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UniProtKB/Swiss-Prot entry P00586


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name THTR_BOVIN
Primary accession number P00586
Secondary accession numbers Q2KIM8 Q5E9C5
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 83)
Name and origin of the protein
Protein name Thiosulfate sulfurtransferase
Synonyms EC 2.8.1.1
Rhodanese
Gene name
Name: TST
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2002017 [NCBI, ExPASy, EBI, Israel, Japan]
Miller D.M., Delgado R., Chirgwin J.M., Hardies S.C., Horowitz P.M.;
"Expression of cloned bovine adrenal rhodanese.";
J. Biol. Chem. 266:4686-4691(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford;
TISSUE=Testis;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 2-295.
TISSUE=Liver;
PubMed=711737 [NCBI, ExPASy, EBI, Israel, Japan]
Russell J., Weng L., Keim P.S., Heinrikson R.L.;
"The covalent structure of bovine liver rhodanese. Isolation and partial structural analysis of cyanogen bromide fragements and the complete sequence of the enzyme.";
J. Biol. Chem. 253:8102-8108(1978).
[5]
ACTIVE SITE.
PubMed=711738 [NCBI, ExPASy, EBI, Israel, Japan]
Weng L., Heinrikson R.L., Westley J.;
"Active site cysteinyl and arginyl residues of rhodanese. A novel formation of disulfide bonds in the active site promoted by phenylglyoxal.";
J. Biol. Chem. 253:8109-8119(1978).
[6]
MUTAGENESIS OF ARG-187 AND LYS-250.
PubMed=8132546 [NCBI, ExPASy, EBI, Israel, Japan]
Luo G.-X., Horowitz P.M.;
"The sulfurtransferase activity and structure of rhodanese are affected by site-directed replacement of Arg-186 or Lys-249.";
J. Biol. Chem. 269:8220-8225(1994).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1016/0022-2836(78)90207-3; PubMed=691057 [NCBI, ExPASy, EBI, Israel, Japan]
Ploegman J.H., Drent G., Kalk K.H., Hol W.G.J.;
"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.";
J. Mol. Biol. 123:557-594(1978).
[8]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1021/bi00281a026; PubMed=6575830 [NCBI, ExPASy, EBI, Israel, Japan]
Lijk L.J., Kalk K.H., Brandenburg N.P., Hol W.G.J.;
"Binding of metal cyanide complexes to bovine liver rhodanese in the crystalline state.";
Biochemistry 22:2952-2957(1983).
[9]
X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS).
DOI=10.1074/jbc.271.35.21054; PubMed=8702871 [NCBI, ExPASy, EBI, Israel, Japan]
Gliubich F., Gazerro M., Zanotti G., Delbono S., Bombieri G., Berni R.;
"Active site structural features for chemically modified forms of rhodanese.";
J. Biol. Chem. 271:21054-21061(1996).
[10]
X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS).
DOI=10.1107/S090744499701216X; PubMed=9761843 [NCBI, ExPASy, EBI, Israel, Japan]
Gliubich F., Berni R., Colapietro M., Barba L., Zanotti G.;
"Structure of sulfur-substituted rhodanese at 1.36-A resolution.";
Acta Crystallogr. D 54:481-486(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M58561; AAA30753.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT020995; AAX09012.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC112580; AAI12581.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A23704; ROBO.
RefSeq NP_803455.1; -.
XP_001249946.1; -.
UniGene Bt.51597
3D structure databases
PDB
1BOH; X-ray; 2.30 A; A=1-297.[ExPASy / RCSB / EBI]
1BOI; X-ray; 2.20 A; A=1-297.[ExPASy / RCSB / EBI]
1DP2; X-ray; 2.01 A; A=1-294.[ExPASy / RCSB / EBI]
1ORB; X-ray; 2.00 A; A=1-297.[ExPASy / RCSB / EBI]
1RHD; X-ray; 2.50 A; A=1-294.[ExPASy / RCSB / EBI]
1RHS; X-ray; 1.36 A; A=1-297.[ExPASy / RCSB / EBI]
2ORA; X-ray; 1.99 A; A=1-297.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BOH; -.
1BOI; -.
1DP2; -.
1ORB; -.
1RHD; -.
1RHS; -.
2ORA; -.
ModBase P00586.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR001763; Rhodanese-like.
IPR001307; Thiosulphate_sulphurtransf_CS.
Graphical view of domain structure.
Gene3D G3DSA:3.40.250.10; Rhodanese-like; 2.
Pfam PF00581; Rhodanese; 2.
Pfam graphical view of domain structure.
SMART SM00450; RHOD; 2.
SMART graphical view of domain structure.
PROSITE PS00380; RHODANESE_1; 1.
PS00683; RHODANESE_2; 1.
PS50206; RHODANESE_3; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00586.
ProtoNet P00586.
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; -.
Other
LinkHub P00586; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Direct protein sequencing; Mitochondrion; Phosphoprotein; Repeat; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   297  296     Thiosulfate sulfurtransferase. PRO_0000139392
DOMAIN   25   143  119     Rhodanese 1. 
DOMAIN   173   288  116     Rhodanese 2. 
REGION   144   159  16     Hinge. 
ACT_SITE   248   248        Cysteine persulfide intermediate. 
BINDING   187   187        Substrate. 
BINDING   250   250        Substrate. 
MOD_RES   136   136        N6-acetyllysine (By similarity). 
MOD_RES   164   164        Phosphothreonine (By similarity). 
MOD_RES   165   165        Phosphotyrosine (By similarity). 
VARIANT   2     3  2     Missing (in some preparations, has no effect on enzyme activity). 
MUTAGEN   187   187        R->L: Reduced rhodanese activity. 
MUTAGEN   250   250        K->A: No rhodanese activity. 
CONFLICT   100   100        D -> N (in Ref. 4; AA sequence). 
CONFLICT   215   215        N -> D (in Ref. 4; AA sequence). 
CONFLICT   220   220        D -> N (in Ref. 4; AA sequence). 
STRAND   9    11  3      
HELIX   13    21  9      
STRAND   29    33  5      
HELIX   44    50  7      
TURN   61    63  3      
STRAND   69    73  5      
HELIX   78    87  10      
STRAND   95    99  5      
STRAND   103   105  3      
HELIX   109   118  10      
STRAND   124   127  4      
HELIX   130   136  7      
HELIX   159   161  3      
HELIX   165   174  10      
STRAND   177   181  5      
HELIX   185   189  5      
STRAND   195   199  5      
HELIX   213   216  4      
HELIX   226   235  10      
STRAND   244   247  4      
STRAND   249   252  4      
HELIX   254   263  10      
STRAND   270   274  5      
HELIX   275   282  8      
HELIX   285   287  3      
STRAND   288   290  3      
Sequence information
Length: 297 AA [This is the length of the unprocessed precursor] Molecular weight: 33296 Da [This is the MW of the unprocessed precursor] CRC64: F2F4AA7294F84B1A [This is a checksum on the sequence]
        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 

P00586 in FASTA format

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