ID A0KYK1_SHESA Unreviewed; 397 AA.
AC A0KYK1;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=L-methionine gamma-lyase {ECO:0000256|ARBA:ARBA00019040};
DE EC=4.4.1.11 {ECO:0000256|ARBA:ARBA00012222};
GN OrderedLocusNames=Shewana3_2643 {ECO:0000313|EMBL:ABK48870.1};
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122 {ECO:0000313|EMBL:ABK48870.1, ECO:0000313|Proteomes:UP000002589};
RN [1] {ECO:0000313|Proteomes:UP000002589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3 {ECO:0000313|Proteomes:UP000002589};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-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}.
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DR EMBL; CP000469; ABK48870.1; -; Genomic_DNA.
DR RefSeq; WP_011717535.1; NC_008577.1.
DR AlphaFoldDB; A0KYK1; -.
DR STRING; 94122.Shewana3_2643; -.
DR KEGG; shn:Shewana3_2643; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_6; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000002589; 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; 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:ABK48870.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 211
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 397 AA; 42887 MW; DC45C9FC28F254FC CRC64;
MQDESSKQWK AATQAIHAGH EREAFGTLVT PLYQTATFVF ESAQQGGERF AGNEPGYIYT
RLGNPTVAEL ERKMAILEGA EAAAATASGM GAVSAALLAN LQMGDHLVAS NAVYGCTFAL
MTSQFARFGI EVTLVDFTDL AAIERAIKPN TRVIFCETPV NPHLQVFDLK GIADIAKRHQ
LVSIVDNTFM TPLLQQPLAF GIDLVVHSAT KYLNGHGDVI AGVVCGSEEQ LHRVKYEILK
DIGAVMSPHD AWLILRGLKT LDVRLQRHCD SAQRVAEFLE QHPAVTRVYY PGLKSHSGHR
FIGGQMAKAG GVIAFELAAS LEQAMAFVGY LKLFSIAVSL GDAESLIQHP ASMTHSPYTP
EARQAAGISD NLLRISIGLE DCGDIIEDLN QALAMLA
//
