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Protein

3-mercaptopyruvate sulfurtransferase

Gene

sseA

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

Functioni

Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity.

Catalytic activityi

3-mercaptopyruvate + cyanide = pyruvate + thiocyanate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei179SubstrateBy similarity1
Active sitei238Cysteine persulfide intermediate1

GO - Molecular functioni

  • 3-mercaptopyruvate sulfurtransferase activity Source: EcoCyc
  • thiosulfate sulfurtransferase activity Source: EcoCyc

GO - Biological processi

  • response to antibiotic Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciEcoCyc:EG11600-MONOMER.
ECOL316407:JW2505-MONOMER.
MetaCyc:EG11600-MONOMER.
BRENDAi2.8.1.2. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
3-mercaptopyruvate sulfurtransferase (EC:2.8.1.2)
Short name:
MST
Alternative name(s):
Rhodanese-like protein
Gene namesi
Name:sseA
Ordered Locus Names:b2521, JW2505
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11600. sseA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi240S → A: Decrease in 3-mercaptopyruvate cyanide sulfurtransferase activity; abolition of thiosulfate binding. 1 Publication1
Mutagenesisi240S → K: Decrease in 3-mercaptopyruvate cyanide sulfurtransferase activity; increased affinity for thiosulfate. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001394092 – 2813-mercaptopyruvate sulfurtransferaseAdd BLAST280

Proteomic databases

EPDiP31142.
PaxDbiP31142.
PRIDEiP31142.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4260592. 12 interactors.
DIPiDIP-10921N.
IntActiP31142. 1 interactor.
MINTiMINT-1289054.
STRINGi511145.b2521.

Structurei

Secondary structure

1281
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 13Combined sources5
Turni14 – 17Combined sources4
Beta strandi21 – 25Combined sources5
Helixi38 – 44Combined sources7
Helixi55 – 58Combined sources4
Beta strandi61 – 67Combined sources7
Helixi72 – 81Combined sources10
Beta strandi88 – 93Combined sources6
Beta strandi95 – 97Combined sources3
Helixi101 – 110Combined sources10
Beta strandi116 – 119Combined sources4
Helixi122 – 128Combined sources7
Beta strandi134 – 136Combined sources3
Helixi151 – 153Combined sources3
Helixi157 – 166Combined sources10
Beta strandi169 – 173Combined sources5
Helixi177 – 180Combined sources4
Beta strandi193 – 195Combined sources3
Helixi204 – 207Combined sources4
Beta strandi208 – 213Combined sources6
Helixi216 – 224Combined sources9
Turni225 – 227Combined sources3
Beta strandi230 – 232Combined sources3
Beta strandi234 – 237Combined sources4
Beta strandi240 – 242Combined sources3
Helixi244 – 253Combined sources10
Beta strandi260 – 262Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1URHX-ray2.80A/B2-281[»]
ProteinModelPortaliP31142.
SMRiP31142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31142.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 135Rhodanese 1PROSITE-ProRule annotationAdd BLAST119
Domaini165 – 278Rhodanese 2PROSITE-ProRule annotationAdd BLAST114

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni238 – 244Substrate specificitySequence analysis7

Domaini

The N-terminal region is the non-catalytic domain; the C-terminus contains the active-site cysteine residue and the CGSGVTA motif probably responsible for substrate specificity.
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 (By similarity).By similarity

Sequence similaritiesi

Contains 2 rhodanese domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105KHC. Bacteria.
COG2897. LUCA.
HOGENOMiHOG000157237.
InParanoidiP31142.
KOiK01011.
OMAiSWGEWGS.
PhylomeDBiP31142.

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.

P31142-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTTWFVGAD WLAEHIDDPE IQIIDARMAS PGQEDRNVAQ EYLNGHIPGA
60 70 80 90 100
VFFDIEALSD HTSPLPHMLP RPETFAVAMR ELGVNQDKHL IVYDEGNLFS
110 120 130 140 150
APRAWWMLRT FGVEKVSILG GGLAGWQRDD LLLEEGAVEL PEGEFNAAFN
160 170 180 190 200
PEAVVKVTDV LLASHENTAQ IIDARPAARF NAEVDEPRPG LRRGHIPGAL
210 220 230 240 250
NVPWTELVRE GELKTTDELD AIFFGRGVSY DKPIIVSCGS GVTAAVVLLA
260 270 280
LATLDVPNVK LYDGAWSEWG ARADLPVEPV K
Length:281
Mass (Da):30,812
Last modified:January 23, 2007 - v3
Checksum:i6744A92A3AB30016
GO

Sequence cautioni

The sequence BAA01382 differs from that shown. Reason: Frameshift at position 59.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10496 Genomic DNA. Translation: BAA01382.1. Frameshift.
U00096 Genomic DNA. Translation: AAC75574.2.
AP009048 Genomic DNA. Translation: BAA16411.2.
PIRiH65028.
RefSeqiNP_417016.4. NC_000913.3.
WP_000108626.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75574; AAC75574; b2521.
BAA16411; BAA16411; BAA16411.
GeneIDi946993.
KEGGiecj:JW2505.
eco:b2521.
PATRICi32120435. VBIEscCol129921_2620.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10496 Genomic DNA. Translation: BAA01382.1. Frameshift.
U00096 Genomic DNA. Translation: AAC75574.2.
AP009048 Genomic DNA. Translation: BAA16411.2.
PIRiH65028.
RefSeqiNP_417016.4. NC_000913.3.
WP_000108626.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1URHX-ray2.80A/B2-281[»]
ProteinModelPortaliP31142.
SMRiP31142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260592. 12 interactors.
DIPiDIP-10921N.
IntActiP31142. 1 interactor.
MINTiMINT-1289054.
STRINGi511145.b2521.

Proteomic databases

EPDiP31142.
PaxDbiP31142.
PRIDEiP31142.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75574; AAC75574; b2521.
BAA16411; BAA16411; BAA16411.
GeneIDi946993.
KEGGiecj:JW2505.
eco:b2521.
PATRICi32120435. VBIEscCol129921_2620.

Organism-specific databases

EchoBASEiEB1557.
EcoGeneiEG11600. sseA.

Phylogenomic databases

eggNOGiENOG4105KHC. Bacteria.
COG2897. LUCA.
HOGENOMiHOG000157237.
InParanoidiP31142.
KOiK01011.
OMAiSWGEWGS.
PhylomeDBiP31142.

Enzyme and pathway databases

BioCyciEcoCyc:EG11600-MONOMER.
ECOL316407:JW2505-MONOMER.
MetaCyc:EG11600-MONOMER.
BRENDAi2.8.1.2. 2026.

Miscellaneous databases

EvolutionaryTraceiP31142.
PROiP31142.

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 nameiTHTM_ECOLI
AccessioniPrimary (citable) accession number: P31142
Secondary accession number(s): P78096
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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