ID A0A117V4G4_9SPHN Unreviewed; 419 AA.
AC A0A117V4G4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Methionine gamma-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AQZ50_03285 {ECO:0000313|EMBL:KUR79908.1};
OS Novosphingobium sp. Fuku2-ISO-50.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1739114 {ECO:0000313|EMBL:KUR79908.1, ECO:0000313|Proteomes:UP000056630};
RN [1] {ECO:0000313|EMBL:KUR79908.1, ECO:0000313|Proteomes:UP000056630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fuku2-ISO-50 {ECO:0000313|EMBL:KUR79908.1,
RC ECO:0000313|Proteomes:UP000056630};
RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA Glaeser S.;
RT "Draft genome sequence of Novosphingobium sp. Fuku2-ISO-50 (=DSM 27930), a
RT Novosphingobium acidiphilum related species isolated from a surface water
RT sample of the southwest basin of Lake Grosse Fuchskuhle.";
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:KUR79908.1}.
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DR EMBL; LLZR01000004; KUR79908.1; -; Genomic_DNA.
DR RefSeq; WP_067742642.1; NZ_KQ954286.1.
DR AlphaFoldDB; A0A117V4G4; -.
DR STRING; 1739114.AQZ50_03285; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000056630; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000056630}.
FT MOD_RES 233
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 419 AA; 44201 MW; 6F88A5CA7D87B09A CRC64;
MPHEPGATFH PETLAIMAGY DPASASGAAK PPVYLTSTFV YESAEQARAI HEAYFRGTGP
MAGQPAYIYA RLSHPNLAML ETRLAAIDGA QSAAVFASGM AAHSAIALTH LRPGDSVLHS
RPIYGGTEAL YNQMMPHFGV HAVPIGDGCD GDHIRAQAEL ALAQGPLALI VIETPANPTA
ALTDIALVVA IADEIGARIG RRPLVVCDNT FLAPFAQRPV ELGVDLTMTS LTKYCGGHSD
LLAGGVSGRA EVIAPLLQWR TMLGSHCDPF TCWLVLRSLE SVAVRSERAM SNAALVAAFL
RDHGKVAGVT FLGFLPEGTP QRMVYDRQCK GAGSTFSFHL HGGEAEAFRL LDGLRLVKQA
VSLGGSETLA CHSATTTHYN VPAEARAAGG ITEGTIRLSV GIEHPDDLIA DFAQALEHV
//