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InterPro: IPR005856 Cysteine synthase K/M

Protein matchesHelp
UniProtKB
Matches:
2168 proteins
AccessionHelp IPR005856 Cys_synthKM
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Children IPR005858 Cysteine synthase B
IPR005859 Cysteine synthase A
Contains IPR001216 Cysteine synthase/cystathionine beta-synthase P-phosphate-binding site
IPR001926 Pyridoxal phosphate-dependent enzyme, beta subunit
GO Term annotationHelp
Process GO:0006535 cysteine biosynthetic process from serine
Function GO:0004124 cysteine synthase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This model discriminates cysteine synthases (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblance to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded.

Cysteine synthase (O-acetylserine (thiol)-lyase) is the enzyme responsible for the formation of cysteine from O-acetyl-serine and hydrogen sulphide with the concomitant release of acetic acid. In bacteria such two forms of the enzyme are known (genes cysK and cysM). CysM differs from CysK in that it can also use thiosulphate instead of sulphide, to produce cysteine thiosulphonate instead of cysteine.

Structural linksHelp
SCOP: c.79.1.1
CATH: 3.40.50.1100
Database linksHelp
Enzyme: EC:2.5.1.47

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR005856 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P0A1E3 Cysteine synthase A

P47998 Cysteine synthase

P73410 Cysteine synthase

Q59966 Cysteine synthase, plasmid

Q9XEA6 Cysteine synthase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001216 Cysteine synthase/cystathionine beta-synthase P-phosphate-binding site
IPR005856 Cysteine synthase K/M
IPR001926 Pyridoxal phosphate-dependent enzyme, beta subunit
IPR005859 Cysteine synthase A
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp

Additional ReadingHelp
Chattopadhyay A, Meier M, Ivaninskii S, Burkhard P, Speroni F, Campanini B, Bettati S, Mozzarelli A, Rabeh WM, Li L, Cook PF.
Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes.
Biochemistry 46 2007 8315-30 [PubMed: 17583914]
http://dx.doi.org/10.1021/bi602603c
Huang B, Vetting MW, Roderick SL.
The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase.
J. Bacteriol. 187 2005 3201-5 [PubMed: 15838047]
http://dx.doi.org/10.1128/JB.187.9.3201-3205.2005
Claus MT, Zocher GE, Maier TH, Schulz GE.
Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli.
Biochemistry 44 2005 8620-6 [PubMed: 15952768]
http://dx.doi.org/10.1021/bi050485+
Schnell R, Oehlmann W, Singh M, Schneider G.
Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex.
J. Biol. Chem. 282 2007 23473-81 [PubMed: 17567578]
http://dx.doi.org/10.1074/jbc.M703518200
Francois JA, Kumaran S, Jez JM.
Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex.
Plant Cell 18 2006 3647-55 [PubMed: 17194764]
http://dx.doi.org/10.1105/tpc.106.047316
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InterPro 23.1