFami TF315133.

Enzyme and pathway databases

Reactomei REACT_213617. Sulfide oxidation to sulfate.

Miscellaneous databases

EvolutionaryTracei P00586.
NextBioi 20805059.
PMAP-CutDB P00586.

Family and domain databases

Gene3Di 3.40.250.10. 2 hits.
InterProi IPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view ]
Pfami PF00581. Rhodanese. 2 hits.
[Graphical view ]
SMARTi SM00450. RHOD. 2 hits.
[Graphical view ]
SUPFAMi SSF52821. SSF52821. 2 hits.
PROSITEi PS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiTHTR_BOVIN
AccessioniPrimary (citable) accession number: P00586
Secondary accession number(s): Q2KIM8, Q5E9C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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