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   16-JUN-2009, entry version 58.
DE   RecName: Full=Cystathionine beta-lyase;
DE            Short=CBL;
DE            EC=4.4.1.8;
DE   AltName: Full=Beta-cystathionase;
DE   AltName: Full=Cysteine 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], AND PROTEIN SEQUENCE OF 2-33.
RC   STRAIN=197;
RX   MEDLINE=93216672; PubMed=8463265;
RA   Gentry-Weeks C.R., Keith J.M., Thompson J.;
RT   "Toxicity of Bordetella avium beta-cystathionase toward MC3T3-E1
RT   osteogenic cells.";
RL   J. Biol. Chem. 268:7298-7314(1993).
CC   -!- FUNCTION: Also has cytotoxic activity toward osteogenic,
CC       osteosarcoma and tracheal cells, in vitro. The chemical basis for
CC       cell toxicity might be the formation and subsequent transfer of
CC       sulfane-sulfur to proteins, derived via beta-cystathionase
CC       cleavage of L-cystine.
CC   -!- CATALYTIC ACTIVITY: L-cystathionine + H(2)O = L-homocysteine +
CC       NH(3) + pyruvate.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homocysteine from L-cystathionine: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
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DR   EMBL; L10425; AAA22978.1; -; Genomic_DNA.
DR   PIR; A46084; A46084.
DR   HSSP; P13254; 1GC0.
DR   BRENDA; 4.4.1.8; 21480.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR006233; Cys_b_lyase_bac.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   PANTHER; PTHR11808:SF8; Cys_b_lyase_bac; 1.
DR   PANTHER; PTHR11808; Cys_Met_Meta_PP; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 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      1       Removed.
FT   CHAIN         2    396       Cystathionine beta-lyase.
FT                                /FTId=PRO_0000114767.
FT   MOD_RES     214    214       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
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
//