ID   METC_LACLC              Reviewed;         380 AA.
AC   P0C2T9; P0A4K3; Q9RAS7; Q9RAS9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 46.
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;
OS   Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=NIZO B78;
RX   PubMed=10618201; DOI=10.1128/aem.66.1.42-48.2000;
RA   Fernandez M., van Doesburg W., Rutten G.A.M., Marugg J.D., Alting A.C.,
RA   van Kranenburg R., Kuipers O.P.;
RT   "Molecular and functional analyses of the metC gene of Lactococcus lactis,
RT   encoding cystathionine beta-lyase.";
RL   Appl. Environ. Microbiol. 66:42-48(2000).
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; AF131881; AAF14695.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C2T9; -.
DR   SMR; P0C2T9; -.
DR   UniPathway; UPA00051; UER00078.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Cytoplasm; Lyase; Methionine biosynthesis;
KW   Pyridoxal phosphate.
FT   CHAIN           1..380
FT                   /note="Cystathionine beta-lyase"
FT                   /id="PRO_0000114773"
FT   MOD_RES         196
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   380 AA;  40984 MW;  D4F8CA9F70CA8569 CRC64;
     MTSLKTKVIH GGISTDRTTG AVSVPIYQTS TYKQNGLGQP KEYEYSRSGN PTRHALEELI
     ADLEGGVQGF AFSSGLAGIH AVLSLFSAGD HIILADDVYG GTFRLVDKVL TKTGIIYDLV
     DLSNLEDLKA AFKAETKAVY FETPSNPLLK VLDIKEISSI AKAHNALTLV DNTFATPYLQ
     QPIALGADIV LHSATKYLGG HSDVVAGLVT TNSNELAIEI GFLQNSIGAV LGPQDSWLVQ
     RGIKTLAPRM EAHSANAQKI AEFLEASQAV SKVYYPGLVN HEGHEIAKKQ MTAFGGMISF
     ELTDENAVKN FVENLRYFTL AESLGGVESL IEVPAVMTHA SIPKELREEI GIKDGLIRLS
     VGVEALEDLL TDLKEALEKE