ID E3H6K7_ILYPC Unreviewed; 391 AA.
AC E3H6K7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:ADO81892.1};
DE EC=4.4.1.11 {ECO:0000313|EMBL:ADO81892.1};
GN OrderedLocusNames=Ilyop_0103 {ECO:0000313|EMBL:ADO81892.1};
OS Ilyobacter polytropus (strain ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Ilyobacter.
OX NCBI_TaxID=572544 {ECO:0000313|EMBL:ADO81892.1, ECO:0000313|Proteomes:UP000006875};
RN [1] {ECO:0000313|EMBL:ADO81892.1, ECO:0000313|Proteomes:UP000006875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1
RC {ECO:0000313|Proteomes:UP000006875};
RX PubMed=21304735; DOI=10.4056/sigs.1273360;
RA Sikorski J., Chertkov O., Lapidus A., Nolan M., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Brambilla E., Yasawong M.,
RA Rohde M., Pukall R., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ilyobacter polytropus type strain (CuHbu1).";
RL Stand. Genomic Sci. 3:304-314(2010).
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; CP002281; ADO81892.1; -; Genomic_DNA.
DR RefSeq; WP_013386563.1; NC_014632.1.
DR AlphaFoldDB; E3H6K7; -.
DR STRING; 572544.Ilyop_0103; -.
DR KEGG; ipo:Ilyop_0103; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_0; -.
DR OrthoDB; 634606at2; -.
DR Proteomes; UP000006875; Chromosome.
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:SF90; 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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ADO81892.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006875}.
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 391 AA; 42697 MW; FA3B307909E45BCB CRC64;
MKINTDLLHA QQKHDPVTGS HVSPLYQTST FVLPNFDEAV RLNQNIDQGF VYSRFGNPTV
DEFERKVAHL EQAEAAVASA SGLGAITLAV MSLVKTGDHV IFGDVIYGCT FALFTKILPS
LGVAYTIVDT TNPEAIEAAI KPNTVLVYVE TPANPTLKIS DIEAVSKVTK KHEKVKLVVD
STFASPYLQN PIVLGADMVV HSATKYLCGH GTVTAGVLAG SKELIDRAKM PYLQCFGSVL
DPFAAWTIMQ GMKTLGVRME KHCSNAMKVA EFLDNHPMVD KVYYPGLPSH ESHETAKKQM
KDFGAMMSVD IKGGIDSCRT VMNSVKVFSL ATSLGNVDSL IQHSPTMSHF DMTLEERCKV
NIFDGQVRIS VGIEDVEDLI EDLDQALKSI K
//
