ID   CYSK1_BRAJU             Reviewed;         322 AA.
AC   O23733;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Cysteine synthase;
DE            Short=CSase;
DE            EC=2.5.1.47;
DE   AltName: Full=O-acetylserine (thiol)-lyase;
DE            Short=OAS-TL;
DE   AltName: Full=O-acetylserine sulfhydrylase;
DE   AltName: Full=OAS-TL4;
OS   Brassica juncea (Indian mustard) (Sinapis juncea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3707;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Vittasso; TISSUE=Root;
RX   PubMed=9620267; DOI=10.1023/a:1005929022061;
RA   Schaefer H.J., Haag-Kerwer A., Rausch T.H.;
RT   "cDNA cloning and expression analysis of genes encoding GSH synthesis in
RT   roots of the heavy-metal accumulator Brassica juncea L.: evidence for Cd-
RT   induction of a putative mitochondrial gamma-glutamylcysteine synthetase
RT   isoform.";
RL   Plant Mol. Biol. 37:87-97(1998).
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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DR   EMBL; Y10845; CAA71798.1; -; mRNA.
DR   AlphaFoldDB; O23733; -.
DR   SMR; O23733; -.
DR   PRIDE; O23733; -.
DR   UniPathway; UPA00136; UER00200.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
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; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01139; cysK; 1.
DR   TIGRFAMs; TIGR01136; cysKM; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW   Phosphoprotein; Pyridoxal phosphate; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P47998"
FT   CHAIN           2..322
FT                   /note="Cysteine synthase"
FT                   /id="PRO_0000167117"
FT   BINDING         77
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         181..185
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P47998"
FT   MOD_RES         46
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         178
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47998"
SQ   SEQUENCE   322 AA;  33902 MW;  28DA67631EF0ABF2 CRC64;
     MASRIAKDVT ELIGNTPLVY LNNVAEGCVG RVAAKLEMME PCSSVKDRIG FSMISDAEQK
     GLIKPGESVL IEPTSGNTGV GLAFTAAAKG YKLIITMPAS MSVERRIILL AFGVELVLTD
     PAKGMKGAIA KAEEILAKTP NGYMLQQFEN PANPKIHYET TGPEIWKGTD GKIDGFVSGI
     GTGGTITGAG KYLKEQNPNV KLYGVEPIES AILSGGKPGP HKIQGIGAGF IPSVLEVDLI
     DEVVQVSSDE SIDMARLLAL KEGLLVGISS GAAAAAAIKL AKRPENAGKL FVAVFPSFGE
     RYLSTVLFDA TRKEAESMTF QA