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Database: UniProt
Entry: W1NDT2_AMBTC
LinkDB: W1NDT2_AMBTC
Original site: W1NDT2_AMBTC 
ID   W1NDT2_AMBTC            Unreviewed;       330 AA.
AC   W1NDT2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985};
DE            EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985};
GN   ORFNames=AMTR_s00004p00055080 {ECO:0000313|EMBL:ERM93521.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERM93521.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC         Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC         Evidence={ECO:0000256|RuleBase:RU003985};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR605856-50, ECO:0000256|RuleBase:RU003985};
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000256|ARBA:ARBA00007103,
CC       ECO:0000256|RuleBase:RU003985}.
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DR   EMBL; KI397628; ERM93521.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1NDT2; -.
DR   STRING; 13333.W1NDT2; -.
DR   EnsemblPlants; ERM93521; ERM93521; AMTR_s00004p00055080.
DR   Gramene; ERM93521; ERM93521; AMTR_s00004p00055080.
DR   eggNOG; KOG1252; Eukaryota.
DR   HOGENOM; CLU_021018_1_0_1; -.
DR   OMA; MWGAEII; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR005856; Cys_synth.
DR   InterPro; IPR005859; CysK.
DR   InterPro; IPR001216; P-phosphate_BS.
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:SF246; CYSTEINE SYNTHASE; 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;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003985};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192,
KW   ECO:0000256|RuleBase:RU003985};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR605856-50,
KW   ECO:0000256|RuleBase:RU003985};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT   DOMAIN          12..296
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         80
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         184..188
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         272
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         49
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   330 AA;  34878 MW;  E86B96C186A6DBAE CRC64;
     MGEEGSAIAK DITELIGKTP LVYLNNVTDG CVARVAAKLE GMEPCSSVKD RIGYSMISDA
     EEKGLITPGQ SVLIEPTSGN TGIGLAFVAA AKGYRLIITM PTSMSLERRI ILRAFGAELV
     LTDPARGMKG AVQKAEELLE KIPNSYILQQ FENPANPKIH YETTGPEIWK GSGGKIDAFV
     SGIGTGGTVT GVGRYLKERN PEIKLFGVEP VESAILSGGK PGPHKIQGIG AGFIPGVLEV
     NILDDVIQVS SDEAVEMAKQ LALKEGLLVG ISSGAAAAAA IKLGKRPEYT GKLIVVSTAS
     FSYTFISDIG SDQRIPIFYH VKISIVLESM
//
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