ID R7RTI8_9CLOT Unreviewed; 399 AA.
AC R7RTI8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=L-methionine gamma-lyase {ECO:0000256|ARBA:ARBA00019040};
DE EC=4.4.1.11 {ECO:0000256|ARBA:ARBA00012222};
GN ORFNames=TCEL_00634 {ECO:0000313|EMBL:CDF58588.1};
OS Thermobrachium celere DSM 8682.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermobrachium.
OX NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF58588.1, ECO:0000313|Proteomes:UP000014923};
RN [1] {ECO:0000313|EMBL:CDF58588.1, ECO:0000313|Proteomes:UP000014923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF58588.1,
RC ECO:0000313|Proteomes:UP000014923};
RA Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT alkalithermophilic Caloramator celere.";
RL Submitted (MAR-2013) 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:CDF58588.1}.
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DR EMBL; CAVN010000097; CDF58588.1; -; Genomic_DNA.
DR RefSeq; WP_018662847.1; NZ_HF952018.1.
DR AlphaFoldDB; R7RTI8; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_3_9; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000014923; 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:CDF58588.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000014923}.
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 399 AA; 43488 MW; 290C0EBB4A658699 CRC64;
MDREFAKNMG FSTKAIHAGN HKNEFGTLAT PIYQTATFVF DSAQQGGNRF AGKEEGYIYT
RLGNPTVTVL EEKIAILEGG EACVATSSGM GAISSALWTA LKAGDHVVAA DTLYGCTFAY
LSHGLTRYGV EVTFVDASNP ENIKEAMRPN TKAIYIETPA NPNLKLIDIK KVAEIAHSKE
DCILIVDNTF CTPYIQRPIE LGADVVVHSA TKFLNGHGDV IAGFVVGRKS FIDQVRLYGI
KDMTGACLSP FDAYLILRGL KTLEIRMERH CSNAMKVAKF LEEHKAVKKV YYPGLESFEQ
YELAKEQMKL PGAIIAFELN GGVEEGIKVL NSCKVCTLAV SLGDAETLIQ HPASMTHSPY
TREERLKAGI SDGLIRLAVG LENAEDIIAD LKQALDAII
//