ID   A0A239LT44_9RHOB        Unreviewed;       402 AA.
AC   A0A239LT44;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Methionine-gamma-lyase {ECO:0000313|EMBL:SNT33847.1};
GN   ORFNames=SAMN05421757_11150 {ECO:0000313|EMBL:SNT33847.1};
OS   Tropicimonas sediminicola.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tropicimonas.
OX   NCBI_TaxID=1031541 {ECO:0000313|EMBL:SNT33847.1, ECO:0000313|Proteomes:UP000198426};
RN   [1] {ECO:0000313|EMBL:SNT33847.1, ECO:0000313|Proteomes:UP000198426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29339 {ECO:0000313|EMBL:SNT33847.1,
RC   ECO:0000313|Proteomes:UP000198426};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZOY01000011; SNT33847.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239LT44; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000198426; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 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:SNT33847.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198426}.
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         211
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   402 AA;  42555 MW;  A3D5648A5CC27061 CRC64;
     MTDRKNSRGP MTLAIHAGEG PDPSTGASAP PLHMSSTFVT DQVAGFSAHD LEDASGYLYT
     RWGNPTVDML ERKIAALEGT DACLCTASGM AAASAIFLTF LSSGDHVVVS DVSYAGVAEL
     ARDTLPRLGI EVSLVDMSDI EAVAAALRDN TRLVHCETPV NPIGRLTDLS AVTRLAHDAG
     ALVSCDATFA SPLGQESAGL GVDLVMHSIT KYIGGHGDAV GGAVAGSAEL IGRMRLEASI
     HHGGILSPFN AWLIARGMAT LPLRMKAHEA GALELANWLE SRDSVTRVIH PGLASHPQRA
     LAERQMTNTA GMISFQVGDA AKGQALAQQM IDRLEVIHYA VSLGHHRSLI FWMETAPLME
     TSFRLQGRQL ESYRAFAGDG VFRLSVGLED PADLIADLAQ VL
//