ID A0A1Q4Y7F2_9PSEU Unreviewed; 343 AA.
AC A0A1Q4Y7F2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:OKI30512.1};
GN ORFNames=A6A25_28160 {ECO:0000313|EMBL:OKI30512.1};
OS Saccharothrix sp. CB00851.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1835005 {ECO:0000313|EMBL:OKI30512.1, ECO:0000313|Proteomes:UP000186828};
RN [1] {ECO:0000313|EMBL:OKI30512.1, ECO:0000313|Proteomes:UP000186828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB00851 {ECO:0000313|EMBL:OKI30512.1,
RC ECO:0000313|Proteomes:UP000186828};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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}.
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:OKI30512.1}.
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DR EMBL; LWLC01000017; OKI30512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4Y7F2; -.
DR STRING; 1835005.A6A25_28160; -.
DR Proteomes; UP000186828; 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: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:OKI30512.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000186828}.
FT MOD_RES 173
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 343 AA; 35409 MW; 96EB0E1A759BCF75 CRC64;
MHSTPVVPGE PFLAGPVFAS AYHLGGNDTY GRAHNPTWRA LEAALGELDG GHTVLFPSGM
AAISTFLRVV LAPGDVVMLP SDGYFLTRTL VAEMPVEVVG APTAGPYPSF EGVRLVLLES
PSNPGLDVCD ITALAEAAHA AGALVAVDNT TATPLGQQPL LLGADAVVSS DTKAVAGHSD
VLLGHVSTSD PALAERVRAA RTTGGAIPGP FEAWLAHRGL GTLDLRLSRQ AANAAALYEA
LKAHPAVTGL RWPGAPEDPA HEVAAKQMRR FGGVLTFELA GADAVAAFLE KSRLVFASTS
FGGLHTSLDR RAQWGDPVPE GLVRLSAGCE DTADLVEDVL GAL
//
