MEGL_STRAW
ID MEGL_STRAW Reviewed; 413 AA.
AC Q826W3;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=L-methionine gamma-lyase {ECO:0000303|PubMed:25817696};
DE Short=MGL {ECO:0000303|PubMed:25817696};
DE EC=4.4.1.11 {ECO:0000269|PubMed:25817696};
DE AltName: Full=Homocysteine desulfhydrase {ECO:0000305|PubMed:25817696};
DE EC=4.4.1.2 {ECO:0000269|PubMed:25817696};
GN Name=mgl {ECO:0000312|EMBL:BAC74773.1};
GN ORFNames=SAVERM_7062 {ECO:0000312|EMBL:BAC74773.1};
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680 {ECO:0000312|Proteomes:UP000000428};
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680 {ECO:0000312|Proteomes:UP000000428};
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=25817696; DOI=10.1016/j.jbiosc.2015.02.019;
RA Kudou D., Yasuda E., Hirai Y., Tamura T., Inagaki K.;
RT "Molecular cloning and characterization of L-methionine gamma-lyase from
RT Streptomyces avermitilis.";
RL J. Biosci. Bioeng. 120:380-383(2015).
CC -!- FUNCTION: Catalyzes the alpha,gamma-elimination of L-methionine to
CC produce methanethiol, 2-oxobutanoate and ammonia. Is probably involved
CC in L-methionine catabolism. Is also able to catalyze the alpha,gamma-
CC elimination of L-homocysteine, and, to a lesser extent, the alpha,beta-
CC elimination of L-cysteine. {ECO:0000269|PubMed:25817696}.
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:25817696};
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:25817696};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteine = H(+) + hydrogen sulfide + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:24931, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:35235; Evidence={ECO:0000269|PubMed:25817696};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305|PubMed:25817696};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.60 mM for L-methionine {ECO:0000269|PubMed:25817696};
CC KM=1.78 mM for L-homocysteine {ECO:0000269|PubMed:25817696};
CC KM=0.20 mM for L-cysteine {ECO:0000269|PubMed:25817696};
CC Note=kcat is 2.90 sec(-1) for the alpha,gamma-elimination of L-
CC methionine. kcat is 1.67 sec(-1) for the alpha,gamma-elimination of
CC L-homocysteine. kcat is 0.03 sec(-1) for the alpha,beta-elimination
CC of L-cysteine. {ECO:0000269|PubMed:25817696};
CC -!- SUBUNIT: Homotetramer; dimer of active dimers.
CC {ECO:0000250|UniProtKB:P13254}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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; BA000030; BAC74773.1; -; Genomic_DNA.
DR RefSeq; WP_010988457.1; NZ_JZJK01000085.1.
DR AlphaFoldDB; Q826W3; -.
DR SMR; Q826W3; -.
DR STRING; 227882.SAV_7062; -.
DR EnsemblBacteria; BAC74773; BAC74773; SAVERM_7062.
DR KEGG; sma:SAVERM_7062; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_11; -.
DR OMA; EVTWTDP; -.
DR OrthoDB; 637281at2; -.
DR BRENDA; 4.4.1.11; 5980.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0047982; F:homocysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:RHEA.
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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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; 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.
PE 1: Evidence at protein level;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..413
FT /note="L-methionine gamma-lyase"
FT /id="PRO_0000443073"
FT REGION 388..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75..77
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 105..106
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 131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT BINDING 218..220
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 365
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P13254"
FT MOD_RES 221
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P13254"
SQ SEQUENCE 413 AA; 43027 MW; D754E4828D4E7A1E CRC64;
MDDGRGAGGF GGGPAVRALD TEAVHAGRDD LARQGLHAAP IDLSTTYPSY DSRAEAARID
AFAADGAEPA GPPVYGRLGN PTVARFETAL ARLEGTDSAV AFASGMAALS AVLLVRNAMG
LRHVVAVRPL YGCSDHLLTA GLLGSEVTWV DPAGVADALR PDTGLVMVES PANPTLAELD
LRALAHACGS VPLLADNTFA TPVLQRPAEH GARLVLHSAT KYLGGHGDVM AGVVACDEEF
ARGLRQIRFA TGGVLHPLAG YLLLRGLSTL PIRVRAASSN AAELARRLAA DPRVARVHYP
RIGGAMIAFE VYGDPHEVIA GVRLITPAVS LGSVDSLIQH PASISHRIVD AADRRGAGVS
DRLLRLSVGL EDVEDLWADL DGALGTDRLP ETAGAGREPS RTALRLPERA ADR
