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Reviewed, UniProtKB/Swiss-Prot P0C2T9 (METC_LACLC)

Last modified June 16, 2009. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cystathionine beta-lyase
      Short name=CBL
    EC=4.4.1.8
Alternative name(s):
    Beta-cystathionase
    Cysteine lyase
Gene names
Name: metC
Synonyms: metB2
OrganismLactococcus lactis subsp. cremoris (Streptococcus cremoris)
Taxonomic identifier1359 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the trans-sulfuration enzymes family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Methionine biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionLyase
Gene Ontology (GO)
   Biological processmethionine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncystathionine beta-lyase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 380380Cystathionine beta-lyase
PRO_0000114773

Amino acid modifications

Modified residue1961N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C2T9-1 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: D4F8CA9F70CA8569

FASTA38040,984
        10         20         30         40         50         60 
MTSLKTKVIH GGISTDRTTG AVSVPIYQTS TYKQNGLGQP KEYEYSRSGN PTRHALEELI 

        70         80         90        100        110        120 
ADLEGGVQGF AFSSGLAGIH AVLSLFSAGD HIILADDVYG GTFRLVDKVL TKTGIIYDLV 

       130        140        150        160        170        180 
DLSNLEDLKA AFKAETKAVY FETPSNPLLK VLDIKEISSI AKAHNALTLV DNTFATPYLQ 

       190        200        210        220        230        240 
QPIALGADIV LHSATKYLGG HSDVVAGLVT TNSNELAIEI GFLQNSIGAV LGPQDSWLVQ 

       250        260        270        280        290        300 
RGIKTLAPRM EAHSANAQKI AEFLEASQAV SKVYYPGLVN HEGHEIAKKQ MTAFGGMISF 

       310        320        330        340        350        360 
ELTDENAVKN FVENLRYFTL AESLGGVESL IEVPAVMTHA SIPKELREEI GIKDGLIRLS 

       370        380 
VGVEALEDLL TDLKEALEKE 

« Hide

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.
Strain: NIZO B78.

Cross-references

Sequence databases

AF131881 Genomic DNA. Translation: AAF14695.1.

3D structure databases

HSSPHSSP built from PDB template 1GC0 based on UniProtKB P13254.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.4.1.8. 289716.

Family and domain databases

InterProIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
PANTHERPTHR11808. Cys_Met_Meta_PP. 1 hit.
PfamPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFPIRSF001434. CGS. 1 hit.
PROSITEPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMETC_LACLC
AccessionPrimary (citable) accession number: P0C2T9
Secondary accession number(s): P0A4K3, Q9RAS7, Q9RAS9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: June 16, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents