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Database: UniProt
Entry: Q9U5E5_ENTDI
LinkDB: Q9U5E5_ENTDI
Original site: Q9U5E5_ENTDI 
ID   Q9U5E5_ENTDI            Unreviewed;       336 AA.
AC   Q9U5E5;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Cysteine synthase 1 {ECO:0000313|EMBL:BAA88219.1};
OS   Entamoeba dispar.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=46681 {ECO:0000313|EMBL:BAA88219.1};
RN   [1] {ECO:0000313|EMBL:BAA88219.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SAW1734R {ECO:0000313|EMBL:BAA88219.1};
RX   PubMed=10717309; DOI=10.1016/S0166-6851(00)00177-8;
RA   Nozaki T., Tokoro M., Imada M., Saito Y., Abe Y., Shigeta Y., Takeuchi T.;
RT   "Cloning and biochemical characterization of genes encoding two isozymes of
RT   cysteine synthase from Entamoeba dispar.";
RL   Mol. Biochem. Parasitol. 107:129-133(2000).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR605856-50};
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DR   EMBL; AB028631; BAA88219.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9U5E5; -.
DR   VEuPathDB; AmoebaDB:EDI_052090; -.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:InterPro.
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; IPR005856; Cys_synth.
DR   InterPro; IPR005859; CysK.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01139; cysK; 1.
DR   NCBIfam; TIGR01136; cysKM; 1.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF253; CYSTEINE SYNTHASE 1; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR605856-50}.
FT   DOMAIN          18..308
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         88
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         192..196
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         280
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         58
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   336 AA;  36238 MW;  40ADD543DB111473 CRC64;
     MQNITINTPR KRIYRNILET IGGTPLVELH GVTEHPTIKK NTKVLVKLEC FNPMSSVKDR
     VGFNIVYQAI KDGRLKPGME IIEATSGNTG IGLCQAGAVF GYPVNIVMPS TMSIERQMIM
     KAFGANLVLS DGTKGMPGAI AKYEDLIKQH PNKYFPANQF GNPDNTAAHI YTANEIWEDT
     NGEVDIIVSA VGTAGTVIGV GENLKKKKQG VKVVAVEPEE SAVLSGKPKG PHGIQGIGAG
     FVTDIYKKEV VDEIITIKTQ DAWKMARATV KYDGIMCGMS SGAAILAGLK EAGKAENEGK
     TIVIILPDCG ERYLSTDLYK TVEEGTKQQV LDSLLL
//
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