ID   O15565_TRIVA            Unreviewed;       398 AA.
AC   O15565; A2FVC9;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   18-JUN-2025, entry version 131.
DE   RecName: Full=L-methionine gamma-lyase {ECO:0000256|ARBA:ARBA00019040};
DE            EC=4.4.1.1 {ECO:0000256|ARBA:ARBA00012085};
DE            EC=4.4.1.11 {ECO:0000256|ARBA:ARBA00012222};
DE   AltName: Full=Gamma-cystathionase {ECO:0000256|ARBA:ARBA00029853};
GN   Name=mgl2 {ECO:0000313|EMBL:CAA04125.1};
OS   Trichomonas vaginalis.
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=5722 {ECO:0000313|EMBL:CAA04125.1};
RN   [1] {ECO:0000313|EMBL:CAA04125.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9488680; DOI=10.1074/jbc.273.10.5549;
RA   McKie A.E., Edlind T., Walker J., Mottram J.C., Coombs G.H.;
RT   "The primitive protozoon Trichomonas vaginalis contains two methionine
RT   gamma-lyase genes that encode members of the gamma-family of pyridoxal 5'-
RT   phosphate-dependent enzymes.";
RL   J. Biol. Chem. 273:5549-5556(1998).
RN   [2] {ECO:0007829|PDB:1PFF}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 68-398.
RA   Allen T.W., Sridhar V., Prasad S.G., Han Q., Xu M., Tan Y., Hoffman R.M.,
RA   Ramaswamy S.;
RT   "Crystal Structure of Homocysteine alpha-, gamma-lyase at 1.8 Angstroms.";
RL   Submitted (MAY-2003) to the PDB data bank.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-methionine + H2O = methanethiol + 2-oxobutanoate + NH4(+);
CC         Xref=Rhea:RHEA:23800, ChEBI:CHEBI:15377, ChEBI:CHEBI:16007,
CC         ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; EC=4.4.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00049180};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362118};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-homocysteine and L-serine: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00005038}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. L-
CC       methionine gamma-lyase subfamily. {ECO:0000256|ARBA:ARBA00008667}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ000487; CAA04125.1; -; Genomic_DNA.
DR   PDB; 1PFF; X-ray; 2.50 A; A/B=68-398.
DR   AlphaFoldDB; O15565; -.
DR   SMR; O15565; -.
DR   FunCoup; O15565; 183.
DR   STRING; 5722.O15565; -.
DR   VEuPathDB; TrichDB:TVAG_147790; -.
DR   VEuPathDB; TrichDB:TVAGG3_0403510; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   InParanoid; O15565; -.
DR   OMA; YKQDGVG; -.
DR   BRENDA; 4.4.1.11; 6459.
DR   EvolutionaryTrace; O15565; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0018826; F:methionine gamma-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   FunFam; 3.40.640.10:FF:000046; Cystathionine gamma-lyase; 1.
DR   FunFam; 3.90.1150.10:FF:000008; Cystathionine gamma-synthase; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR006237; L-Met_gamma_lys.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01328; met_gam_lyase; 1.
DR   PANTHER; PTHR11808:SF80; CYSTATHIONINE GAMMA-LYASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PDBsum; 1PFF; -.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1PFF};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CAA04125.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         212
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   398 AA;  43112 MW;  48A1AB942B3B400A CRC64;
     MSGHAIDPTH TDTLSIHANP QKDQFGAIVA PIYQTSTFLF DNCDQGGARF GGKEAGYMYT
     RIGNPTNSAL EGKIAKLEHA EACAATASGM GAIAASVWTF LKAGDHLISD DCLYGCTHAL
     FEHQLRKFGV EVDFIDMAVP GNIEKHLKPN TRIVYFETPA NPTLKVIDIE DAVKQARKQK
     DILVIVDNTF ASPILTNPLD LGVDIVVHSA TKYINGHTDV VAGLVCSRAD IIAKVKSQGI
     KDITGAIISP HDAWLITRGT LTLDMRVKRA AENAQKVAEF LHEHKAVKKV YYPGLPDHPG
     HEIAKKQMKM FGSMIAFDVD GLEKAKKVLD NCHVVSLAVS LGGPESLIQH PASMTHAGVP
     KEEREAAGLT DNLIRLSVGC ENVQDIIDDL KQALDLVL
//