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Database: UniProt
Entry: A0A059LLZ0_9CHLO
LinkDB: A0A059LLZ0_9CHLO
Original site: A0A059LLZ0_9CHLO 
ID   A0A059LLZ0_9CHLO        Unreviewed;       304 AA.
AC   A0A059LLZ0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985};
DE            EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985};
GN   ORFNames=H632_c738p0 {ECO:0000313|EMBL:KDD75333.1};
OS   Helicosporidium sp. ATCC 50920.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Helicosporidium.
OX   NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD75333.1, ECO:0000313|Proteomes:UP000026042};
RN   [1] {ECO:0000313|EMBL:KDD75333.1, ECO:0000313|Proteomes:UP000026042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD75333.1,
RC   ECO:0000313|Proteomes:UP000026042};
RX   PubMed=24809511;
RA   Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT   "A lack of parasitic reduction in the obligate parasitic green alga
RT   helicosporidium.";
RL   PLoS Genet. 10:E1004355-E1004355(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDD75333.1}.
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DR   EMBL; AYPS01000738; KDD75333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059LLZ0; -.
DR   STRING; 1291522.A0A059LLZ0; -.
DR   OrthoDB; 5487987at2759; -.
DR   Proteomes; UP000026042; Unassembled WGS sequence.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
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:SF241; CYSTEINE SYNTHASE, MITOCHONDRIAL; 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:UP000026042};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT   DOMAIN          2..279
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         60
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         164..168
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         252
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         29
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   304 AA;  31925 MW;  47000BAE65DE2051 CRC64;
     MVFLDKVTRG AGARVAAKLE IMEPCSSVKD RIGYSMIMEA EKAGRIVPGK TTLVEPTSGN
     TGIALAFISA ARGYRLVLTM PASMSLERRI LLRAFGAELI LTDPAKGMKG AVAKAEEIAA
     TIPDSYILQQ FDNPANPKVH YETTGPEIWK DTEGRVDIFV AGVGTGGTIT GTGRFLKKQS
     PSVQIVAVEP LESPVIGGGE PGPHMIQGIG AGFVPKNLDM SIVDEVLAVG SSEAMVAARR
     LASEEGLLVG VSSGAALVAA DKLARRPENA GKLIVTVLPS MGERYLSSAL FQDLRSAAET
     MSVE
//
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