ID   CBL_MYCTU               Reviewed;         407 AA.
AC   P9WQ83; L0TC32; P63502; Q50672;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Putative 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   OrderedLocusNames=Rv2294; ORFNames=MTCY339.16c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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   -!- 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; AL123456; CCP45076.1; -; Genomic_DNA.
DR   PIR; B70733; B70733.
DR   RefSeq; NP_216810.1; NC_000962.3.
DR   RefSeq; WP_003899255.1; NZ_NVQJ01000012.1.
DR   AlphaFoldDB; P9WQ83; -.
DR   SMR; P9WQ83; -.
DR   STRING; 83332.Rv2294; -.
DR   PaxDb; P9WQ83; -.
DR   GeneID; 45426274; -.
DR   GeneID; 885868; -.
DR   KEGG; mtu:Rv2294; -.
DR   TubercuList; Rv2294; -.
DR   eggNOG; COG1168; Bacteria.
DR   OMA; RINIGCP; -.
DR   PhylomeDB; P9WQ83; -.
DR   UniPathway; UPA00051; UER00078.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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:0016740; F:transferase activity; IEA:UniProt.
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; Reference proteome.
FT   CHAIN           1..407
FT                   /note="Putative cystathionine beta-lyase"
FT                   /id="PRO_0000163850"
FT   MOD_RES         237
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   407 AA;  44283 MW;  AA6296F845E2622F CRC64;
     MIPNPLEELT LEQLRSQRTS MKWRAHPADV LPLWVAEMDV KLPPTVADAL RRAIDDGDTG
     YPYGTEYAEA VREFACQRWQ WHDLEVSRTA IVPDVMLGIV EVLRLITDRG DPVIVNSPVY
     APFYAFVSHD GRRVIPAPLR GDGRIDLDAL QEAFSSARAS SGSSGNVAYL LCNPHNPTGS
     VHTADELRGI AERAQRFGVR VVSDEIHAPL IPSGARFTPY LSVPGAENAF ALMSASKAWN
     LGGLKAALAI AGREAAADLA RMPEEVGHGP SHLGVIAHTA AFRTGGNWLD ALLRGLDHNR
     TLLGALVDEH LPGVQYRWPQ GTYLAWLDCR ELGFDDAASD EMTEGLAVVS DLSGPARWFL
     DHARVALSSG HVFGIGGAGH VRINFATSRA ILIEAVSRMS RSLLERR