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P00586

- THTR_BOVIN

UniProt

P00586 - THTR_BOVIN

Protein

Thiosulfate sulfurtransferase

Gene

TST

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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.By similarity

    Catalytic activityi

    Thiosulfate + cyanide = sulfite + thiocyanate.

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. rRNA import into mitochondrion Source: UniProtKB
    2. rRNA transport Source: UniProtKB

    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

    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 sulfurtransferasePRO_0000139392Add
    BLAST

    Amino acid modifications

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

    1
    297
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00586.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 143119Rhodanese 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini173 – 288116Rhodanese 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni144 – 15916HingeAdd
    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).1 Publication

    Sequence similaritiesi

    Contains 2 rhodanese domains.PROSITE-ProRule annotation

    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

    « Hide

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001D → N AA sequence (PubMed:711737)Curated
    Sequence conflicti215 – 2151N → D AA sequence (PubMed:711737)Curated
    Sequence conflicti220 – 2201D → N AA sequence (PubMed:711737)Curated

    Natural variant

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

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 133 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