ID A0A137QHV8_9AGAR Unreviewed; 444 AA.
AC A0A137QHV8;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:KXN86831.1};
GN ORFNames=AN958_09567 {ECO:0000313|EMBL:KXN86831.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN86831.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN86831.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN86831.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-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|RuleBase:RU362118}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ962312; KXN86831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QHV8; -.
DR STRING; 1714833.A0A137QHV8; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000070249; 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; 2.
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:KXN86831.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 444 AA; 47822 MW; 56AC3FB3FE9768DA CRC64;
MAPALDLRHT TVSNSHVNGV SKKHHPVEGF STRAIHVGSE PNLETGAVVP PISLATTYKQ
DAIGVHKGFE YSRSSNPNRD ALERTLASIE LGGGHALAFA SGSSTTATVL QLLGPNAHII
SVNDVYGGTF RYMSRVAKEN QGLETTFLDL ENLSEDGAEL LNEIRDNTRL IWIETPTNPT
LRLISIQSIR AHISKLENPP LILVDNTFLS PFYSSPLLLG ADIVLHSLTK YINGHSDVVM
GALILPNTPF HTELASKLRF LQNAIGAVPS AYDSWLAQRG AKTLALRMKA HGVNALAVAH
ALKASPLVEE VTYPGLASHP RHHIAWESLS PHAKKWIEAL PDQLSSTTDF PYSGMISFSI
KGGLEAADKF LTSTRLFALA ESLGGVESLA EHPAKMTHGS IPPAEREKLG ISDGLIRLSV
GVEDEEDLVE DVLQALEKAA GHLA
//