ID A0A0Q5ZK65_9BURK Unreviewed; 394 AA.
AC A0A0Q5ZK65;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:KQT13199.1};
DE EC=4.4.1.11 {ECO:0000313|EMBL:KQT13199.1};
GN ORFNames=ASG30_20740 {ECO:0000313|EMBL:KQT13199.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT13199.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT13199.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT13199.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT13199.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT13199.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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|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:KQT13199.1}.
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DR EMBL; LMQL01000005; KQT13199.1; -; Genomic_DNA.
DR RefSeq; WP_055893754.1; NZ_LMQL01000005.1.
DR AlphaFoldDB; A0A0Q5ZK65; -.
DR STRING; 1736365.ASG30_20740; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000051173; 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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:0000313|EMBL:KQT13199.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000051173}.
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 394 AA; 42464 MW; 969B6C7AD0823163 CRC64;
MNPSTSQAFE TTVVHAGEDP ERHMGSLSTP IYQTALHVFP NAEDGHLIHE GHKPGYFYGR
MGNPTQAALE QAMCEVEGGE AALALASGMA AISNAILSIV EPGDHIVAPA SLYATTGALL
DGLLPKLGVK VSYVDATHAA NYQEAVTPKT KLFYLESPAN PTMKMVDIEA VVSVARSKSI
TTVMDNTFAT PYNQRPLDLG VDVVVHSATK YLGGHGDLTA GVIVGRKDVV DRAHWQTNKV
LGGVIAPWTA WLVIRGLRTL ALRMERHNSN ALKLARFLAN HPKVREVHYP GLETHPQHVL
ARRQMKGFGG MLSFDVGGVD EGRRLVDNVK LCSLAVSLGD VSTLIQHSAS MTHAIVPRER
RLAVGITDGL LRLSVGIEDP DDLVADLRQA LQHV
//
