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InterPro: IPR005859 Cysteine synthase A

Protein matchesHelp
UniProtKB
Matches:
1694 proteins
AccessionHelp IPR005859 CysK
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR005856 Cysteine synthase K/M
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 synthase A (CysK) and cysteine synthase B (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, EC:2.5.1.47) 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). CysK differs from CysM in that it can also use sulphide instead of thiosulphate, to produce cysteine instead of cysteine thiosulphonate.

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
IPR005859 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
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
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
Heine A, Canaves JM, von Delft F, Brinen LS, Dai X, Deacon AM, Elsliger MA, Eshaghi S, Floyd R, Godzik A, Grittini C, Grzechnik SK, Guda C, Jaroszewski L, Karlak C, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, McMullan D, McPhillips TM, Miller MA, Miller MD, Morse A, Moy K, Ouyang J, Page R, Robb A, Rodrigues K, Schwarzenbacher R, Selby TL, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Hodgson KO, Wooley J, Wilson IA.
Crystal structure of O-acetylserine sulfhydrylase (TM0665) from Thermotoga maritima at 1.8 A resolution.
Proteins 56 2004 387-91 [PubMed: 15211522]
http://dx.doi.org/10.1002/prot.20003
Bonner ER, Cahoon RE, Knapke SM, Jez JM.
Molecular basis of cysteine biosynthesis in plants: structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana.
J. Biol. Chem. 280 2005 38803-13 [PubMed: 16166087]
http://dx.doi.org/10.1074/jbc.M505313200
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