ID   CBL_CORGT               Reviewed;         368 AA.
AC   Q93QC6; Q6M3D6;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 104.
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;
OS   Corynebacterium glutamicum (Brevibacterium saccharolyticum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1718;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 13059 / ASO19;
RX   PubMed=11355704;
RA   Kim J.W., Kim H.J., Kim Y., Lee M.S., Lee H.S.;
RT   "Properties of the Corynebacterium glutamicum metC gene encoding
RT   cystathionine beta-lyase.";
RL   Mol. Cells 11:220-225(2001).
CC   -!- FUNCTION: Catalyzes the transformation of cystathionine to
CC       homocysteine. {ECO:0000269|PubMed:11355704}.
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         Evidence={ECO:0000269|PubMed:11355704};
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       {ECO:0000269|PubMed:11355704}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show methionine
CC       prototrophy, suggesting that additional methionine biosynthetic pathway
CC       can be present in C.glutamicum. The mutant strains also completely lose
CC       their ability to show resistance to the S-(beta-aminoethyl)-cysteine,
CC       which is a toxic lysine analog. {ECO:0000269|PubMed:11355704}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF276227; AAK69425.1; -; Genomic_DNA.
DR   RefSeq; WP_011015029.1; NZ_JOLA01000052.1.
DR   AlphaFoldDB; Q93QC6; -.
DR   SMR; Q93QC6; -.
DR   DNASU; 1020260; -.
DR   UniPathway; UPA00051; UER00078.
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   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Lyase; Methionine biosynthesis;
KW   Pyridoxal phosphate.
FT   CHAIN           1..368
FT                   /note="Cystathionine beta-lyase"
FT                   /id="PRO_0000425957"
FT   MOD_RES         221
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   368 AA;  40730 MW;  D6B7B95CBCD7244A CRC64;
     MRFPELEELK NRRTLKWTRF PEDVLPLWVA ESDFGTCPQL KEAMADAVER EVFGYPPDAT
     GLNDALTGFY ERRYGFGPNP ESVFAIPDVV RGLKLAIEHF TKPGSAIIVP LPAYPPFIEL
     PKVTGRQAIY IDAHEYDLKE IEKAFADGAG SLLFCNPHNP LGTVFSEEYI RELTDIAAKY
     DARIIVDEIH APLVYEGTHV VAAGVSENAA NTCITITATS KAWNTAGLKC AQIFFSNEAD
     VKAWKNLSDI TRDGVSILGL IAAETVYNEG EEFLDESIQI LKDNRDFAAA ELEKLGVKVY
     APDSTYLMWL DFAGTKIEEA PSKILREEGK VMLNDGAAFG GFTTCARLNF ACSRETLEEG
     LRRIASVL