ID   A0A1G7WG68_9ACTN        Unreviewed;       379 AA.
AC   A0A1G7WG68;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:SDG70888.1};
GN   ORFNames=SAMN05660324_3325 {ECO:0000313|EMBL:SDG70888.1};
OS   Klenkia brasiliensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Klenkia.
OX   NCBI_TaxID=333142 {ECO:0000313|EMBL:SDG70888.1, ECO:0000313|Proteomes:UP000198863};
RN   [1] {ECO:0000313|EMBL:SDG70888.1, ECO:0000313|Proteomes:UP000198863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44526 {ECO:0000313|EMBL:SDG70888.1,
RC   ECO:0000313|Proteomes:UP000198863};
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; FNCF01000005; SDG70888.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7WG68; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000198863; Unassembled WGS sequence.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
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; 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.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:SDG70888.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   379 AA;  39876 MW;  F3952638A8F000A5 CRC64;
     MSGFNTRAIH DGQEPDPTTG AVAVPLHLTS TYKQDGVGGL RNGYEYSRSA NPTRTALQEA
     LASLEQGAAG LAFASGLAAE DALLRTVLDP GDHLVIPIDA YGGTFRLISK VLQRWGVEHT
     PVDLSDLDAV RAAFRPTTKL VWCETPTNPL LGIADIAALA QLAHEHGALL AVDNTFASPY
     LQQPLTLGAD VVVHSTTKYL GGHSDVVGGA LVAGTAELGE RLAFHQNAMG AVAGPFDAWL
     VLRGIKTLGV RMDRHQANAT KVAEFLVEHP AVSTVLYPGL PTHPGHEVAA RQMSGPGGML
     SFRLRAGEEA ALAVCERAQV FTLAESLGGV ESLVEHPHRM THASVAGSAL EVPADLVRLS
     VGIEDVEDLL ADLDRMLAG
//