ID A0A0M2P9H8_9BACI Unreviewed; 396 AA.
AC A0A0M2P9H8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=L-methionine gamma-lyase {ECO:0000256|ARBA:ARBA00019040};
DE EC=4.4.1.11 {ECO:0000256|ARBA:ARBA00012222};
GN ORFNames=WQ54_28400 {ECO:0000313|EMBL:KKI89139.1};
OS Bacillus sp. SA1-12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI89139.1, ECO:0000313|Proteomes:UP000034887};
RN [1] {ECO:0000313|EMBL:KKI89139.1, ECO:0000313|Proteomes:UP000034887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1-12 {ECO:0000313|EMBL:KKI89139.1,
RC ECO:0000313|Proteomes:UP000034887};
RA Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-methionine = 2-oxobutanoate + methanethiol + NH4(+);
CC Xref=Rhea:RHEA:23800, ChEBI:CHEBI:15377, ChEBI:CHEBI:16007,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; EC=4.4.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000271};
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. L-
CC methionine gamma-lyase subfamily. {ECO:0000256|ARBA:ARBA00008667}.
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:KKI89139.1}.
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DR EMBL; LATZ01000131; KKI89139.1; -; Genomic_DNA.
DR RefSeq; WP_046589700.1; NZ_LATZ01000131.1.
DR AlphaFoldDB; A0A0M2P9H8; -.
DR PATRIC; fig|1455638.3.peg.6295; -.
DR OrthoDB; 9803887at2; -.
DR Proteomes; UP000034887; 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: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; IPR006237; L-Met_gamma_lys.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01328; met_gam_lyase; 1.
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:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KKI89139.1};
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; 43593 MW; AC93E8CD9A4E5DE9 CRC64;
MKKESKAHFE TIAIHAGYSP KNYHDSLTPP IYQTSTFTFS TMEQGASRFA GIEDGYIYSR
LSNPTVEVLE ERMAVLEEGE AALAFGSGMA AVSAALIGLT KKNDHILCSK GVYGCTYGLL
QLLKEKYQID YSFSELSTVD EIISNIQENT ACIFLETPIN PTMKLIDLAL VAKIAKEKGV
KVVVDNTFLT PYLQKPLTLG CDLVVHSGTK YIGGHGDVIA GIIVGGQETI QYLKRTIQKD
IGGIISPFDA WLLLRGIKTL AVRMDRHCEN AEKLHSCLKG HSKIKAVYYP GDKDHPDYKI
MNRQMKKGGG VLSFELEGTY EDALKAVNAL KLIPIAVSLG DAETLIQHPA SMTHAVVPEE
ARQKMGISNQ LLRLSVGLEA WEDIWEDLKQ ALDTLL
//
