ID   A0A143X9U2_9ACTN        Unreviewed;       426 AA.
AC   A0A143X9U2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:CVH79430.1};
DE            EC=4.4.1.11 {ECO:0000313|EMBL:CVH79430.1};
GN   Name=mdeA {ECO:0000313|EMBL:CVH79430.1};
GN   ORFNames=BN3658_01976 {ECO:0000313|EMBL:CVH79430.1};
OS   Coriobacteriaceae bacterium CHKCI002.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae.
OX   NCBI_TaxID=1780377 {ECO:0000313|EMBL:CVH79430.1, ECO:0000313|Proteomes:UP000199067};
RN   [1] {ECO:0000313|Proteomes:UP000199067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Millard A.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; FCNB01000191; CVH79430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A143X9U2; -.
DR   STRING; 1780377.BN3658_01976; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000199067; Unassembled WGS sequence.
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:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; 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; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR   PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR   PANTHER; PTHR43797:SF3; O-ACETYLHOMOSERINE SULFHYDRYLASE; 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:CVH79430.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199067}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         206
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   426 AA;  45374 MW;  C84BF44758AFB07A CRC64;
     MSESIGTTCV QGGYRPGDGE PRQLPIYQST TWKFDTSEHM GRLFDLEEAG YFYTRLQNPT
     NDAVAAKIAE LEGGTAAMLT SSGQAANFFA VFNIAGAGDH VVASSAIYGG TYNLLAHTMR
     RMGLECTFVA PDCTDEELAA AFRPNTKAVF GETIANPALS VLDIKRFAAA AHTHGVPLIV
     DNTFPTPVNC RPIEWGADIV THSTTKYLDG HGVSVGGAIV DSGRFDWTAH ADKFPGLTTP
     DESYHGVVYT ERFGLEGAFI TKATAQLMRD FGAIQSPQNA FYVNLGLESL HLRMAQHNKN
     GLAMAEHLAA HPKVAWVRYP GLPGDAQHEL ARKYLPAGAS GVVSFGVAGG RAAAETFMAN
     LKLAQIATHV ADARTCVLHP ANATHRQMND AELAAAGITP DLVRLSCGIE ATEDLIADVD
     QALAAV
//