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InterPro: IPR001216 Cysteine synthase/cystathionine beta-synthase P-phosphate-binding site

Protein matchesHelp
UniProtKB
Matches:
3042 proteins
AccessionHelp IPR001216 Cys_synth_BS
TypeHelp Binding_site
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR001926 Pyridoxal phosphate-dependent enzyme, beta subunit
IPR005856 Cysteine synthase K/M
IPR005857 Cystathionine beta-synthase
IPR005858 Cysteine synthase B
IPR005859 Cysteine synthase A
GO Term annotationHelp
Process GO:0006535 cysteine biosynthetic process from serine
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Cysteine synthase (EC:4.2.99.8) (CSase) is the enzyme responsible for the formation of cysteine from O-acetyl-serine and hydrogen sulphide with the concomitant release of acetic acid [1]. In bacteria two such forms of the enzyme are known (genes cysK and cysM). In plants there are also two forms, one located in the cytoplasm and the other in chloroplasts.

Cystathionine beta-synthase (EC:4.2.1.22) that catalyses the first irreversible step in homocysteine transulphuration; the conjugation of homocysteine and serine forming cystathionine, also belongs to this group of sequences [2]. Both synthases are pyridoxal-phosphate dependent and are evolutionary related. The pyridoxal-phosphate attaches to the lysine residue which is part of this signature and which is found in the N-terminal section of these enzymes; the sequence around the lysine residue is highly conserved.

Structural linksHelp
SCOP: c.79.1.1
CATH: 3.40.50.1100
Database linksHelp
PDBe-motif: PS00901
Enzyme: EC:2.5.1.47
PROSITE doc: PDOC00700
COMe: PRX000818

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001216 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P32582 Cystathionine beta-synthase

P35520 Cystathionine beta-synthase

P47998 Cysteine synthase

Q91WT9 Cystathionine beta-synthase

Q9XEA6 Cysteine synthase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR005856 Cysteine synthase K/M
IPR001216 Cysteine synthase/cystathionine beta-synthase P-phosphate-binding site
IPR000644 Cystathionine beta-synthase, core
IPR001926 Pyridoxal phosphate-dependent enzyme, beta subunit
IPR005859 Cysteine synthase A
IPR005857 Cystathionine beta-synthase
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Saito K, Kurosawa M, Murakoshi I.
Determination of a functional lysine residue of a plant cysteine synthase by site-directed mutagenesis, and the molecular evolutionary implications.
FEBS Lett. 328 111-4 1993 [PubMed: 8344414]
http://dx.doi.org/10.1016/0014-5793(93)80976-2
2. Swaroop M, Bradley K, Ohura T, Tahara T, Roper MD, Rosenberg LE, Kraus JP.
Rat cystathionine beta-synthase. Gene organization and alternative splicing.
J. Biol. Chem. 267 11455-61 1992 [PubMed: 1597473]
http://intl.jbc.org/cgi/content/abstract/267/16/11455

Additional ReadingHelp
Oda Y, Mino K, Ishikawa K, Ataka M.
Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution.
J. Mol. Biol. 351 2005 334-44 [PubMed: 16005886]
http://dx.doi.org/10.1016/j.jmb.2005.05.064
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
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