ID A0A109LQW5_9SPHN Unreviewed; 442 AA.
AC A0A109LQW5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:KWV91996.1};
GN ORFNames=AUC45_12635 {ECO:0000313|EMBL:KWV91996.1};
OS Erythrobacter sp. YT30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1735012 {ECO:0000313|EMBL:KWV91996.1, ECO:0000313|Proteomes:UP000055668};
RN [1] {ECO:0000313|EMBL:KWV91996.1, ECO:0000313|Proteomes:UP000055668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YT30 {ECO:0000313|EMBL:KWV91996.1,
RC ECO:0000313|Proteomes:UP000055668};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Erythrobacter sp. YT30.";
RL Submitted (OCT-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:KWV91996.1}.
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DR EMBL; LMAF01000002; KWV91996.1; -; Genomic_DNA.
DR RefSeq; WP_067603154.1; NZ_LMAF01000002.1.
DR AlphaFoldDB; A0A109LQW5; -.
DR STRING; 1735012.AUC45_12635; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000055668; 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:SF86; METHIONINE 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:KWV91996.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000055668}.
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 257
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 442 AA; 47769 MW; 8A2F70B8E1851AF1 CRC64;
MTDLPVDQNA APIEPTPRRK PKPERTEIGG RPLKPSTLMM GHGFDPVLSE GSLKAPIFLT
STFAFPSAAD GKRHFEGITG KREGGADGLV YSRFNGPNQE ILEDRLAIWD GAEDALTFSS
GMTAICVLMM AYVSQGDVIV HSGPLYAASE GFVSKVLSKF GVTYIDFPAG ASREELDDVL
KRAKCQAGEN GGKVAMIYLE SPANPTNALV DIEAVKEARD ANLKWDCPIA IDNTFLGPLW
QRPLDHGADI VAYSLTKYVG GHSDLVAGSI AGAKKWMDPV RALRNTMGGI VDPNTAWMLL
RSLETVELRM QRAGENAEKV CECLKAHPKV TGLGYLGHIK DARQQYIFDR HCKGAGSTFS
VFLKGGETEC FRFLDHLTIA KLAVSLGGTE TLASHPASMT HLSVPDERKA ALGITDSLVR
ISIGIEDADD LIADFEQALE HV
//
