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Database: UniProt
Entry: W7LQS1_GIBM7
LinkDB: W7LQS1_GIBM7
Original site: W7LQS1_GIBM7 
ID   W7LQS1_GIBM7            Unreviewed;       422 AA.
AC   W7LQS1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:EWG37860.1};
GN   ORFNames=FVEG_01304 {ECO:0000313|EMBL:EWG37860.1};
OS   Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS   fungus) (Fusarium verticillioides).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG37860.1, ECO:0000313|Proteomes:UP000009096};
RN   [1] {ECO:0000313|EMBL:EWG37860.1, ECO:0000313|Proteomes:UP000009096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7600 {ECO:0000313|EMBL:EWG37860.1}, and M3125 / FGSC 7600
RC   {ECO:0000313|Proteomes:UP000009096};
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA   Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA   Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA   Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA   Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [2] {ECO:0000313|EMBL:EWG37860.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=7600 {ECO:0000313|EMBL:EWG37860.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RL   Submitted (NOV-2013) 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; DS022242; EWG37856.1; -; Genomic_DNA.
DR   EMBL; DS022242; EWG37857.1; -; Genomic_DNA.
DR   EMBL; DS022242; EWG37858.1; -; Genomic_DNA.
DR   EMBL; DS022242; EWG37859.1; -; Genomic_DNA.
DR   EMBL; DS022242; EWG37860.1; -; Genomic_DNA.
DR   EMBL; DS022242; EWG37861.1; -; Genomic_DNA.
DR   EMBL; DS022242; EWG37862.1; -; Genomic_DNA.
DR   EMBL; DS022242; EWG37863.1; -; Genomic_DNA.
DR   EMBL; DS022242; EWG37864.1; -; Genomic_DNA.
DR   RefSeq; XP_018744047.1; XM_018888191.1.
DR   RefSeq; XP_018744048.1; XM_018888192.1.
DR   RefSeq; XP_018744049.1; XM_018888193.1.
DR   RefSeq; XP_018744050.1; XM_018888194.1.
DR   RefSeq; XP_018744051.1; XM_018888195.1.
DR   RefSeq; XP_018744052.1; XM_018888196.1.
DR   RefSeq; XP_018744053.1; XM_018888197.1.
DR   RefSeq; XP_018744054.1; XM_018888198.1.
DR   RefSeq; XP_018744055.1; XM_018888199.1.
DR   AlphaFoldDB; W7LQS1; -.
DR   STRING; 334819.W7LQS1; -.
DR   EnsemblFungi; FVEG_01304T0; FVEG_01304T0; FVEG_01304.
DR   GeneID; 30059612; -.
DR   KEGG; fvr:FVEG_01304; -.
DR   VEuPathDB; FungiDB:FVEG_01304; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   HOGENOM; CLU_018986_2_3_1; -.
DR   OMA; YKQDGVG; -.
DR   Proteomes; UP000009096; Chromosome 1.
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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:EWG37860.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009096};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         216
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   422 AA;  44691 MW;  AB06B2CBE7CF2E6A CRC64;
     MSAAPLNSDP VATPPRPPSP VHSFGTLAVH AGAPHDPATG AVIESISLST TFAQSAVGKP
     VGEYEYSRSA NPNRTNFETA VAALEHAKYA LAFSSGSATT ATILQSLAAG SHVISVSDVY
     GGTHRYFTQV AKAHGVKVTF TPEIEVDISE HITPDTRLIW IESPSNPTLR LVDVRAVVSE
     AHKHGVLVVV DNTFLSPYVQ NPLDFGADIV VHSVTKYING HSDVVMGVAA FNSDELKNRL
     SFLQNAIGAV PSAFDSWLAH RGLKTLHLRA REASRNADAV ARALEASPLV IAVNYPGLDS
     HPHRHIAKKQ HRDGLGGGML SFRIQGGHAA AERFCQVTKI FTLAESLGGV ESLVEVPSSM
     THAGIPRDQR EAVGIFDDLV RISCGVEDAQ DLTNDVLQAL EKATSAVKTN GFNGNGNGVN
     GS
//
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