ID A0A0D0WS78_9ACTN Unreviewed; 393 AA.
AC A0A0D0WS78;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:KIR61821.1};
DE EC=4.4.1.11 {ECO:0000313|EMBL:KIR61821.1};
GN ORFNames=TK50_30510 {ECO:0000313|EMBL:KIR61821.1};
OS Micromonospora haikouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=686309 {ECO:0000313|EMBL:KIR61821.1, ECO:0000313|Proteomes:UP000032254};
RN [1] {ECO:0000313|EMBL:KIR61821.1, ECO:0000313|Proteomes:UP000032254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR61821.1,
RC ECO:0000313|Proteomes:UP000032254};
RA Long Z., Huang Y., Jiang Y.;
RT "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1
RT genome.";
RL Submitted (JAN-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:KIR61821.1}.
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DR EMBL; JXSX01000003; KIR61821.1; -; Genomic_DNA.
DR RefSeq; WP_043968983.1; NZ_JXSX01000003.1.
DR AlphaFoldDB; A0A0D0WS78; -.
DR PATRIC; fig|47853.6.peg.6392; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000032254; 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:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 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:KIR61821.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000032254}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 393 AA; 40800 MW; 5A36AA4EF8B982ED CRC64;
MTGIGTTAIH GDDDLHPPGA VSPPIVQSAT FGAESDERFT EVATQVRPDA FYTRYGNPNH
AQVAAVVAEL EGVETGLVTA SGMGAVTTIA LALLSAGDHV IVQRSTYGGT TSLATGLLTR
FGVTCTQVDQ TDVDAFARAL TPRTRLLLVE TPSNPLLELT DLTAVIELAH AHGAYAVVDN
TFATPVNQRP AALGADLVWH SATKFLGGHS DVTAGVVVGS AELVDRVWQT AIVTGATLGP
IDSWLLLRGI RTLPLRMARH NDNALALARE LEAHPAVARV RYPGLPSHPQ HDLATKQMSG
YGGVFSLDLA GGQPAAATLL AELRLAKRAA SLGSVSTLVV HPRSMWAGIV DTAQLAATGI
GEGLVRVSTG IEDTADLLAD FTRALDAVAG QAG
//
