P06721 · METC_ECOLI
- ProteinCystathionine beta-lyase MetC
- GenemetC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids395 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Primarily catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis (PubMed:7049234).
Also exhibits cysteine desulfhydrase activity, producing sulfide from cysteine (PubMed:12883870).
In addition, under certain growth conditions, exhibits significant alanine racemase coactivity (PubMed:21193606).
Also exhibits cysteine desulfhydrase activity, producing sulfide from cysteine (PubMed:12883870).
In addition, under certain growth conditions, exhibits significant alanine racemase coactivity (PubMed:21193606).
Catalytic activity
- H2O + L,L-cystathionine = L-homocysteine + NH4+ + pyruvate
Cofactor
Activity regulation
L-cysteine inhibits cystathionine beta-lyase activity competitively (PubMed:7049234).
Inhibited by aminoethoxyvinylglycine (AVG) (PubMed:9376370).
Inhibited by aminoethoxyvinylglycine (AVG) (PubMed:9376370).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.04 mM | L-cystathionine | |||||
0.25 mM | L-cystine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
249 μmol/min/mg | with L-cystathionine as substrate | ||||
263 μmol/min/mg | with L-cystine as substrate |
pH Dependence
Optimum pH is 8.0-9.0.
Pathway
Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | protein-containing complex | |
Molecular Function | alanine racemase activity | |
Molecular Function | cysteine-S-conjugate beta-lyase activity | |
Molecular Function | identical protein binding | |
Molecular Function | L-cysteine desulfhydrase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | L-cysteine catabolic process to pyruvate | |
Biological Process | methionine biosynthetic process | |
Biological Process | protein homotetramerization | |
Biological Process | transsulfuration |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCystathionine beta-lyase MetC
- EC number
- Short namesCBL ; CL
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP06721
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Disruption of the gene increases the amounts of L-cysteine and L-cystine produced after 72 hours of cultivation.
Chemistry
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000114768 | 2-395 | Cystathionine beta-lyase MetC | |||
Sequence: ADKKLDTQLVNAGRSKKYTLGAVNSVIQRASSLVFDSVEAKKHATRNRANGELFYGRRGTLTHFSLQQAMCELEGGAGCVLFPCGAAAVANSILAFIEQGDHVLMTNTAYEPSQDFCSKILSKLGVTTSWFDPLIGADIVKHLQPNTKIVFLESPGSITMEVHDVPAIVAAVRSVVPDAIIMIDNTWAAGVLFKALDFGIDVSIQAATKYLVGHSDAMIGTAVCNARCWEQLRENAYLMGQMVDADTAYITSRGLRTLGVRLRQHHESSLKVAEWLAEHPQVARVNHPALPGSKGHEFWKRDFTGSSGLFSFVLKKKLNNEELANYLDNFSLFSMAYSWGGYESLILANQPEHIAAIRPQGEIDFSGTLIRLHIGLEDVDDLIADLDAGFARIV | ||||||
Modified residue | 210 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Proteomic databases
Structure
Sequence
- Sequence statusComplete
- Length395
- Mass (Da)43,212
- Last updated1988-01-01 v1
- ChecksumFD3308423D6427C6
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M12858 EMBL· GenBank· DDBJ | AAA24158.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U28377 EMBL· GenBank· DDBJ | AAA69175.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
U00096 EMBL· GenBank· DDBJ | AAC76044.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE77065.1 EMBL· GenBank· DDBJ | Genomic DNA |