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Protein

Thiosulfate sulfurtransferase YnjE

Gene

ynjE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Thiosulfate + cyanide = sulfite + thiocyanate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei385 – 3851Cysteine persulfide intermediatePROSITE-ProRule annotation1 Publication
Binding sitei390 – 3901SubstrateBy similarity

GO - Molecular functioni

  • sulfurtransferase activity Source: EcoCyc
  • thiosulfate sulfurtransferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciEcoCyc:G6952-MONOMER.
ECOL316407:JW5287-MONOMER.
MetaCyc:G6952-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiosulfate sulfurtransferase YnjE (EC:2.8.1.1)
Gene namesi
Name:ynjE
Ordered Locus Names:b1757, JW5287
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14007. ynjE.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi385 – 3851C → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323PROSITE-ProRule annotationAdd
BLAST
Chaini24 – 435412Thiosulfate sulfurtransferase YnjEPRO_0000030429Add
BLAST

Proteomic databases

PaxDbiP78067.
PRIDEiP78067.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4262126. 192 interactions.
DIPiDIP-12782N.
STRINGi511145.b1757.

Structurei

Secondary structure

1
435
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 376Combined sources
Beta strandi41 – 444Combined sources
Helixi48 – 525Combined sources
Beta strandi63 – 653Combined sources
Helixi73 – 786Combined sources
Helixi81 – 9010Combined sources
Beta strandi99 – 1035Combined sources
Helixi105 – 11713Combined sources
Beta strandi123 – 1264Combined sources
Turni127 – 1304Combined sources
Helixi133 – 1353Combined sources
Helixi142 – 1443Combined sources
Helixi148 – 1558Combined sources
Beta strandi168 – 17710Combined sources
Helixi180 – 1834Combined sources
Beta strandi190 – 1934Combined sources
Helixi194 – 1963Combined sources
Turni200 – 2034Combined sources
Helixi208 – 21710Combined sources
Beta strandi224 – 2296Combined sources
Helixi233 – 24614Combined sources
Beta strandi251 – 2544Combined sources
Turni255 – 2573Combined sources
Helixi258 – 2636Combined sources
Helixi290 – 2923Combined sources
Helixi296 – 3005Combined sources
Turni301 – 3044Combined sources
Beta strandi306 – 3127Combined sources
Helixi316 – 3194Combined sources
Beta strandi333 – 3353Combined sources
Helixi351 – 3533Combined sources
Beta strandi358 – 3603Combined sources
Helixi363 – 3719Combined sources
Turni372 – 3743Combined sources
Beta strandi379 – 3846Combined sources
Beta strandi386 – 3883Combined sources
Helixi389 – 40012Combined sources
Beta strandi404 – 4118Combined sources
Helixi412 – 4165Combined sources
Helixi431 – 4344Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WLRX-ray1.45A24-435[»]
2WLXX-ray1.90A24-435[»]
3IPOX-ray2.40A/B20-435[»]
3IPPX-ray2.40A/B20-435[»]
ProteinModelPortaliP78067.
SMRiP78067. Positions 20-435.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78067.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 138103Rhodanese 1PROSITE-ProRule annotationAdd
BLAST
Domaini164 – 270107Rhodanese 2PROSITE-ProRule annotationAdd
BLAST
Domaini304 – 425122Rhodanese 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 rhodanese domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4107RM6. Bacteria.
COG2897. LUCA.
HOGENOMiHOG000282520.
InParanoidiP78067.
KOiK01011.
OMAiYMGVKDV.
PhylomeDBiP78067.

Family and domain databases

Gene3Di3.40.250.10. 3 hits.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTiSM00450. RHOD. 3 hits.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 3 hits.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P78067-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRVSQMTAL AMALGLACAS SWAAELAKPL TLDQLQQQNG KAIDTRPSAF
60 70 80 90 100
YNGWPQTLNG PSGHELAALN LSASWLDKMS TEQLNAWIKQ HNLKTDAPVA
110 120 130 140 150
LYGNDKDVDA VKTRLQKAGL THISILSDAL SEPSRLQKLP HFEQLVYPQW
160 170 180 190 200
LHDLQQGKEV TAKPAGDWKV IEAAWGAPKL YLISHIPGAD YIDTNEVESE
210 220 230 240 250
PLWNKVSDEQ LKAMLAKHGI RHDTTVILYG RDVYAAARVA QIMLYAGVKD
260 270 280 290 300
VRLLDGGWQT WSDAGLPVER GTPPKVKAEP DFGVKIPAQP QLMLDMEQAR
310 320 330 340 350
GLLHRQDASL VSIRSWPEFI GTTSGYSYIK PKGEIAGARW GHAGSDSTHM
360 370 380 390 400
EDFHNPDGTM RSADDITAMW KAWNIKPEQQ VSFYCGTGWR ASETFMYARA
410 420 430
MGWKNVSVYD GGWYEWSSDP KNPVATGERG PDSSK
Length:435
Mass (Da):48,229
Last modified:December 15, 1998 - v2
Checksum:iC66CCFB50EC464BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74827.2.
AP009048 Genomic DNA. Translation: BAA15548.2.
PIRiE64935.
RefSeqiNP_416271.4. NC_000913.3.
WP_001350515.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74827; AAC74827; b1757.
BAA15548; BAA15548; BAA15548.
GeneIDi946505.
KEGGiecj:JW5287.
eco:b1757.
PATRICi32118825. VBIEscCol129921_1830.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74827.2.
AP009048 Genomic DNA. Translation: BAA15548.2.
PIRiE64935.
RefSeqiNP_416271.4. NC_000913.3.
WP_001350515.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WLRX-ray1.45A24-435[»]
2WLXX-ray1.90A24-435[»]
3IPOX-ray2.40A/B20-435[»]
3IPPX-ray2.40A/B20-435[»]
ProteinModelPortaliP78067.
SMRiP78067. Positions 20-435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262126. 192 interactions.
DIPiDIP-12782N.
STRINGi511145.b1757.

Proteomic databases

PaxDbiP78067.
PRIDEiP78067.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74827; AAC74827; b1757.
BAA15548; BAA15548; BAA15548.
GeneIDi946505.
KEGGiecj:JW5287.
eco:b1757.
PATRICi32118825. VBIEscCol129921_1830.

Organism-specific databases

EchoBASEiEB3763.
EcoGeneiEG14007. ynjE.

Phylogenomic databases

eggNOGiENOG4107RM6. Bacteria.
COG2897. LUCA.
HOGENOMiHOG000282520.
InParanoidiP78067.
KOiK01011.
OMAiYMGVKDV.
PhylomeDBiP78067.

Enzyme and pathway databases

BioCyciEcoCyc:G6952-MONOMER.
ECOL316407:JW5287-MONOMER.
MetaCyc:G6952-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP78067.
PROiP78067.

Family and domain databases

Gene3Di3.40.250.10. 3 hits.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTiSM00450. RHOD. 3 hits.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 3 hits.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiYNJE_ECOLI
AccessioniPrimary (citable) accession number: P78067
Secondary accession number(s): P78171
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 15, 1998
Last modified: September 7, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In vitro, YnjE can be efficiently persulfurated by the cysteine desulfurase IscS.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.