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}.
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; 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
//