ID A0A0L6VJH8_9BASI Unreviewed; 458 AA.
AC A0A0L6VJH8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Cystathionine gamma-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=VP01_1509g1 {ECO:0000313|EMBL:KNZ60727.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ60727.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ60727.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ60727.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) 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}.
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:KNZ60727.1}.
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DR EMBL; LAVV01005664; KNZ60727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6VJH8; -.
DR STRING; 27349.A0A0L6VJH8; -.
DR VEuPathDB; FungiDB:VP01_1509g1; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000037035; 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:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
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:SF15; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000037035}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 242
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 458 AA; 49385 MW; 13E56B7AFCE3E2BF CRC64;
MTNHLVDASP ISKPMSSNPH GDHLNTRLIH VGAHSDPSTG AVIRPISLSS TFAQSAVGSH
SGYEYSRSLN PNRLDLETVV ASLEGVDELE RVEPAGLPLP GALAVSSGSA ATATIINALV
GPGAHLVAMS DVYGGTYRYL NQVANQLGIK STMVDLAFTD DSPQAAQLAL KRLQQSILPG
LTKLIWIETP TNPTLRLVDI ACLSGFARKN GILLVVDNTF LSPYYQQPLR LGADVVLHSA
TKYINGHSDV VLGVIISRHR DLIQKMRFLQ NAHGAVPSAF DCWLAQRGLK TLALRMLRHG
TNALAIASWL QDEALPQGWI TQVRYVGLTG SQIGWRQIPS ETQEELRKLG YDGDGGGRYP
YGGMISFKIR SSAQPNGSGT DYSNADTFLK NCRLFTLAES LGGIESLASL PAKMTHATLT
EEHRAQLGID GSLVRLSVGI ENAQDLIADL EQSFRKTF
//
