ECMDB

Identification

Name:

3-mercaptopyruvate sulfurtransferase

Synonyms:

MST
Rhodanese-like protein

Gene Name:

sseA

Enzyme Class:

Biological Properties

General Function:

Involved in thiosulfate sulfurtransferase activity

Specific 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

Cellular Location:

Cytoplasm (Probable)

SMPDB Pathways:

Hydrogen Sulfide Biosynthesis I PW002066
Sulfur metabolism PW000922
Thiosulfate Disproportionation III PW002060
sulfur metabolism (butanesulfonate) PW000923
sulfur metabolism (ethanesulfonate) PW000925
sulfur metabolism (isethionate) PW000926
sulfur metabolism (methanesulfonate) PW000927
sulfur metabolism (propanesulfonate) PW000924

KEGG Pathways:

Cysteine and methionine metabolism ec00270
Metabolic pathways eco01100
Sulfur metabolism ec00920

KEGG Reactions:

1.0

↔

1.0

1.0Hydrogen cyanide + 1.03-Mercaptopyruvic acid + 1.0Cyanide ↔ 1.0Hydrogen ion + 1.0Pyruvic acid + 1.0Thiocyanate
ReactionCard

1.0

↔

1.0

1.0Thiosulfate + 1.0Cyanide ↔ 1.0Sulfite + 1.0Thiocyanate
ReactionCard

1.0

↔

1.0

1.03-Mercaptopyruvic acid + 1.0Sulfite ↔ 1.0Thiosulfate + 1.0Pyruvic acid
ReactionCard

1.0

↔

1.0

1.0Hydrogen cyanide + 1.03-Mercaptopyruvic acid ↔ 1.0Thiocyanate + 1.0Pyruvic acid
ReactionCard

SMPDB Reactions:

1.0Cyanide

1.0Thiosulfate

1.0

→

1.0Thiocyanate

1.0Sulfite

1.0

1.0Cyanide + 1.0Thiosulfate + 1.0Cyanide + 1.0Thiosulfate → 1.0Thiocyanate + 1.0Sulfite + 1.0Hydrogen ion + 1.0Thiocyanate + 1.0Sulfite
ReactionCard

1.0

→

1.0

2.0

1.0Hydrogen cyanide + 1.0Thiosulfate → 1.0Thiocyanate + 1.0Sulfite + 2.0Hydrogen ion
ReactionCard

1.0

→

1.0

1.03-Mercaptopyruvic acid → 1.0Pyruvic acid + 1.0Hydrogen sulfide
ReactionCard

EcoCyc Reactions:

1.0

↔

1.0

1.0Hydrogen cyanide + 1.03-Mercaptopyruvic acid + 1.0Cyanide ↔ 1.0Hydrogen ion + 1.0Pyruvic acid + 1.0Thiocyanate
ReactionCard

1.0

↔

1.0

1.0Hydrogen cyanide + 1.03-Mercaptopyruvic acid ↔ 1.0Thiocyanate + 1.0Pyruvic acid
ReactionCard

1.0

→

1.0

1.0Hydrogen ion + 1.03-Mercaptopyruvic acid → 1.0Pyruvic acid + 1.0Hydrogen sulfide
ReactionCard

1.0

1.0Hydrogen cyanide + 1.03-Mercaptopyruvic acid ? 1.0Hydrogen ion + 1.0Pyruvic acid + 1.0Thiocyanate
ReactionCard

Complex Reactions:

1.0

→

1.0

1.03-Mercaptopyruvic acid + 1.0Hydrogen cyanide → 1.0Pyruvic acid + 1.0Thiocyanate
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB01368	3-Mercaptopyruvic acid	MetaboCard
ECMDB02084	Cyanide	MetaboCard
ECMDB21231	Hydrogen cyanide	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB03276	Hydrogen sulfide	MetaboCard
ECMDB00243	Pyruvic acid	MetaboCard
ECMDB00240	Sulfite	MetaboCard
ECMDB21289	Thiocyanate	MetaboCard
ECMDB00257	Thiosulfate	MetaboCard

GO Classification:

Function
catalytic activity
sulfurtransferase activity
thiosulfate sulfurtransferase activity
transferase activity
transferase activity, transferring sulfur-containing groups
Process
anion transport
establishment of localization
inorganic anion transport
ion transport
sulfate transport
transport

Gene Properties

Blattner:

b2521

Gene Orientation

Clockwise

Centisome Percentage:

57.13

Left Sequence End

2650516

Right Sequence End

2651361

Gene Sequence:

>846 bp
ATGAATAATTTACCGGTAGTTCGTTCGCCCTGGCGGATTGTGATTTTGCTGCTGGGCTTT
ACCTTTCTCTACGCGCCAATGCTGATGCTGGTTATCTATTCGTTTAACAGCTCGAAGCTG
GTGACGGTGTGGGCCGGCTGGTCAACGCGCTGGTATGGTGAGTTATTGCGCGATGACGCG
ATGATGAGTGCGGTTGGTTTAAGTCTGACAATTGCGGCCTGTGCGGCGACGGCGGCGGCG
ATCCTCGGAACTATTGCGGCGGTGGTGCTGGTGCGCTTTGGCAGGTTTCGCGGATCAAAT
GGCTTTGCCTTTATGATCACCGCGCCGCTGGTAATGCCAGATGTCATCACGGGCTTGTCG
CTGTTGTTATTATTCGTCGCGCTTGCTCATGCCATTGGCTGGCCTGCGGACCGCGGTATG
CTCACCATCTGGCTGGCGCATGTCACTTTTTGTACGGCTTATGTGGCGGTCGTTATTTCT
TCAAGATTGCGGGAACTGGATCGCTCGATAGAAGAAGCAGCGATGGATCTCGGTGCGACG
CCGCTGAAAGTGTTTTTCGTCATTACGCTACCGATGATCATGCCCGCGATCATTTCTGGC
TGGTTACTGGCTTTTACTTTGTCGCTTGATGATCTGGTGATCGCCAGCTTTGTTTCCGGG
CCGGGAGCCACCACGTTACCGATGCTGGTCTTTTCCAGCGTGCGGATGGGGGTGAATCCG
GAAATCAACGCCCTGGCAACATTGATCCTCGGCGCGGTCGGAATTGTCGGATTTATCGCC
TGGTATCTGATGGCTCGCGCAGAAAAACAGCGGATACGCGACATCCAGCGTGCAAGACGT
GGCTGA

Protein Properties

Pfam Domain Function:

Rhodanese (PF00581 )

Protein Residues:

281

Protein Molecular Weight:

30812

Protein Theoretical pI:

PDB File:

1URH

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>3-mercaptopyruvate sulfurtransferase
MSTTWFVGADWLAEHIDDPEIQIIDARMASPGQEDRNVAQEYLNGHIPGAVFFDIEALSD
HTSPLPHMLPRPETFAVAMRELGVNQDKHLIVYDEGNLFSAPRAWWMLRTFGVEKVSILG
GGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVKVTDVLLASHENTAQIIDARPAARF
NAEVDEPRPGLRRGHIPGALNVPWTELVREGELKTTDELDAIFFGRGVSYDKPIIVSCGS
GVTAAVVLLALATLDVPNVKLYDGAWSEWGARADLPVEPVK

References

External Links:

Resource	Link
Uniprot ID:	P31142
Uniprot Name:	THTM_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	1651390
PDB ID:	1URH
Ecogene ID:	EG11600
Ecocyc:	EG11600
ColiBase:	b2521
Kegg Gene:	b2521
EchoBASE ID:	EB1557
CCDB:	THTM_ECOLI
BacMap:	90111451

General Reference:

Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
Colnaghi, R., Cassinelli, G., Drummond, M., Forlani, F., Pagani, S. (2001). "Properties of the Escherichia coli rhodanese-like protein SseA: contribution of the active-site residue Ser240 to sulfur donor recognition." FEBS Lett 500:153-156. Pubmed: 11445076
Hama, H., Kayahara, T., Ogawa, W., Tsuda, M., Tsuchiya, T. (1994). "Enhancement of serine-sensitivity by a gene encoding rhodanese-like protein in Escherichia coli." J Biochem 115:1135-1140. Pubmed: 7982894
Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
Spallarossa, A., Forlani, F., Carpen, A., Armirotti, A., Pagani, S., Bolognesi, M., Bordo, D. (2004). "The "rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: crystal structure of SseA from Escherichia coli." J Mol Biol 335:583-593. Pubmed: 14672665
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., Horiuchi, T., et, a. l. .. (1997). "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." DNA Res 4:91-113. Pubmed: 9205837

3-mercaptopyruvate sulfurtransferase (P31142)