MEGL_TREDE
ID MEGL_TREDE Reviewed; 401 AA.
AC Q73KL7;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=L-methionine gamma-lyase {ECO:0000305|PubMed:15845368};
DE Short=MGL {ECO:0000305};
DE EC=4.4.1.11 {ECO:0000269|PubMed:15845368};
DE AltName: Full=Homocysteine desulfhydrase {ECO:0000305|PubMed:15845368};
DE EC=4.4.1.2 {ECO:0000269|PubMed:15845368};
DE AltName: Full=L-methionine-alpha-deamino-gamma-mercaptomethane-lyase {ECO:0000303|PubMed:15845368};
DE Short=METase {ECO:0000303|PubMed:15845368};
GN Name=megL {ECO:0000303|PubMed:15845368, ECO:0000312|EMBL:AAS12720.1};
GN OrderedLocusNames=TDE_2200 {ECO:0000312|EMBL:AAS12720.1};
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=15845368; DOI=10.1016/j.bbrc.2005.03.139;
RA Fukamachi H., Nakano Y., Okano S., Shibata Y., Abiko Y., Yamashita Y.;
RT "High production of methyl mercaptan by L-methionine-alpha-deamino-gamma-
RT mercaptomethane lyase from Treponema denticola.";
RL Biochem. Biophys. Res. Commun. 331:127-131(2005).
CC -!- FUNCTION: Catalyzes the alpha,gamma-elimination of L-methionine to
CC produce methanethiol, 2-oxobutanoate and ammonia; methanethiol (methyl
CC mercaptan) is considered to be one of the main causes of the oral
CC malodor associated with periodontitis and may also play a role in the
CC pathogenicity of T.denticola. Also displays homocysteine desulfhydrase
CC activity, degrading homocysteine to produce hydrogen sulfide, 2-
CC oxobutanoate and ammonia. {ECO:0000269|PubMed:15845368}.
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:0000269|PubMed:15845368};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-homocysteine = 2-oxobutanoate + H(+) + hydrogen
CC sulfide + NH4(+); Xref=Rhea:RHEA:14501, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:58199; EC=4.4.1.2;
CC Evidence={ECO:0000269|PubMed:15845368};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P13254, ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.55 mM for L-methionine {ECO:0000269|PubMed:15845368};
CC Vmax=36.6 umol/min/mg enzyme with L-methionine as substrate
CC {ECO:0000269|PubMed:15845368};
CC -!- SUBUNIT: Homotetramer; dimer of active dimers.
CC {ECO:0000250|UniProtKB:P13254}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. L-
CC methionine gamma-lyase subfamily. {ECO:0000305}.
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DR EMBL; AE017226; AAS12720.1; -; Genomic_DNA.
DR RefSeq; NP_972801.1; NC_002967.9.
DR RefSeq; WP_002674490.1; NC_002967.9.
DR AlphaFoldDB; Q73KL7; -.
DR SMR; Q73KL7; -.
DR STRING; 243275.TDE_2200; -.
DR PRIDE; Q73KL7; -.
DR EnsemblBacteria; AAS12720; AAS12720; TDE_2200.
DR GeneID; 2739476; -.
DR KEGG; tde:TDE_2200; -.
DR PATRIC; fig|243275.7.peg.2076; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_3_12; -.
DR OMA; YGGMITF; -.
DR OrthoDB; 637281at2; -.
DR BRENDA; 4.4.1.11; 6426.
DR SABIO-RK; Q73KL7; -.
DR Proteomes; UP000008212; Chromosome.
DR GO; GO:0047982; F:homocysteine desulfhydrase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..401
FT /note="L-methionine gamma-lyase"
FT /id="PRO_0000436015"
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 210..212
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 377
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT MOD_RES 213
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P13254"
SQ SEQUENCE 401 AA; 43488 MW; 4E0CF48F2603283E CRC64;
MNRKELEKLG FASKQIHAGS IKNKYGALAT PIYQTSTFAF DSAEQGGRRF ALEEEGYIYT
RLGNPTTTVV EEKLACLENG EACMSASSGI GAVTSCIWSI VNAGDHIVAG KTLYGCTFAF
LNHGLSRFGV DVTFVDTRDP ENVKKALKPN TKIVYLETPA NPNMYLCDIA AVSKIAHAHN
PECKVIVDNT YMTPYLQRPL DLGADVVLHS ATKYLNGHGD VIAGFVVGKK EFIDQVRFVG
VKDMTGSTLG PFEAYLIGRG MKTLDIRMEK HCANAQKVAE FLEKHPAVES IAFPGLKSFP
QYELAKKQMK LCGAMIAFTV KGGLEAGKTL INSVKFATIA VSLGDAETLI QHPASMTHSP
YTPEERAASD IAEGLVRLSV GLEDAEDIIA DLKQALDKLV K
