ID Q1YSN5_9GAMM Unreviewed; 399 AA.
AC Q1YSN5;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=L-methionine gamma-lyase {ECO:0000256|ARBA:ARBA00019040};
DE EC=4.4.1.11 {ECO:0000256|ARBA:ARBA00012222};
GN ORFNames=GB2207_11158 {ECO:0000313|EMBL:EAS47171.1};
OS gamma proteobacterium HTCC2207.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Porticoccaceae; SAR92 clade.
OX NCBI_TaxID=314287 {ECO:0000313|EMBL:EAS47171.1, ECO:0000313|Proteomes:UP000005555};
RN [1] {ECO:0000313|EMBL:EAS47171.1, ECO:0000313|Proteomes:UP000005555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2207 {ECO:0000313|EMBL:EAS47171.1,
RC ECO:0000313|Proteomes:UP000005555};
RA Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-methionine = 2-oxobutanoate + methanethiol + NH4(+);
CC Xref=Rhea:RHEA:23800, ChEBI:CHEBI:15377, ChEBI:CHEBI:16007,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; EC=4.4.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000271};
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. L-
CC methionine gamma-lyase subfamily. {ECO:0000256|ARBA:ARBA00008667}.
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:EAS47171.1}.
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DR EMBL; AAPI01000003; EAS47171.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1YSN5; -.
DR STRING; 314287.GB2207_11158; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_6; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000005555; 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; IPR006237; L-Met_gamma_lys.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01328; met_gam_lyase; 1.
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:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EAS47171.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 214
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 399 AA; 42999 MW; 901593167C732CBA CRC64;
MSIDHHKKLS FATRSVHAGY DSSANQGALN PPIYMTSTYS FGSVADGAGR FSGEQKGHFY
SRISNPTQEI LETRLADLEE GEAALATASG MGAITAALWT LVGPGDQILV DKTLYGCTFS
FMEHGLKKFG VEICYADFTN HAEVQAHLSD KTKVVYFETP VNPNMRVIDI AAVSALVKGH
SSAIKIMVDN TYCTPALQRP LSLGADLVVH SATKYLGGHG DLIAGAVVGD AETIQQIRLF
GLKDMTGAVI SPMNVFLILR GIKTLQLRME RHCQNAQAIA EMLEQHPAVD QVFFPGLKSD
PWHAIASKQM DDFGGMIALE LKGGYEASVR MLNKLKLAKL AVSLGDAETL IQHPASMTHS
VYTPEERAEH GISEGLVRIS AGLEAAEDII ADLQQALAD
//
