ID A0A0F0KRG1_9MICO Unreviewed; 434 AA.
AC A0A0F0KRG1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:KJL22685.1};
DE EC=4.4.1.11 {ECO:0000313|EMBL:KJL22685.1};
GN Name=mdeA_2 {ECO:0000313|EMBL:KJL22685.1};
GN ORFNames=RN50_01364 {ECO:0000313|EMBL:KJL22685.1};
OS Microbacterium foliorum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=104336 {ECO:0000313|EMBL:KJL22685.1, ECO:0000313|Proteomes:UP000033572};
RN [1] {ECO:0000313|EMBL:KJL22685.1, ECO:0000313|Proteomes:UP000033572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12966 {ECO:0000313|EMBL:KJL22685.1,
RC ECO:0000313|Proteomes:UP000033572};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJL22685.1}.
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DR EMBL; JYIU01000038; KJL22685.1; -; Genomic_DNA.
DR RefSeq; WP_045253762.1; NZ_JYIU01000038.1.
DR AlphaFoldDB; A0A0F0KRG1; -.
DR KEGG; mfol:DXT68_10335; -.
DR PATRIC; fig|104336.4.peg.1400; -.
DR Proteomes; UP000033572; 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:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KJL22685.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000033572}.
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 434 AA; 45931 MW; 32D3AB2201D41C15 CRC64;
MTQEHRFGFR TRALHAGGTP DAATGARAVP IYQTTSFVFE DATDAGNLFA LQKYGNIYSR
IGNPTVAALE ERLASLEGGI GAVATASGMS AEFITFAALV GAGDHVVASA QLYGGTVTQL
DVTLRRFGVE TTFVASTDPD DYAAAIRPET KVVYVEMIGN PSGEIADIEG LAEVAHAAGV
PLVVDATLAT PYLARPLEHG ADIVIHSVTK FLGGHGTTLG GVVIEKGTFD WGNGRFPQMT
EPVESYGGIA WWGNFGEYGF LTKLRTEQLR DIGPALSPQS AFNLLQGVET LPQRIDAHLA
NARVVADWLA SDPRVAYVTW AGLEGHPHHA RAAKYLPLGP GSVFAFGVKA EDGRAAGETL
IENLQLASHL ANIGDARTLV IHPASTTHRQ LSESQLVAAG VRPDLIRISV GLEDADDIIW
DLDQALSTAT GANR
//
