P31142 (THTM_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-mercaptopyruvate sulfurtransferase
Short name=MST
EC=2.8.1.2

Alternative name(s):
Rhodanese-like protein

Gene names

Name:	sseA
Ordered Locus Names:	b2521, JW2505

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	281 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	3-mercaptopyruvate + cyanide = pyruvate + thiocyanate.
Subunit structure	Monomer. Ref.7
Subcellular location	Cytoplasm Probable.
Domain	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.
Sequence similarities	Contains 2 rhodanese domains.
Sequence caution	The sequence BAA01382.1 differs from that shown. Reason: Frameshift at position 59.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Repeat
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	response to antibiotic Inferred from mutant phenotype PubMed 22096201. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3-mercaptopyruvate sulfurtransferase activity Inferred from direct assay Ref.6. Source: EcoCyc thiosulfate sulfurtransferase activity Inferred from direct assay Ref.6Ref.1. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 281

280

3-mercaptopyruvate sulfurtransferase

PRO_0000139409

Regions

Domain

17 – 135

119

Rhodanese 1

Domain

165 – 278

114

Rhodanese 2

Region

238 – 244

7

Substrate specificity Potential

Sites

Active site

238

1

Cysteine persulfide intermediate

Binding site

179

1

Substrate By similarity

Experimental info

Mutagenesis

240

1

S → A: Decrease in 3-mercaptopyruvate cyanide sulfurtransferase activity; abolition of thiosulfate binding. Ref.6

Mutagenesis

240

1

S → K: Decrease in 3-mercaptopyruvate cyanide sulfurtransferase activity; increased affinity for thiosulfate. Ref.6

Secondary structure

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281

Helix Strand Turn

Details...

Helix

9 – 13

5

Turn

14 – 17

4

Beta strand

21 – 25

5

Helix

38 – 44

7

Helix

55 – 58

4

Beta strand

61 – 67

7

Helix

72 – 81

10

Beta strand

88 – 93

6

Beta strand

95 – 97

3

Helix

101 – 110

10

Beta strand

116 – 119

4

Helix

122 – 128

7

Beta strand

134 – 136

3

Helix

151 – 153

3

Helix

157 – 166

10

Beta strand

169 – 173

5

Helix

177 – 180

4

Beta strand

193 – 195

3

Helix

204 – 207

4

Beta strand

208 – 213

6

Helix

216 – 224

9

Turn

225 – 227

3

Beta strand

230 – 232

3

Beta strand

234 – 237

4

Beta strand

240 – 242

3

Helix

244 – 253

10

Beta strand

260 – 262

3

Sequences

	Sequence		Length	Mass (Da)
	P31142 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 6744A92A3AB30016	FASTA	281	30,812
	10 20 30 40 50 60 MSTTWFVGAD WLAEHIDDPE IQIIDARMAS PGQEDRNVAQ EYLNGHIPGA VFFDIEALSD 70 80 90 100 110 120 HTSPLPHMLP RPETFAVAMR ELGVNQDKHL IVYDEGNLFS APRAWWMLRT FGVEKVSILG 130 140 150 160 170 180 GGLAGWQRDD LLLEEGAVEL PEGEFNAAFN PEAVVKVTDV LLASHENTAQ IIDARPAARF 190 200 210 220 230 240 NAEVDEPRPG LRRGHIPGAL NVPWTELVRE GELKTTDELD AIFFGRGVSY DKPIIVSCGS 250 260 270 280 GVTAAVVLLA LATLDVPNVK LYDGAWSEWG ARADLPVEPV K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D10496 Genomic DNA. Translation: BAA01382.1. Frameshift.
U00096 Genomic DNA. Translation: AAC75574.2.
AP009048 Genomic DNA. Translation: BAA16411.2.

PIR

H65028.

RefSeq

NP_417016.4. NC_000913.2.
YP_490749.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1URH	X-ray	2.80	A/B	2-281	[»]

ProteinModelPortal

P31142.

SMR

P31142. Positions 3-268.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10921N.

IntAct

P31142. 1 interaction.

MINT

MINT-1289054.

STRING

511145.b2521.

Proteomic databases

PaxDb

P31142.

PRIDE

P31142.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75574; AAC75574; b2521.
BAA16411; BAA16411; BAA16411.

GeneID

12931598.
946993.

KEGG

ecj:Y75_p2474.
eco:b2521.

PATRIC

32120435. VBIEscCol129921_2620.

Organism-specific databases

EchoBASE

EB1557.

EcoGene

EG11600. sseA.

Phylogenomic databases

eggNOG

COG2897.

HOGENOM

HOG000157237.

KO

K01011.

OMA

HIPGTVN.

ProtClustDB

PRK11493.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11600-MONOMER.
ECOL316407:JW2505-MONOMER.
MetaCyc:EG11600-MONOMER.

Gene expression databases

Genevestigator

P31142.

Family and domain databases

Gene3D

3.40.250.10. 2 hits.

InterPro

IPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]

Pfam

PF00581. Rhodanese. 2 hits.
[Graphical view]

SMART

SM00450. RHOD. 2 hits.
[Graphical view]

SUPFAM

SSF52821. Rhodanese-like. 2 hits.

PROSITE

PS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P31142.

Entry information

Entry name

THTM_ECOLI

Accession

Primary (citable) accession number: P31142
Secondary accession number(s): P78096

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 124 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program