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Database: UniProt
Entry: A0A1C7D762_9SPHN
LinkDB: A0A1C7D762_9SPHN
Original site: A0A1C7D762_9SPHN 
ID   A0A1C7D762_9SPHN        Unreviewed;       442 AA.
AC   A0A1C7D762;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:ANU07309.1};
DE            EC=4.4.1.11 {ECO:0000313|EMBL:ANU07309.1};
GN   Name=mdeA {ECO:0000313|EMBL:ANU07309.1};
GN   ORFNames=A6F65_00999 {ECO:0000313|EMBL:ANU07309.1};
OS   Paraurantiacibacter namhicola.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Paraurantiacibacter.
OX   NCBI_TaxID=645517 {ECO:0000313|EMBL:ANU07309.1, ECO:0000313|Proteomes:UP000092698};
RN   [1] {ECO:0000313|EMBL:ANU07309.1, ECO:0000313|Proteomes:UP000092698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16345 {ECO:0000313|EMBL:ANU07309.1,
RC   ECO:0000313|Proteomes:UP000092698};
RA   Cheng H., Wu Y.-H., Jian S.-L., Huo Y.-Y., Wang C.-S., Xu X.-W.;
RT   "Complete genome sequence of Altererythrobacter namhicola JCM 16345T,
RT   containing esterase-encoding genes.";
RL   Submitted (JUL-2016) 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}.
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DR   EMBL; CP016545; ANU07309.1; -; Genomic_DNA.
DR   RefSeq; WP_067786461.1; NZ_CP016545.1.
DR   AlphaFoldDB; A0A1C7D762; -.
DR   STRING; 645517.A6F65_00999; -.
DR   KEGG; anh:A6F65_00999; -.
DR   PATRIC; fig|645517.4.peg.994; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000092698; Chromosome.
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.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:ANU07309.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092698}.
FT   REGION          1..30
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;  47396 MW;  F68F4AF9C67E7A3A CRC64;
     MTDAPHTPDN AQGKPTPRRK PKPEATTIGG RQLKPATLMM GHGYDPALSE GSLKAPIFLT
     STFAFENAAA GKRHFEGLTG IREGGAEGLV YSRFNGPNQE ILEDRLAIWD GAEDALCFSS
     GMTAICVLML AMCSQGDVIV HSGPLYAASE GFVAKVLSKF GVNYIAFPAG ADRETFDGVL
     EQAKAKASEN GGKVAMIYLE SPGNPTNALV DIEMVKEARD AALDWSCPIA IDNTFLGPLW
     QRPLDHGADI VVYSLTKYVG GHSDLVAGSI AGAKKWMDPV RALRNTMGGI ADPNTAWMLM
     RSLETVELRM QRAGENAAKV CDFLKDHPKV NGLGYLGHIK DARQQDIYDR HCLGAGSTFS
     VFIKGGEEAC FRFLDALKVA KLAVSLGGTE TLASHPASMT HLSVPEGRRT ELGISDELVR
     ISIGIEDADD LIADFEQALK AV
//
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