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Database: UniProt
Entry: D0NLW7_PHYIT
LinkDB: D0NLW7_PHYIT
Original site: D0NLW7_PHYIT 
ID   D0NLW7_PHYIT            Unreviewed;       534 AA.
AC   D0NLW7;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Cystathionine beta-lyase {ECO:0000313|EMBL:EEY60664.1};
GN   ORFNames=PITG_13402 {ECO:0000313|EMBL:EEY60664.1};
OS   Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY60664.1, ECO:0000313|Proteomes:UP000006643};
RN   [1] {ECO:0000313|Proteomes:UP000006643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX   PubMed=19741609; DOI=10.1038/nature08358;
RG   The Broad Institute Genome Sequencing Platform;
RA   Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA   Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA   Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA   Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA   Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA   Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA   Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA   Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA   Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA   Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA   Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA   Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA   Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA   Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA   Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA   Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA   Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA   Nusbaum C.;
RT   "Genome sequence and analysis of the Irish potato famine pathogen
RT   Phytophthora infestans.";
RL   Nature 461:393-398(2009).
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; DS028145; EEY60664.1; -; Genomic_DNA.
DR   RefSeq; XP_002900037.1; XM_002899991.1.
DR   AlphaFoldDB; D0NLW7; -.
DR   STRING; 403677.D0NLW7; -.
DR   EnsemblProtists; PITG_13402T0; PITG_13402T0; PITG_13402.
DR   GeneID; 9477969; -.
DR   KEGG; pif:PITG_13402; -.
DR   VEuPathDB; FungiDB:PITG_13402; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   HOGENOM; CLU_018986_2_1_1; -.
DR   InParanoid; D0NLW7; -.
DR   OMA; IANGVCN; -.
DR   OrthoDB; 6018at2759; -.
DR   Proteomes; UP000006643; Partially assembled 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   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006643}.
FT   REGION          36..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  58107 MW;  6AA6F1C099C869F7 CRC64;
     MASSSAALQQ SLGESEVFDL VCDYLRTRQF FEAERTLRSE REQAETTGSP RAASPVAAAN
     QQDATPSEDA TAPSLASRLE FMLERSYVTQ LVSGTGQEEP EKIFVPRHEL ETTPKRARAN
     LDGNEALEIE DVNRNTLEEG DDEFNISTRI VSFEACKDDP HGSATMPIYQ TSTFAQPSGT
     TFGAYDYTRS GNPTRAALER QMAELEGGHR AFAFTSGMAA LSAVSRLAHA GDEIVLSDDS
     YGGTYRLLSK VATKNGVDVK YVDLSGENGP KNLLAALSDK TKLVMMESPT NPMQRICDIK
     RLAEAAHTVG ALLSVDNTMM SPILQNPLKL GADIVVHSAT KFICGHSDTM SGIVIAKDPE
     LCRDVYFYQN AEGTGLAPFD CWLLLRGVKT MSLRVLAAQK NAVKVANFLN DHPLIKTVHY
     TNLLPENSAD RKIHDSQARG CGSVVCFRTG SLAFSQHLLT VTKLFKITVS FGSVNSLISL
     PGAMSHASIP EEVRKARSFP EDLVRLSIGV EDAKDLIKDL SQALQSYVPP QTTQ
//
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