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Database: UniProt
Entry: A0A0Q3W4S2_9BACI
LinkDB: A0A0Q3W4S2_9BACI
Original site: A0A0Q3W4S2_9BACI 
ID   A0A0Q3W4S2_9BACI        Unreviewed;       400 AA.
AC   A0A0Q3W4S2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:KQL37493.1};
DE            EC=4.4.1.11 {ECO:0000313|EMBL:KQL37493.1};
GN   ORFNames=AN959_05660 {ECO:0000313|EMBL:KQL37493.1};
OS   Psychrobacillus sp. FJAT-21963.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX   NCBI_TaxID=1712028 {ECO:0000313|EMBL:KQL37493.1, ECO:0000313|Proteomes:UP000051878};
RN   [1] {ECO:0000313|EMBL:KQL37493.1, ECO:0000313|Proteomes:UP000051878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-21963 {ECO:0000313|EMBL:KQL37493.1,
RC   ECO:0000313|Proteomes:UP000051878};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (SEP-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:KQL37493.1}.
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DR   EMBL; LJIY01000001; KQL37493.1; -; Genomic_DNA.
DR   RefSeq; WP_053591014.1; NZ_LJIY01000001.1.
DR   AlphaFoldDB; A0A0Q3W4S2; -.
DR   PATRIC; fig|1712028.3.peg.1271; -.
DR   Proteomes; UP000051878; 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:SF80; GAMMA-CYSTATHIONASE; 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:KQL37493.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051878}.
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   400 AA;  43829 MW;  B47CB22D12B0A5A0 CRC64;
     MNKANWKIDT KIIHECLTPD EKTRAIVPSI TPAVAYSFST AEEAASVVAG MEEGIYYGRY
     GNPTVRKLEE KIASLEYGEA ALALSSGMAA ISTALLSCLK TGDHVLVTKD VYGGTYSFLT
     TLAERIGIQF DFVDCTNPKN ILEAMLSNTK AIYIETPSNP NLTILDIEQI ASVSKKMGVP
     LIVDNTFMSP ILQNPLLLGA DIVVHSGTKY INGHGDVLCG FIVSDANRID MMRKKIMGDL
     GQNLNAYEAF LVIRGLKTIS LRIEKHCSNA RKVAEFLASH PMIEKVYYPG LKCHPGHEIA
     IKQMRDMGGI VSFEVKGGLE QGKLFINSLE LAMISFSLGD PETLIQHPAS MTHAQIPKEE
     RAKYGITDGL MRLSVGLEDS QDIINDLEQA LKKVDIRMSV
//
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