ID   E3HX90_ACHXA            Unreviewed;       396 AA.
AC   E3HX90;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Methionine gamma-lyase 2 {ECO:0000313|EMBL:ADP17612.1};
DE            EC=4.4.1.11 {ECO:0000313|EMBL:ADP17612.1};
GN   Name=megL2 {ECO:0000313|EMBL:ADP17612.1};
GN   OrderedLocusNames=AXYL_04293 {ECO:0000313|EMBL:ADP17612.1};
OS   Achromobacter xylosoxidans (strain A8).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP17612.1, ECO:0000313|Proteomes:UP000006876};
RN   [1] {ECO:0000313|EMBL:ADP17612.1, ECO:0000313|Proteomes:UP000006876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A8 {ECO:0000313|EMBL:ADP17612.1,
RC   ECO:0000313|Proteomes:UP000006876};
RX   PubMed=21097610; DOI=10.1128/JB.01299-10;
RA   Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT   "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT   Achromobacter xylosoxidans A8.";
RL   J. Bacteriol. 193:791-792(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; CP002287; ADP17612.1; -; Genomic_DNA.
DR   RefSeq; WP_013394920.1; NC_014640.1.
DR   AlphaFoldDB; E3HX90; -.
DR   STRING; 762376.AXYL_04293; -.
DR   KEGG; axy:AXYL_04293; -.
DR   PATRIC; fig|762376.5.peg.4300; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_0_4; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000006876; Chromosome.
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:SF90; CYSTATHIONINE 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:ADP17612.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   396 AA;  42447 MW;  452F103DBC1EB162 CRC64;
     MTESTQHGFA TRAIHLGYDP LDEQGALAPP LYLTSTYTQD SIEAFDQIRL GEKQGYVYGR
     TRNPTQALLE ERLASLEGAE AGVVTASGMA AISATLFSLL QSGDEIVVDQ IVYGTAFTLF
     TQGLARFGVR AVFADFTRPE TVAAALGPKT RAVYFETPAN PNLRLVDIAA VSAIARGKGV
     LTIVDNTFAT PVLQRPLEHG ADIVLHSATK YLGGHGDLLA GAVLGRKEHI DAIRLQGLRY
     FTGATLSPFT AFLVLRGIKT LELRVARHSE SALRVAKLLR EHAAVADVFY PGLADTAGAE
     IARRQQSAGG GLVAFELKGG LTAGRKLLNS LKLARIAVSL GDPETLIQHP ASMTHASYTA
     EDRERYGLSE GLLRLSVGLE TPEDILSDLR QGLDRL
//