Reviewed,
UniProtKB/Swiss-Prot P0A4K2 (METC_LACLA)
Last modified
November 3, 2009.
Version 35.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 |
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| Organism | Lactococcus lactis subsp. lactis (Streptococcus lactis) [Complete proteome] [HAMAP] | ||||||||
| Taxonomic identifier | 1360 [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 | Inferred from homology. |
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
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References
| [1] | "The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403." Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A. Genome Res. 11:731-753(2001) [PubMed: 11337471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IL1403. |
Cross-references
Sequence databases | |
|---|---|
| AE005176 Genomic DNA. Translation: AAK04879.1. | |
| PIR | E86722. |
| RefSeq | NP_266937.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GC0 based on UniProtKB P13254. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1114408. |
| GenomeReviews | Gene locus LL0781 in contig AE005176_GR. |
| KEGG | lla:L0181. |
| NMPDR | fig|272623.1.peg.801. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0A4K2. |
| OMA | NQYEYSR. |
Enzyme and pathway databases | |
| BioCyc | LLAC272623:L0181-MON. |
| BRENDA | 4.4.1.8. 278870. |
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_LACLA | ||||||||
| Accession | Primary (citable) accession number: P0A4K2 Secondary accession number(s): Q9RAS7, Q9RAS9 | ||||||||
| Entry history |
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| 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


