MEGL_FUSNP
ID MEGL_FUSNP Reviewed; 395 AA.
AC Q8L0X4;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=L-methionine gamma-lyase {ECO:0000305|PubMed:12123816};
DE Short=MGL {ECO:0000305};
DE EC=4.4.1.11 {ECO:0000269|PubMed:12123816};
DE AltName: Full=Homocysteine desulfhydrase {ECO:0000305|PubMed:12123816};
DE EC=4.4.1.2 {ECO:0000269|PubMed:12123816};
DE AltName: Full=L-methionine-alpha-deamino-gamma-mercaptomethane-lyase {ECO:0000303|PubMed:12123816};
DE Short=METase {ECO:0000303|PubMed:12123816};
GN Name=mgl {ECO:0000303|PubMed:12123816};
OS Fusobacterium nucleatum subsp. polymorphum.
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=76857;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND ANTIBIOTIC RESISTANCE.
RC STRAIN=ATCC 10953 / DSM 20482 / CCUG 9126 / JCM 12990 / NCTC 10562 / 555A;
RX PubMed=12123816; DOI=10.1016/s0014-5793(02)02958-7;
RA Yoshimura M., Nakano Y., Fukamachi H., Koga T.;
RT "3-Chloro-DL-alanine resistance by L-methionine-alpha-deamino-gamma-
RT mercaptomethane-lyase activity.";
RL FEBS Lett. 523:119-122(2002).
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. Also displays homocysteine
CC desulfhydrase activity, degrading homocysteine to produce hydrogen
CC sulfide, 2-oxobutanoate and ammonia. L-cysteine and S-methyl-L-cysteine
CC are poor substrates for the enzyme. {ECO:0000269|PubMed:12123816}.
CC -!- FUNCTION: Plays an important role in the resistance of F.nucleatum to
CC the antibacterial agent 3-chloro-DL-alanine (3CA), thanks to its 3CA
CC chloride-lyase (deaminating) activity. {ECO:0000269|PubMed:12123816}.
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:12123816};
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:12123816};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P13254, ECO:0000305};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q8RDT4}.
CC -!- MISCELLANEOUS: F.nucleatum strain ATCC 10953 is able to grow in medium
CC containing 1 mM 3CA. {ECO:0000269|PubMed:12123816}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. L-
CC methionine gamma-lyase subfamily. {ECO:0000305}.
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DR EMBL; AB077041; BAC02724.1; -; Genomic_DNA.
DR RefSeq; WP_005898783.1; NZ_LN831027.1.
DR AlphaFoldDB; Q8L0X4; -.
DR SMR; Q8L0X4; -.
DR STRING; 76857.RO02_12380; -.
DR PRIDE; Q8L0X4; -.
DR GeneID; 45635777; -.
DR PATRIC; fig|76857.9.peg.1983; -.
DR OrthoDB; 637281at2; -.
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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Direct protein sequencing; Lyase;
KW Pyridoxal phosphate.
FT CHAIN 1..395
FT /note="L-methionine gamma-lyase"
FT /id="PRO_0000436013"
FT BINDING 56..58
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 86..87
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 111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT BINDING 206..208
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 373
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P13254"
SQ SEQUENCE 395 AA; 43288 MW; CAE0A78C2A58EBB2 CRC64;
METKKYGLGT TAIHAGTLKN LYGTLAMPIY QTSTFIFDSA EQGGRRFALE EAGYIYTRLG
NPTTTVLENK IAALEEGEAA VATSSGMGAI SSTLWTVLKA GDHVVTDKTL YGCTFALMCH
GLTRFGIEVT FVDTSNLDEV KNAMKKNTRV VYLETPANPN LKIVDLEALS KLAHTNPNTL
VIVDNTFATP YMQKPLKLGA DIVVHSVTKY INGHGDVIAG LVITNKELAD QIRFIGLKDM
TGAVLGPQDA YYIIRGMKTF EIRMERHCKN AKKVVEFLNK HPKIERVYYP GLETHPGHEI
AKKQMKDFGA MISFELKGGF EAGKTLLNNL KLCSLAVSLG DTETLIQHPA SMTHSPYTKE
EREAAGITDG LVRLSVGLEN VEDIIADLEQ GLEKI
