ID   METC_LACLM              Reviewed;         380 AA.
AC   A2RM21; P0A4K3; Q9RAS7; Q9RAS9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   02-SEP-2026, entry version 92.
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=llmg_1776;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=10620674; DOI=10.1111/j.1574-6968.2000.tb08903.x;
RA   Dobric N., Limsowtin G.K., Hillier A.J., Dudman N.P., Davidson B.E.;
RT   "Identification and characterization of a cystathionine beta/gamma-lyase
RT   from Lactococcus lactis ssp. cremoris MG1363.";
RL   FEMS Microbiol. Lett. 182:249-254(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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=L,L-cystathionine + H2O = L-homocysteine + pyruvate + NH4(+);
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 + pyruvate +
CC         NH4(+); 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; AF131880; AAF14693.1; -; Genomic_DNA.
DR   EMBL; AF170901; AAF36088.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL98348.1; -; Genomic_DNA.
DR   PIR; T47232; T47232.
DR   RefSeq; WP_010905558.1; NC_009004.1.
DR   AlphaFoldDB; A2RM21; -.
DR   SMR; A2RM21; -.
DR   STRING; 416870.llmg_1776; -.
DR   PaxDb; 416870-llmg_1776; -.
DR   GeneID; 89632914; -.
DR   KEGG; llm:llmg_1776; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_0_9; -.
DR   OrthoDB; 9780685at2; -.
DR   PhylomeDB; A2RM21; -.
DR   BRENDA; 4.4.1.1; 2903.
DR   BRENDA; 4.4.1.13; 2903.
DR   UniPathway; UPA00051; UER00078.
DR   Proteomes; UP000000364; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:TreeGrafter.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:TreeGrafter.
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:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   FunFam; 3.90.1150.10:FF:000008; Cystathionine gamma-synthase; 1.
DR   FunFam; 3.40.640.10:FF:000009; Cystathionine gamma-synthase homolog; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR054542; Cys_met_metab_PP.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF004821; PRK06176.1; 1.
DR   NCBIfam; NF005810; PRK07671.1; 1.
DR   NCBIfam; NF005871; PRK07811.1; 1.
DR   PANTHER; PTHR11808:SF15; CYSTATHIONINE GAMMA-LYASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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; Reference proteome.
FT   CHAIN           1..380
FT                   /note="Cystathionine beta-lyase"
FT                   /id="PRO_0000285238"
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
//