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Database: UniProt
Entry: A0A245ZIV6_9SPHN
LinkDB: A0A245ZIV6_9SPHN
Original site: A0A245ZIV6_9SPHN 
ID   A0A245ZIV6_9SPHN        Unreviewed;       440 AA.
AC   A0A245ZIV6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:OWK29657.1};
DE            EC=4.4.1.11 {ECO:0000313|EMBL:OWK29657.1};
GN   Name=mdeA {ECO:0000313|EMBL:OWK29657.1};
GN   ORFNames=SPMU_20770 {ECO:0000313|EMBL:OWK29657.1};
OS   Sphingomonas mucosissima.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=370959 {ECO:0000313|EMBL:OWK29657.1, ECO:0000313|Proteomes:UP000197783};
RN   [1] {ECO:0000313|EMBL:OWK29657.1, ECO:0000313|Proteomes:UP000197783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17494 {ECO:0000313|EMBL:OWK29657.1,
RC   ECO:0000313|Proteomes:UP000197783};
RA   Poehlein A., Wuebbeler J.H., Steinbuechel A., Daniel R.;
RT   "Genome sequence of Sphingomonas mucosissima DSM 17494.";
RL   Submitted (MAR-2017) 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:OWK29657.1}.
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DR   EMBL; NBBJ01000003; OWK29657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A245ZIV6; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000197783; 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: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   Lyase {ECO:0000313|EMBL:OWK29657.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         250
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   440 AA;  46597 MW;  FD4F79F30F9E25C3 CRC64;
     MTKETEADLT GVEARVSPKP AVDEIGGRKL KPATLMMGHG YDPALSEGAL KPPIFLTSTF
     VFPNAAAGKR HFEGVTGKRP GGAEGLVYSR FNGPNQEILE DRLSIWEDAE DALAFSSGMS
     AIATLFLSMV KPGDTIVHSG PLYAATETLI ARILGRFGVH WLDFPAGATR EEIDAVLSKA
     ASGNVALIYL ESPANPTNAL VDVEAVSASR DAIFTGANKP PIAIDNTFLG PLWHKPLRHG
     ADLVVYSLTK YAGGHSDLVA GGVLGSKAHM DTIRLMRNTI GTICDPNTAW MLLRSLETLE
     LRMSRAGENA AKVCAFLRDH SAVEKVGYLG FLEGGQDARQ ADIYRRHCNG AGSTFSLYLK
     GGEAEAFAFL DALKIAKLAV SLGGTETLAS HPAAMTHLSV PDARKAALGI TDNLVRISIG
     VEDADDLIAD FSQALDAIGG
//
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