ID A0A1H6U8V6_9FLAO Unreviewed; 405 AA.
AC A0A1H6U8V6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Methionine-gamma-lyase {ECO:0000313|EMBL:SEI88798.1};
GN ORFNames=SAMN05660918_1821 {ECO:0000313|EMBL:SEI88798.1};
OS Flavobacterium terrigena.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402734 {ECO:0000313|EMBL:SEI88798.1, ECO:0000313|Proteomes:UP000199702};
RN [1] {ECO:0000313|EMBL:SEI88798.1, ECO:0000313|Proteomes:UP000199702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17934 {ECO:0000313|EMBL:SEI88798.1,
RC ECO:0000313|Proteomes:UP000199702};
RA de Groot N.N.;
RL Submitted (OCT-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; FNYA01000004; SEI88798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6U8V6; -.
DR STRING; 402734.SAMN05660918_1821; -.
DR OrthoDB; 9803729at2; -.
DR Proteomes; UP000199702; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:SF15; CYSTATHIONINE 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:SEI88798.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 405 AA; 43833 MW; 49B293600CB30325 CRC64;
MNNFNPADKI QDLQYFGEFG GVNPSISDSS TYTFLSAKTM FDTFEGNAEG CYLYSRHSSP
SNLYLDKALA AMEGTETANV SASGMGAITP TILQLCGQGD HVVSSRTIYG GTYAFLKNFA
PRFGVATTFV DITKLDLVEA AITPNTKVLY CETVSNPLLE VADIASLAKI AKKHNIKLVV
DNTFSPLSVS PAKLGADIVI HSLTKYINGS SDTVGGVTCA SQEFINDLKN VNSGASMLLG
PTMDSLRSAS VMKNLRTLHI RMKQHSHNAM YLANKFEADG IKTVYPGLAS HPSHEVYKNM
INPEYGFGGM MTIDVGSLDK ANALMELMQE RNLGYLAVSL GFYKTLFSAP GTSTSSEIPL
EEQAEMGLTD GLIRFSIGLD NDIERTYQSM NACMKELGIL QLENA
//