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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//