GenomeNet

Database: UniProt
Entry: E3Q9M2_COLGM
LinkDB: E3Q9M2_COLGM
Original site: E3Q9M2_COLGM 
ID   E3Q9M2_COLGM            Unreviewed;       438 AA.
AC   E3Q9M2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:EFQ27560.1};
GN   ORFNames=GLRG_02704 {ECO:0000313|EMBL:EFQ27560.1};
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN   [1] {ECO:0000313|Proteomes:UP000008782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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; GG697338; EFQ27560.1; -; Genomic_DNA.
DR   RefSeq; XP_008091580.1; XM_008093389.1.
DR   AlphaFoldDB; E3Q9M2; -.
DR   STRING; 645133.E3Q9M2; -.
DR   EnsemblFungi; EFQ27560; EFQ27560; GLRG_02704.
DR   GeneID; 24408069; -.
DR   VEuPathDB; FungiDB:GLRG_02704; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   HOGENOM; CLU_018986_2_1_1; -.
DR   OrthoDB; 6018at2759; -.
DR   Proteomes; UP000008782; Unassembled WGS sequence.
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:EFQ27560.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008782};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          1..40
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   438 AA;  47379 MW;  95849DA0932ACB35 CRC64;
     MSTPPNNGAA AKSSNPLKRV DLDGHDLPPS PTPSSPRNGR RRYALATELV YTDSNDQYGA
     SSIPIYQSAT FKQTSATGGN EYDYTRSGNP TRTHLERHLA KIMNATRALA VGSGMGALDV
     ITRLLRPGDE VITGDDLYGG TNRLLAYLSS NQGIIVHHVD TTNVENLRHV VSDKTAMVLL
     ETPTNPLIKI VDIPSIAKLV HDVNDKALVV VDNTMLSPML LNPLDIGADI VYESGTKYLS
     GHHDIMAGVI GVNDSSIGDK LYFTINATGC GLSPNDSFLL MRGIKTLAIR MEKQQANAQQ
     IAEFLESHGF KVRYPGLKSH PQYDLHWSMA RGAGAVLSFE TGDAALSERI VEAAKLYSIS
     VSFGCVNSLI SMPCQMSHAS IDAKTRKERQ MPEDLIRLCV GIEDVTDLIE DLSRALVQAG
     AVHVTLEGFH AAQSVQEA
//
DBGET integrated database retrieval system