MEGL_PORGI
ID MEGL_PORGI Reviewed; 399 AA.
AC Q7MX71;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=L-methionine gamma-lyase {ECO:0000305|PubMed:11083813};
DE Short=MGL {ECO:0000305};
DE EC=4.4.1.11 {ECO:0000269|PubMed:11083813};
DE AltName: Full=Homocysteine desulfhydrase {ECO:0000250|UniProtKB:Q73KL7};
DE EC=4.4.1.2 {ECO:0000250|UniProtKB:Q73KL7};
DE AltName: Full=L-methionine-alpha-deamino-gamma-mercaptomethane-lyase {ECO:0000303|PubMed:11083813};
DE Short=METase {ECO:0000303|PubMed:11083813};
GN Name=mgl {ECO:0000303|PubMed:11083813};
GN Synonyms=megL {ECO:0000312|EMBL:AAQ65554.1};
GN OrderedLocusNames=PG_0343 {ECO:0000312|EMBL:AAQ65554.1};
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=11083813; DOI=10.1128/iai.68.12.6912-6916.2000;
RA Yoshimura M., Nakano Y., Yamashita Y., Oho T., Saito T., Koga T.;
RT "Formation of methyl mercaptan from L-methionine by Porphyromonas
RT gingivalis.";
RL Infect. Immun. 68:6912-6916(2000).
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 in periodontal disease and may also play a role in the
CC pathogenicity of P.gingivalis in that disease (PubMed:11083813). Is
CC also able to catalyze the alpha,gamma-elimination of L-homocysteine (By
CC similarity). {ECO:0000250|UniProtKB:Q73KL7,
CC ECO:0000269|PubMed:11083813}.
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:11083813};
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:0000250|UniProtKB:Q73KL7};
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=23.1 mM for L-methionine {ECO:0000269|PubMed:11083813};
CC Vmax=21.9 umol/min/mg enzyme {ECO:0000269|PubMed:11083813};
CC -!- SUBUNIT: Homotetramer; dimer of active dimers.
CC {ECO:0000250|UniProtKB:P13254}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a marked decrease in
CC the formation of methyl mercaptan from L-methionine and decreased
CC virulence compared with the wild-type strain W83. The hydrogen sulfide
CC content in the culture supernatants of mutant and wild-type strains is
CC similar. {ECO:0000269|PubMed:11083813}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. L-
CC methionine gamma-lyase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ65554.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE015924; AAQ65554.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_005873786.1; NC_002950.2.
DR AlphaFoldDB; Q7MX71; -.
DR SMR; Q7MX71; -.
DR STRING; 242619.PG_0343; -.
DR EnsemblBacteria; AAQ65554; AAQ65554; PG_0343.
DR GeneID; 29256789; -.
DR KEGG; pgi:PG_0343; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_3_10; -.
DR OrthoDB; 637281at2; -.
DR BRENDA; 4.4.1.11; 756.
DR SABIO-RK; Q7MX71; -.
DR PHI-base; PHI:7938; -.
DR Proteomes; UP000000588; 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; Virulence.
FT CHAIN 1..399
FT /note="L-methionine gamma-lyase"
FT /id="PRO_0000436014"
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"
SQ SEQUENCE 399 AA; 43262 MW; F9D5C79336B85F31 CRC64;
MKKEDLMRSG FATRAIHGGA IENAFGCLAT PIYQTSTFVF DTAEQGGRRF AGEEDGYIYT
RLGNPNCTQV EEKLAMLEGG EAAASASSGI GAISSAIWVC VKAGDHIVAG KTLYGCTFAF
LTHGLSRYGV EVTLVDTRHP EEVEAAIRPN TKLVYLETPA NPNMYLTDIK AVCDIAHKHE
GVRVMVDNTY CTPYICRPLE LGADIVVHSA TKYLNGHGDV IAGFVVGKED YIKEVKLVGV
KDLTGANMSP FDAYLISRGM KTLQIRMEQH CRNAQTVAEF LEKHPAVEAV YFPGLPSFPQ
YELAKKQMAL PGAMIAFEVK GGCEAGKKLM NNLHLCSLAV SLGDTETLIQ HPASMTHSPY
TPEERAASDI SEGLVRLSVG LENVEDIIAD LKHGLDSLI
