| General Information |
| MoonProt ID | 200 |
| First appeared in release | 1.0 |
| Name(s) | MalY
Cystathionine beta-lyase MalY
Beta-cystathionase
Cysteine lyase
CBL
Gene Name:malY |
| UniProt ID | P23256 (MALY_ECOLI), Reviewed |
| GO terms | GO:0006351 transcription, DNA-templated
GO:0006355 regulation of transcription, DNA-templated
GO:0008652 cellular amino acid biosynthetic process
GO:0009058 biosynthetic process
GO:0009086 methionine biosynthetic process
GO:0043433 negative regulation of sequence-specific DNA binding transcription factor activity
GO:0003824 catalytic activity
GO:0004121 cystathionine beta-lyase activity
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0080146 L-cysteine desulfhydrase activity |
| Organisms for which functions have been demonstrated | Escherichia coli (Gram negative bacterium) |
| Sequence length | 390 |
| FASTA sequence | >sp|P23256|MALY_ECOLI Protein MalY OS=Escherichia coli (strain K12) GN=malY PE=1 SV=1
MFDFSKVVDRHGTWCTQWDYVADRFGTADLLPFTISDMDFATAPCIIEALNQRLMHGVFGYSRWKNDEFLAAIAHWFSTQHYTAIDSQTVVYGPSVIYMVSELIRQWSETGEGVVIHTPAYDAFYKAIEGNQRTVMPVALEKQADGWFCDMGKLEAVLAKPECKIMLLCSPQNPTGKVWTCDELEIMADLCERHGVRVISDEIHMDMVWGEQPHIPWSNVARGDWALLTSGSKSFNIPALTGAYGIIENSSSRDAYLSALKGRDGLSSPSVLALTAHIAAYQQGAPWLDALRIYLKDNLTYIADKMNAAFPELNWQIPQSTYLAWLDLRPLNIDDNALQKALIEQEKVAIMPGYTYGEEGRGFVRLNAGCPRSKLEKGVAGLINAIRAVR
|
| Structure Information |
| PDB ID | 1D2F |
| Quaternary structure | |
| SCOP | PLP-dependent transferase-like |
| CATH | 3.90.1150.10, 3.40.640.10 |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 389-390 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | beta-cystathionase, enzyme
cleavage of cystathionine to homocysteine, ammonia, and pyruvate
L-cystathionine + H2O => L-homocysteine + NH3 + pyruvate
Amino-acid biosynthesis, methionine biosynthesis |
| References for function | Zdych E, Peist R, Reidl J, Boos W. MalY of Escherichia coli is an enzyme with the activity of a beta C-S lyase (cystathionase). J Bacteriol. 1995 Sep. PMID: 7665481 |
| E.C. number | 4.4.1.8 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | transcription regulation binds to MalT activator of mal regulon and prevents its action |
| References for function | Joly N, Danot O, Schlegel A, Boos W, Richet E. The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon. J Biol Chem. 2002 May 10. PMID: 11867639
Zdych E, Peist R, Reidl J, Boos W. MalY of Escherichia coli is an enzyme with the activity of a beta C-S lyase (cystathionase). J Bacteriol. 1995 Sep. PMID: 7665481 |
| E.C. number | N/A |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |