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Protein

Thiosulfate sulfurtransferase

Gene

TST

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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.By similarity

Catalytic activityi

Thiosulfate + cyanide = sulfite + thiocyanate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei187Substrate1
Active sitei248Cysteine persulfide intermediatePROSITE-ProRule annotation1 Publication1
Binding sitei250Substrate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BRENDAi2.8.1.1. 908.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiosulfate sulfurtransferase (EC:2.8.1.11 Publication)
Alternative name(s):
Rhodanese
Gene namesi
Name:TST
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi187R → L: Reduced rhodanese activity. 1 Publication1
Mutagenesisi250K → A: No rhodanese activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001393922 – 297Thiosulfate sulfurtransferaseAdd BLAST296

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14N6-acetyllysine; alternateBy similarity1
Modified residuei14N6-succinyllysine; alternate1 Publication1
Glycosylationi35O-linked (GlcNAc)By similarity1
Modified residuei38PhosphoserineBy similarity1
Modified residuei136N6-acetyllysine; alternateBy similarity1
Modified residuei136N6-succinyllysine; alternateBy similarity1
Modified residuei163N6-acetyllysineBy similarity1
Modified residuei175N6-acetyllysine; alternateBy similarity1
Modified residuei175N6-succinyllysine; alternateBy similarity1
Modified residuei224N6-acetyllysine; alternateBy similarity1
Modified residuei224N6-succinyllysine; alternateBy similarity1
Modified residuei236N6-acetyllysineBy similarity1
Modified residuei237N6-acetyllysine; alternateBy similarity1
Modified residuei237N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP00586.
PeptideAtlasiP00586.
PRIDEiP00586.

Miscellaneous databases

PMAP-CutDBP00586.

Expressioni

Tissue specificityi

Expressed in numerous tissues.

Gene expression databases

BgeeiENSBTAG00000030650.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

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

Protein-protein interaction databases

IntActiP00586. 2 interactors.
STRINGi9913.ENSBTAP00000040894.

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 6Combined sources4
Beta strandi9 – 11Combined sources3
Helixi13 – 21Combined sources9
Turni26 – 28Combined sources3
Beta strandi29 – 33Combined sources5
Turni39 – 41Combined sources3
Helixi44 – 50Combined sources7
Beta strandi56 – 58Combined sources3
Turni61 – 63Combined sources3
Beta strandi69 – 73Combined sources5
Helixi78 – 87Combined sources10
Beta strandi95 – 99Combined sources5
Beta strandi103 – 105Combined sources3
Helixi109 – 118Combined sources10
Beta strandi124 – 127Combined sources4
Helixi130 – 136Combined sources7
Helixi159 – 161Combined sources3
Helixi165 – 174Combined sources10
Beta strandi177 – 181Combined sources5
Helixi185 – 189Combined sources5
Beta strandi190 – 192Combined sources3
Beta strandi195 – 199Combined sources5
Beta strandi208 – 210Combined sources3
Helixi213 – 216Combined sources4
Helixi226 – 235Combined sources10
Beta strandi244 – 247Combined sources4
Beta strandi249 – 252Combined sources4
Helixi254 – 263Combined sources10
Beta strandi270 – 274Combined sources5
Helixi275 – 282Combined sources8
Helixi285 – 287Combined sources3
Beta strandi288 – 290Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00586.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 143Rhodanese 1PROSITE-ProRule annotationAdd BLAST119
Domaini173 – 288Rhodanese 2PROSITE-ProRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 159HingeAdd BLAST16

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

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiP00586.
KOiK01011.
OMAiSRAQGRY.
OrthoDBiEOG091G0X2Q.
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

        10         20         30         40         50
MVHQVLYRAL VSTKWLAESV RAGKVGPGLR VLDASWYSPG TREARKEYLE
60 70 80 90 100
RHVPGASFFD IEECRDKASP YEVMLPSEAG FADYVGSLGI SNDTHVVVYD
110 120 130 140 150
GDDLGSFYAP RVWWMFRVFG HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP
160 170 180 190 200
AIFKATLNRS LLKTYEQVLE NLESKRFQLV DSRAQGRYLG TQPEPDAVGL
210 220 230 240 250
DSGHIRGSVN MPFMNFLTED GFEKSPEELR AMFEAKKVDL TKPLIATCRK
260 270 280 290
GVTACHIALA AYLCGKPDVA IYDGSWFEWF HRAPPETWVS QGKGGKA
Length:297
Mass (Da):33,296
Last modified:January 23, 2007 - v3
Checksum:iF2F4AA7294F84B1A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti100D → N AA sequence (PubMed:711737).Curated1
Sequence conflicti215N → D AA sequence (PubMed:711737).Curated1
Sequence conflicti220D → N AA sequence (PubMed:711737).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti2 – 3Missing in some preparations, has no effect on enzyme activity. 2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
UniGeneiBt.51597.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
UniGeneiBt.51597.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00586. 2 interactors.
STRINGi9913.ENSBTAP00000040894.

Proteomic databases

PaxDbiP00586.
PeptideAtlasiP00586.
PRIDEiP00586.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7263.

Phylogenomic databases

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiP00586.
KOiK01011.
OMAiSRAQGRY.
OrthoDBiEOG091G0X2Q.
TreeFamiTF315133.

Enzyme and pathway databases

BRENDAi2.8.1.1. 908.

Miscellaneous databases

EvolutionaryTraceiP00586.
PMAP-CutDBP00586.

Gene expression databases

BgeeiENSBTAG00000030650.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 149 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.