ID   A0A1I2GQS9_9ACTN        Unreviewed;       397 AA.
AC   A0A1I2GQS9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Methionine-gamma-lyase {ECO:0000313|EMBL:SFF19638.1};
GN   ORFNames=SAMN05421541_10773 {ECO:0000313|EMBL:SFF19638.1};
OS   Actinoplanes philippinensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=35752 {ECO:0000313|EMBL:SFF19638.1, ECO:0000313|Proteomes:UP000199645};
RN   [1] {ECO:0000313|EMBL:SFF19638.1, ECO:0000313|Proteomes:UP000199645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43019 {ECO:0000313|EMBL:SFF19638.1,
RC   ECO:0000313|Proteomes:UP000199645};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FONV01000007; SFF19638.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2GQS9; -.
DR   STRING; 35752.SAMN05421541_10773; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000199645; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:SFF19638.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199645}.
FT   REGION          30..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         211
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   397 AA;  40988 MW;  DA884EEDB8CF409E CRC64;
     MTSPLHSDSV AVHAGRADLT ALGVHAPPLD LSSTYPLPDP ERGGESYEAM ATGGHPLPDG
     GAVYARLWNP TVARFETALA QLEQTATAVA FGSGMAAMTA AILAHTAMAG RPHVVAVRPL
     YGGTDHLLAT GLLGTEVTFC AESEVAARIR PDTGLVILET PANPTLDLVD IAAVAGQAGD
     VPLLVDNTFA TPVLQNPVTL GATMALHSAT KYLGGHGDVV AGVIACGEAT AGRLRQVRAV
     TGGLLHPWGA YLLHRGLATL PVRMRAQQDS ARRIAAWLAG HPAVARVHYP GLDGDPRGLL
     GRQSRGPGAM VSIALRGGFE AACRLTTGTR LFTHAVSLGG VDSLIQHPAA LTHRPVPAHA
     RPSADLVRLS IGLEHAGDLI ADLDRALAAT VPPRRSS
//