Reviewed,
UniProtKB/Swiss-Prot A2RM21 (METC_LACLM)
Last modified
November 3, 2009.
Version 19.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Cystathionine beta-lyase Short name=CBL EC=4.4.1.8 Alternative name(s): Beta-cystathionase Cysteine lyase | ||||||
| Gene names |
| ||||||
| Organism | Lactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 416870 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus |
Protein attributes
| Sequence length | 380 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | The enzymatic degradation of amino acids in cheese is believed to generate aroma compounds and therefore to be essential for flavor development. Cystathionine beta-lyase (CBL) can convert cystathionine to homocysteine but is also able to catalyze an alpha, gamma elimination. With methionine as a substrate, it produces volatile sulfur compounds which are important for flavor formation in Gouda cheese. |
| Catalytic activity | L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Pathway | |
| Subcellular location | |
| Sequence similarities | Belongs to the trans-sulfuration enzymes family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Methionine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Pyridoxal phosphate |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | cystathionine beta-lyase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Molecular and functional analyses of the metC gene of Lactococcus lactis, encoding cystathionine beta-lyase." Fernandez M., van Doesburg W., Rutten G.A.M., Marugg J.D., Alting A.C., van Kranenburg R., Kuipers O.P. Appl. Environ. Microbiol. 66:42-48(2000) [PubMed: 10618201] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. |
| [2] | "Identification and characterization of a cystathionine beta/gamma-lyase from Lactococcus lactis ssp. cremoris MG1363." Dobric N., Limsowtin G.K., Hillier A.J., Dudman N.P., Davidson B.E. FEMS Microbiol. Lett. 182:249-254(2000) [PubMed: 10620674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. |
| [3] | "The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363." Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J. J. Bacteriol. 189:3256-3270(2007) [PubMed: 17307855] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AF131880 Genomic DNA. Translation: AAF14693.1. AF170901 Genomic DNA. Translation: AAF36088.1. AM406671 Genomic DNA. Translation: CAL98348.1. | |
| PIR | T47232. |
| RefSeq | YP_001033049.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GC0 based on UniProtKB P13254. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A2RM21. |
Genome annotation databases | |
| GeneID | 4798866. |
| GenomeReviews | Gene locus llmg_1776 in contig AM406671_GR. |
| KEGG | llm:llmg_1776. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | NQYEYSR. |
Family and domain databases | |
| InterPro | IPR000277. Cys/Met-Metab_PyrdxlP-dep_enz. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit. |
| PANTHER | PTHR11808. Cys_Met_Meta_PP. 1 hit. |
| Pfam | PF01053. Cys_Met_Meta_PP. 1 hit. [Graphical view] |
| PIRSF | PIRSF001434. CGS. 1 hit. |
| PROSITE | PS00868. CYS_MET_METAB_PP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | METC_LACLM | ||||||||
| Accession | Primary (citable) accession number: A2RM21 Secondary accession number(s): P0A4K3, Q9RAS7, Q9RAS9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


