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Database: UniProt
Entry: A0A137QHV8_9AGAR
LinkDB: A0A137QHV8_9AGAR
Original site: A0A137QHV8_9AGAR 
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}.
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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
//
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