ID   W6ZFJ1_COCMI            Unreviewed;       430 AA.
AC   W6ZFJ1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=cysteine synthase {ECO:0000256|ARBA:ARBA00012681};
DE            EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681};
GN   ORFNames=COCMIDRAFT_86538 {ECO:0000313|EMBL:EUC48785.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC48785.1};
RN   [1] {ECO:0000313|EMBL:EUC48785.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC48785.1};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000256|ARBA:ARBA00007103}.
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DR   EMBL; KI963938; EUC48785.1; -; Genomic_DNA.
DR   RefSeq; XP_007684781.1; XM_007686591.1.
DR   AlphaFoldDB; W6ZFJ1; -.
DR   STRING; 930090.W6ZFJ1; -.
DR   GeneID; 19126879; -.
DR   KEGG; bor:COCMIDRAFT_86538; -.
DR   eggNOG; KOG1481; Eukaryota.
DR   HOGENOM; CLU_021018_1_0_1; -.
DR   OrthoDB; 852805at2759; -.
DR   Proteomes; UP000054032; Unassembled WGS sequence.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF35; MITOCHONDRIAL CYSTEINE SYNTHASE-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
FT   DOMAIN          83..399
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   430 AA;  46375 MW;  CCEF84FEBDCA13D0 CRC64;
     MSDRSRYYIL GTFLLGAAAI AAYNKKLAAE KNDTASSHSL LAQQQNLLLQ LAKVNDLEEF
     KKGLLEIERS LENGTASIKE GIEGCIGNTP LIKIKSLSEY TGCDILAKAE FLNGAGNSPK
     DRVALSIIEM AEQKGLLIPH SGDTIYEGTV GSTGISLAAI CRARGYKAHI CMPNDMAIEK
     SDLLLKLGAE VEKVRPAPIV DQKQFVNLAR SRAEEHTASA EKSGRGLFAD QFETEANWRA
     HFTGTGPEIY EQTGHRLDAF VSGAGTGGTI SGVAMFLKSK LPNLKVVLAD PPGSGLFNRV
     KYGVMFDPKE REGTRRRHQV DTIVEGIGIN RVTHNFDVGR ELIDDAIRVT DEQAISMARW
     LVEHDGIFVG SSSAVNCVAA AKLAKSLGPG HRIVTILCDS GARHLSKFWK STEPIGGVDS
     DVSLEAIIDA
//