ID   E5B877_ERWAM            Unreviewed;       426 AA.
AC   E5B877;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   28-JUN-2023, entry version 33.
DE   SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:CBX81682.1};
DE            EC=4.4.1.11 {ECO:0000313|EMBL:CBX81682.1};
GN   Name=mdeA3 {ECO:0000313|EMBL:CBX81682.1};
GN   ORFNames=EAIL5_2862 {ECO:0000313|EMBL:CBX81682.1};
OS   Erwinia amylovora ATCC BAA-2158.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=889211 {ECO:0000313|EMBL:CBX81682.1};
RN   [1] {ECO:0000313|EMBL:CBX81682.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC BAA-2158 {ECO:0000313|EMBL:CBX81682.1};
RA   Powney R., Smits T.H., Sawbridge T., Frey B., Blom J., Frey J.E.,
RA   Plummer K.M., Beer S.V., Luck J., Duffy B., Rodoni B.;
RT   "Genome Sequence of an Erwinia amylovora Strain with Pathogenicity
RT   Restricted to Rubus Plants.";
RL   J. Bacteriol. 193:785-786(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; FR719195; CBX81682.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5B877; -.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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:SF86; METHIONINE GAMMA-LYASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:CBX81682.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         241
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   426 AA;  45864 MW;  83504319CE922B9F CRC64;
     MLSSHSKKTH IGQRELQPET QMLNYGYDPA LSEGAVKPPV FLTSTFIFNS AEEGRDFFDY
     VSGRREPPAG EGNGLVYSRF NHPNSEIVED RLAIYERSES AALFSSGMSA IATTLLTFVR
     PGDAILHSQP LYGGSETLLS KTFGNLGVAA IGFADGIDEA LVQAAADKAL AQGRVSAILI
     ESPANPTNSL VDIALIKRVA DRIEQQQQHR PVIACDNTLL GPVFSRPLEH GADISLYSLT
     KYVGGHSDLI AGAAMGNRAL IRQVKALRSA IGTQLDAHSS WMIGRSLETL ALRMDRANDN
     AAAVAEFLRS HSLVEQIHYL PFIDPHSAAG KVYSDQCSGA GSTFSFDIRG GQDAAFRFLN
     GLQLFKLAVS LGGTESLASH PASTTHSGVD LAVRERMGIK ASTLRLSIGI ENKDDLIEDL
     RLALDR
//