ID A0A0F0C6L8_9CLOT Unreviewed; 439 AA.
AC A0A0F0C6L8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:KJJ65801.1};
DE EC=4.4.1.11 {ECO:0000313|EMBL:KJJ65801.1};
GN Name=mdeA_2 {ECO:0000313|EMBL:KJJ65801.1};
GN ORFNames=CLFS41_54830 {ECO:0000313|EMBL:KJJ65801.1};
OS Clostridium sp. FS41.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ65801.1, ECO:0000313|Proteomes:UP000033604};
RN [1] {ECO:0000313|EMBL:KJJ65801.1, ECO:0000313|Proteomes:UP000033604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS41 {ECO:0000313|EMBL:KJJ65801.1,
RC ECO:0000313|Proteomes:UP000033604};
RA Poehlein A., Daniel R.;
RT "Genome sequencing of Clostridium sp. FS41.";
RL Submitted (FEB-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|ARBA:ARBA00009077, 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:KJJ65801.1}.
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DR EMBL; JYHN01000092; KJJ65801.1; -; Genomic_DNA.
DR RefSeq; WP_007860383.1; NZ_JYHN01000092.1.
DR AlphaFoldDB; A0A0F0C6L8; -.
DR GeneID; 77446668; -.
DR PATRIC; fig|1609975.3.peg.5843; -.
DR Proteomes; UP000033604; 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:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; 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; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR PANTHER; PTHR43797:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 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:KJJ65801.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000033604}.
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 439 AA; 47648 MW; 4BB3C310EF3E7A91 CRC64;
MGEKRKRENR QFRFETTQLH AGQETPDPAT GARAVPIYQT SSYVFDNCDH GAARFNLSDA
GNIYSRLTNP TLDVFEARMA ALEGGVAALA TASGAAALAY TFQNLTRAGD HLVASSHIYG
GTYNYLAHTF PEYGVGTTFV DPADLKGLEL AIRDNTKAVF IETLGNPNSD IADIEAIADI
AHRHQIPLVI DNTFATPYLV RPIEYGADIV VHSATKFIGG HGTTVGGVIV DGGKFDWVGS
GKFPGLTDAN ASYHGIRFAQ DVGAAAFVTR IRAILLRDTG ATLSPFHGFL FLQGLESLSL
RVERHVVNAL KVVDYLNSHP QVEAVHHPAV SNDPVQQALY KKYFPNGGGS IFTFEIRGGA
QKAREFIDNL ELFSLLANVA DVKSLVIHPA STTHSQLNEE ELLEQGIRPG TIRLSIGTEH
IDDILEDLEE AFQAVEQHP
//