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Database: UniProt
Entry: E4ZIC3_LEPMJ
LinkDB: E4ZIC3_LEPMJ
Original site: E4ZIC3_LEPMJ 
ID   E4ZIC3_LEPMJ            Unreviewed;       454 AA.
AC   E4ZIC3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Similar to cystathionine beta-lyase {ECO:0000313|EMBL:CBX90784.1};
GN   ORFNames=LEMA_P058180.1 {ECO:0000313|EMBL:CBX90784.1};
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN   [1] {ECO:0000313|Proteomes:UP000002668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC   {ECO:0000313|Proteomes:UP000002668};
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
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; FP929065; CBX90784.1; -; Genomic_DNA.
DR   RefSeq; XP_003834149.1; XM_003834101.1.
DR   AlphaFoldDB; E4ZIC3; -.
DR   STRING; 985895.E4ZIC3; -.
DR   EnsemblFungi; CBX90784; CBX90784; LEMA_P058180.1.
DR   GeneID; 13292577; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   HOGENOM; CLU_018986_2_1_1; -.
DR   InParanoid; E4ZIC3; -.
DR   OMA; IANGVCN; -.
DR   OrthoDB; 6018at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:InterPro.
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; IPR006238; Cys_b_lyase_euk.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01329; cysta_beta_ly_E; 1.
DR   PANTHER; PTHR11808:SF50; CYSTATHIONINE BETA-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   Lyase {ECO:0000313|EMBL:CBX90784.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         237
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   454 AA;  48409 MW;  8011A87605C0F608 CRC64;
     MAGESSKVKA NGAGKAALPI DIDGHNLPPS PAPSSPRNGR KYALMTELVY TESTDQYNAS
     SVPIYQSATF KQDSATGGGG EYDYTRSGNP TRTHLERHLA KIMSANRALV VSSGMGALDV
     ITRLLRPGDE VVTGDDLYGG TNRLLKYLST HGGIIVHHVD TTNPDSVRAV VSSKTAMVLL
     ETPTNPLIKI CDIPAISAIT HAASPSAVVA VDNTMMSPML LNPLDLGADI VYESGTKYLS
     GHHDLMAGVI AVNDSALGDR LFFTINASGC GLSPFDSWLL LRGIKTLGIR MEKQQANAQR
     IAEFLESHGF KVRFPGLKSH PQYELHWSMA RGAGAVLSFE TGDVDISERI VESARLWGIS
     VSFGCVNSLI SMPCRMSHAS IDEKTRRERN MPEDIIRLCV GIEDVEDLLD DLSRALVQAG
     AVNITPGGFH ALGSTAAQTI EATSTAPAPA PAES
//
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