ID   METC_LACLA              Reviewed;         380 AA.
AC   P0A4K2; Q9RAS7; Q9RAS9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Cystathionine beta-lyase;
DE            Short=CBL;
DE            EC=4.4.1.13;
DE   AltName: Full=Beta-cystathionase;
DE   AltName: Full=Cysteine lyase;
DE   AltName: Full=Cysteine-S-conjugate beta-lyase;
GN   Name=metC; Synonyms=metB2; OrderedLocusNames=LL0781; ORFNames=L0181;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: The enzymatic degradation of amino acids in cheese is
CC       believed to generate aroma compounds and therefore to be essential for
CC       flavor development. Cystathionine beta-lyase (CBL) can convert
CC       cystathionine to homocysteine but is also able to catalyze an alpha,
CC       gamma elimination. With methionine as a substrate, it produces volatile
CC       sulfur compounds which are important for flavor formation in Gouda
CC       cheese.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) +
CC         pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homocysteine from L-cystathionine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000305}.
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DR   EMBL; AE005176; AAK04879.1; -; Genomic_DNA.
DR   PIR; E86722; E86722.
DR   RefSeq; NP_266937.1; NC_002662.1.
DR   RefSeq; WP_010905558.1; NC_002662.1.
DR   AlphaFoldDB; P0A4K2; -.
DR   SMR; P0A4K2; -.
DR   STRING; 272623.L0181; -.
DR   PaxDb; P0A4K2; -.
DR   EnsemblBacteria; AAK04879; AAK04879; L0181.
DR   KEGG; lla:L0181; -.
DR   PATRIC; fig|272623.7.peg.836; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_0_9; -.
DR   OMA; MQTKLIH; -.
DR   UniPathway; UPA00051; UER00078.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:RHEA.
DR   GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808; PTHR11808; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Lyase; Methionine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..380
FT                   /note="Cystathionine beta-lyase"
FT                   /id="PRO_0000114772"
FT   MOD_RES         196
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   380 AA;  40938 MW;  77A580507FE50B0D CRC64;
     MTSIKTKVIH GGISTDKTTG AVSVPIYQTS TYKQNGLGQP KEYEYSRSGN PTRHALEELI
     ADLEGGVQGF AFSSGLAGIH AVLSLFSAGD HIILADDVYG GTFRLMDKVL TKTGIIYDLV
     DLSNLDDLKA AFKEETKAIY FETPSNPLLK VLDIKEISAI AKAHDALTLV DNTFATPYLQ
     QPIALGADIV LHSATKYLGG HSDVVAGLVT TNSKELASEI GFLQNSIGAV LGPQDSWLVQ
     RGIKTLALRM EAHSANAQKI AEFLETSKAV SKVYYPGLNS HPGHEIAKKQ MSAFGGMISF
     ELTDENAVKD FVENLSYFTL AESLGGVESL IEVPAVMTHA SIPKELREEI GIKDGLIRLS
     VGVEAIEDLL TDIKEALEKK