ID   F3Z868_9ACTN            Unreviewed;       409 AA.
AC   F3Z868;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Putative methionine gamma-lyase {ECO:0000313|EMBL:EGJ76054.1};
GN   ORFNames=STTU_3265 {ECO:0000313|EMBL:EGJ76054.1};
OS   Streptomyces sp. Tu6071.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ76054.1};
RN   [1] {ECO:0000313|EMBL:EGJ76054.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ76054.1};
RA   Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA   Gunther S.;
RT   "Genome sequence of Streptomyces sp. Tu6071.";
RL   Submitted (APR-2011) 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|RuleBase:RU362118}.
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DR   EMBL; CM001165; EGJ76054.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3Z868; -.
DR   HOGENOM; CLU_018986_2_2_11; -.
DR   Proteomes; UP000003955; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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:SF93; CYSTATHIONINE GAMMA-LYASE-RELATED; 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:EGJ76054.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         233
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   409 AA;  43156 MW;  2C5A5A0A85F32853 CRC64;
     MPHPGSPAQR GAGEVRTSPV TAPTGGPGAA ADEKRDSMTG DGTRAVRAGL PEAARNEPTM
     PGPVFAAHFH LPGEVAGPYT YGRDGNPTWT GLESALSELE APGEEAGTLL FASGMAAISA
     VLFSQTRSGD TVVLPSDGYQ VLPLVREQLT AYGVTVRTAP TGGDAELDAL DGARLLWIES
     PSNPGLDVCD IRRLVAAAHE RGALVGVDNT LSTPLGQRPL DLGADFSVAS DTKALTGHGD
     VLLGHVTTRD PALLEGVRRW RKIIGAIPGP METWLAHRSL ATLHLRLDRQ NANALALAEA
     LRARPEVSGL RYPGLPDDPA HQLATAQMLR YGTVLGFTLP SREHAERFLA RARLVEDATS
     FGGVRSTAER RRRWGGDAVA EGFVRFSAGA EDTEDLVADV LRALDESEG
//