ID   MEGL_PSEDM              Reviewed;         399 AA.
AC   A0A0J6G7P5; A0A0F6P9W0;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=L-methionine gamma-lyase {ECO:0000250|UniProtKB:P13254};
DE            Short=MGL {ECO:0000250|UniProtKB:P13254};
DE            EC=4.4.1.11 {ECO:0000250|UniProtKB:P13254};
GN   Name=megL {ECO:0000303|PubMed:25807229};
GN   ORFNames=SAMN04489800_2602 {ECO:0000312|EMBL:SEE88007.1};
OS   Pseudomonas deceptionensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=882211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 25555;
RA   Varghese N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-399, AND DISRUPTION PHENOTYPE.
RC   STRAIN=M1;
RX   PubMed=25807229; DOI=10.1038/ncomms7579;
RA   Carrion O., Curson A.R., Kumaresan D., Fu Y., Lang A.S., Mercade E.,
RA   Todd J.D.;
RT   "A novel pathway producing dimethylsulphide in bacteria is widespread in
RT   soil environments.";
RL   Nat. Commun. 6:6579-6579(2015).
CC   -!- FUNCTION: Catalyzes the alpha,gamma-elimination of L-methionine to
CC       produce methanethiol, 2-oxobutanoate and ammonia.
CC       {ECO:0000250|UniProtKB:P13254}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-methionine = 2-oxobutanoate + methanethiol + 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:0000250|UniProtKB:P13254};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P13254};
CC   -!- SUBUNIT: Homotetramer; dimer of active dimers.
CC       {ECO:0000250|UniProtKB:P13254}.
CC   -!- DISRUPTION PHENOTYPE: Mutant cannot make methanethiol (MeSH) or
CC       dimethylsulfide (DMS) from either minimal medium or medium supplemented
CC       with methionine. However, it can make DMS when exogenous MeSH is added.
CC       {ECO:0000269|PubMed:25807229}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. L-
CC       methionine gamma-lyase subfamily. {ECO:0000305}.
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DR   EMBL; FNUD01000002; SEE88007.1; -; Genomic_DNA.
DR   EMBL; KM030270; AJE75745.1; -; Genomic_DNA.
DR   RefSeq; WP_048358391.1; NZ_JYKX01000001.1.
DR   AlphaFoldDB; A0A0J6G7P5; -.
DR   SMR; A0A0J6G7P5; -.
DR   EnsemblBacteria; SEE88007; SEE88007; SAMN04489800_2602.
DR   PATRIC; fig|882211.3.peg.459; -.
DR   BioCyc; MetaCyc:MON-19897; -.
DR   Proteomes; UP000183613; Unassembled WGS sequence.
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   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   PANTHER; PTHR11808; PTHR11808; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01328; met_gam_lyase; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate.
FT   CHAIN           1..399
FT                   /note="L-methionine gamma-lyase"
FT                   /id="PRO_0000446295"
FT   BINDING         59..61
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P13254"
FT   BINDING         89..90
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P13254"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P13254"
FT   BINDING         209..211
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P13254"
FT   BINDING         376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P13254"
FT   MOD_RES         212
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P13254"
FT   CONFLICT        75..82
FT                   /note="AALENGEA -> RREGTAS (in Ref. 2; AJE75745)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   399 AA;  43025 MW;  A6503B4E5610AC77 CRC64;
     MNDKHKNFGF STRAIHYGYN ALENNGALIP PVYMTSTFAF PTVEYGAGCF AGEESGHFYT
     RISNPTLALL ESRMAALENG EAGVAFSSGM GAIAATFWTL LRPGDEIIVN RTLYGCTFAL
     LHHGIGEFGV VVKHVDMSNL AELEAAIGPA TRMIYFETPA NPNMQLVDIA AVSAIAHTHN
     DLIVVIDNTY CTPYLQRPLE LGADVVVHSA TKYLSGHSDI TAGVVVTRQS LADRIRLQGL
     KDLTGAVLSP HDAHLLMRGI KTLALRMDRH CSSAQVIAQM LQDHPAVEWV AYPGLPSFPQ
     YALASRQMKL PGGMIAFELK GGMAAGQRFM NALQLFSRAV SLGGAESLAQ HPASMTHSTY
     TLEERAKHGI SEGLVRLAVG LEDIADLLAD IEQAMKAMA