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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei179 – 1791SubstrateBy similarity
Active sitei238 – 2381Cysteine persulfide intermediate

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.
RETL1328306-WGS:GSTH-1817-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi240 – 2401S → A: Decrease in 3-mercaptopyruvate cyanide sulfurtransferase activity; abolition of thiosulfate binding. 1 Publication
Mutagenesisi240 – 2401S → K: Decrease in 3-mercaptopyruvate cyanide sulfurtransferase activity; increased affinity for thiosulfate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 2812803-mercaptopyruvate sulfurtransferasePRO_0000139409Add
BLAST

Proteomic databases

EPDiP31142.
PaxDbiP31142.
PRIDEiP31142.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4260592. 12 interactions.
DIPiDIP-10921N.
IntActiP31142. 1 interaction.
MINTiMINT-1289054.
STRINGi511145.b2521.

Structurei

Secondary structure

1
281
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 135Combined sources
Turni14 – 174Combined sources
Beta strandi21 – 255Combined sources
Helixi38 – 447Combined sources
Helixi55 – 584Combined sources
Beta strandi61 – 677Combined sources
Helixi72 – 8110Combined sources
Beta strandi88 – 936Combined sources
Beta strandi95 – 973Combined sources
Helixi101 – 11010Combined sources
Beta strandi116 – 1194Combined sources
Helixi122 – 1287Combined sources
Beta strandi134 – 1363Combined sources
Helixi151 – 1533Combined sources
Helixi157 – 16610Combined sources
Beta strandi169 – 1735Combined sources
Helixi177 – 1804Combined sources
Beta strandi193 – 1953Combined sources
Helixi204 – 2074Combined sources
Beta strandi208 – 2136Combined sources
Helixi216 – 2249Combined sources
Turni225 – 2273Combined sources
Beta strandi230 – 2323Combined sources
Beta strandi234 – 2374Combined sources
Beta strandi240 – 2423Combined sources
Helixi244 – 25310Combined sources
Beta strandi260 – 2623Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1URHX-ray2.80A/B2-281[»]
ProteinModelPortaliP31142.
SMRiP31142. Positions 3-268.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31142.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 135119Rhodanese 1PROSITE-ProRule annotationAdd
BLAST
Domaini165 – 278114Rhodanese 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni238 – 2447Substrate specificitySequence analysis

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.
OrthoDBiEOG651SS8.
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 BAA01382.1 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
EntryMethodResolution (Å)ChainPositionsPDBsum
1URHX-ray2.80A/B2-281[»]
ProteinModelPortaliP31142.
SMRiP31142. Positions 3-268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260592. 12 interactions.
DIPiDIP-10921N.
IntActiP31142. 1 interaction.
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.
OrthoDBiEOG651SS8.
PhylomeDBiP31142.

Enzyme and pathway databases

BioCyciEcoCyc:EG11600-MONOMER.
ECOL316407:JW2505-MONOMER.
MetaCyc:EG11600-MONOMER.
RETL1328306-WGS:GSTH-1817-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...

Publicationsi

« Hide 'large scale' publications
  1. "Enhancement of serine-sensitivity by a gene encoding rhodanese-like protein in Escherichia coli."
    Hama H., Kayahara T., Ogawa W., Tsuda M., Tsuchiya T.
    J. Biochem. 115:1135-1140(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3133-2.
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  6. "Properties of the Escherichia coli rhodanese-like protein SseA: contribution of the active-site residue Ser240 to sulfur donor recognition."
    Colnaghi R., Cassinelli G., Drummond M., Forlani F., Pagani S.
    FEBS Lett. 500:153-156(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF SER-240.
  7. "The 'rhodanese' fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: crystal structure of SseA from Escherichia coli."
    Spallarossa A., Forlani F., Carpen A., Armirotti A., Pagani S., Bolognesi M., Bordo D.
    J. Mol. Biol. 335:583-593(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT.

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: March 16, 2016
This is version 145 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.