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Information on EC 2.5.1.47 - cysteine synthase and Organism(s) Bacillus subtilis and UniProt Accession P37887

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EC Tree
IUBMB Comments
A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51 (beta-pyrazolylalanine synthase), EC 2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine synthase).
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This record set is specific for:
Bacillus subtilis
UNIPROT: P37887
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
gyy4137, cysteine synthase, cysteine synthetase, o-acetylserine sulfhydrylase, oastl, oas-tl, o-acetylserine(thiol)lyase, csase, o-acetylserine (thiol) lyase, oass-a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
O-acetylserine sulfhydrylase
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O-acetylserine sulfhydrylase A
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acetylserine sulfhydrylase
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CSase
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cysteine synthetase
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O-acetyl-L-serine acetate-lyase (adding hydrogen sulfide)
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O-acetyl-L-serine sulfhydrylase
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-
-
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O-acetyl-L-serine sulfohydrolase
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-
-
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O-acetyl-L-serine(thiol)lyase
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-
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O-acetylserine (Thiol)-lyase
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-
-
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O-acetylserine (thiol)lyase
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-
-
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O-acetylserine sulfhydrylase
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-
-
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O-acetylserine sulfhydrylase A
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-
-
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O-acetylserine(thiol)lyase
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-
-
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O-acetylserine-(thiol)lyase
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O-acetylserine-O-acetylhomoserine sulfhydro-lyase
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-
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OAS Shase
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-
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OAS thiol-lyases
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OAS-TL
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-
-
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OASS
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-
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OASTL
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-
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S-sulfocysteine synthase
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synthase, cysteine
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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-
-
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C-O bond cleavage
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-
-
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SYSTEMATIC NAME
IUBMB Comments
O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
A pyridoxal-phosphate protein. Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. Not identical with EC 2.5.1.51 (beta-pyrazolylalanine synthase), EC 2.5.1.52 (L-mimosine synthase) and EC 2.5.1.53 (uracilylalanine synthase).
CAS REGISTRY NUMBER
COMMENTARY hide
37290-89-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
enzyme that catalyzes the final step in cysteine biosynthesis. Cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
O-acetyl-L-serine + hydrogen sulfide
L-cysteine + acetate
show the reaction diagram
-
-
-
?
O-acetyl-L-Ser + H2S
L-Cys + acetate
show the reaction diagram
-
enzyme that catalyzes the final step in cysteine biosynthesis. Cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene cysK
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the CysK/CysE binding interaction is conserved in most bacterial and plant systems
metabolism
the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview
physiological function
enzyme CysK is organized in a complex with serine acetyltransferase (CysE), which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. CysK influences transcription in Gram-positive bacteria. In Bacillus subtilis, CysK modulates the affinity of an Rrf2-type transcription factor for its operator sequences, thereby regulating expression of the cysteine regulon. The enzyme from Bacillus subtilis interacts with CymR in transcription repression. CdiA-CT toxins are activated by CysK, also from other species
additional information
each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Albanesi, D.; Mansilla, M.C.; Schujman, G.E.; de Mendoza, D.
Bacillus subtilis cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation
J. Bacteriol.
187
7631-7638
2005
Bacillus subtilis
Manually annotated by BRENDA team
Hullo, M.F.; Auger, S.; Soutourina, O.; Barzu, O.; Yvon, M.; Danchin, A.; Martin-Verstraete, I.
Conversion of methionine to cysteine in Bacillus subtilis and its regulation
J. Bacteriol.
189
187-197
2007
Bacillus subtilis
Manually annotated by BRENDA team
Campanini, B.; Benoni, R.; Bettati, S.; Beck, C.M.; Hayes, C.S.; Mozzarelli, A.
Moonlighting O-acetylserine sulfhydrylase: new functions for an old protein
Biochim. Biophys. Acta
1854
1184-1193
2015
Arabidopsis thaliana (P47998), Bacillus subtilis (P37887), Caenorhabditis elegans (Q93244), Entamoeba histolytica (Q401L7), Escherichia coli (P0ABK5), Escherichia coli, Glycine max (A3RM03), Haemophilus influenzae (P45040), Mycobacterium tuberculosis (P9WP55), Salmonella enterica subsp. enterica serovar Typhimurium (P0A1E3), Staphylococcus aureus
Manually annotated by BRENDA team