METC_LACLM
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 03-AUG-2022, entry version 76.
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; Firmicutes; 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=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; 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; NZ_WJVF01000003.1.
DR AlphaFoldDB; A2RM21; -.
DR SMR; A2RM21; -.
DR STRING; 416870.llmg_1776; -.
DR EnsemblBacteria; CAL98348; CAL98348; llmg_1776.
DR KEGG; llm:llmg_1776; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_9; -.
DR OMA; MQTKLIH; -.
DR PhylomeDB; A2RM21; -.
DR BioCyc; LLAC416870:LLMG_RS08915-MON; -.
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: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_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
