ID   METC_BORAV              Reviewed;         396 AA.
AC   Q07703;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Cystathionine beta-lyase;
DE            Short=CBL;
DE            EC=4.4.1.13 {ECO:0000250|UniProtKB:P06721};
DE   AltName: Full=Beta-cystathionase;
DE   AltName: Full=Cysteine lyase;
DE   AltName: Full=Cysteine-S-conjugate beta-lyase;
DE   AltName: Full=Osteotoxin;
GN   Name=metC;
OS   Bordetella avium.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-33, AND FUNCTION.
RC   STRAIN=197;
RX   PubMed=8463265; DOI=10.1016/s0021-9258(18)53176-8;
RA   Gentry-Weeks C.R., Keith J.M., Thompson J.;
RT   "Toxicity of Bordetella avium beta-cystathionase toward MC3T3-E1 osteogenic
RT   cells.";
RL   J. Biol. Chem. 268:7298-7314(1993).
CC   -!- FUNCTION: Catalyzes the cleavage of cystathionine to homocysteine,
CC       pyruvate and ammonia during methionine biosynthesis (By similarity).
CC       Also has cytotoxic activity toward osteogenic, osteosarcoma and
CC       tracheal cells, in vitro. The chemical basis for cell toxicity might be
CC       the formation and subsequent transfer of sulfane-sulfur to proteins,
CC       derived via beta-cystathionase cleavage of L-cystine (PubMed:8463265).
CC       {ECO:0000250|UniProtKB:P06721, ECO:0000269|PubMed:8463265}.
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:0000250|UniProtKB:P06721};
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         Evidence={ECO:0000250|UniProtKB:P06721};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P06721};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homocysteine from L-cystathionine: step 1/1.
CC       {ECO:0000250|UniProtKB:P06721}.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06721}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000305}.
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DR   EMBL; L10425; AAA22978.1; -; Genomic_DNA.
DR   PIR; A46084; A46084.
DR   RefSeq; WP_012419002.1; NZ_UFTG01000001.1.
DR   AlphaFoldDB; Q07703; -.
DR   SMR; Q07703; -.
DR   GeneID; 41395197; -.
DR   OMA; LVYEMCD; -.
DR   UniPathway; UPA00051; UER00078.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
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; IPR006233; Cys_b_lyase_bac.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43500; PTHR43500; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01324; cysta_beta_ly_B; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Cytoplasm; Direct protein sequencing; Lyase;
KW   Methionine biosynthesis; Pyridoxal phosphate.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8463265"
FT   CHAIN           2..396
FT                   /note="Cystathionine beta-lyase"
FT                   /id="PRO_0000114767"
FT   MOD_RES         214
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P06721"
SQ   SEQUENCE   396 AA;  42610 MW;  F0D11DA6E108F064 CRC64;
     MSDTSAKHID TLLQHLGSAP FNPDTGAAPV NLPSVRASTV RFQSLAKLED AQRRKAAGER
     ASTYGRMGMD THAALEQVFA ELEGGTHCYL ASSGLAGISM VFLSLLSAGE HALVADCAYG
     PVHELHEAVL SRLGIDVTFF DAKADLASLV RPTTRLIFAE APGSLLFEML DMPALARFAK
     QHDLILATDN TWGSGYIYRP LTLGAQVSVI AGTKYVGGHS DLMLGAVVTN DEAIAKRLNR
     TQYALGYSVS ADDAWLALRG VRTMPVRMAQ HARHALEVCE FLQNRPEVVR LYHPAWPADP
     GHALWQRDCS GSNGMLAVQL GLSPQAARDF VNALTLFGIG FSWGGFESLV QLVTPGELAR
     HQYWQGGSDA LVRLHIGLES PADLIADLAQ ALDRAA