ID   CYSK_SPIOL              Reviewed;         325 AA.
AC   Q00834;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Cysteine synthase;
DE            EC=2.5.1.47;
DE   AltName: Full=CSase A;
DE   AltName: Full=O-acetylserine (thiol)-lyase;
DE            Short=OAS-TL A;
DE   AltName: Full=O-acetylserine sulfhydrylase;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 5-11; 71-90; 163-182
RP   AND 246-262.
RC   STRAIN=cv. Parade; TISSUE=Leaf;
RX   PubMed=1518833; DOI=10.1073/pnas.89.17.8078;
RA   Saito K., Miura N., Yamazaki M., Hirano H., Murakoshi I.;
RT   "Molecular cloning and bacterial expression of cDNA encoding a plant
RT   cysteine synthase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:8078-8082(1992).
RN   [2]
RP   MUTAGENESIS OF LYSINE RESIDUES.
RX   PubMed=8344414; DOI=10.1016/0014-5793(93)80976-2;
RA   Saito K., Kurosawa M., Murakoshi I.;
RT   "Determination of a functional lysine residue of a plant cysteine synthase
RT   by site-directed mutagenesis, and the molecular evolutionary
RT   implications.";
RL   FEBS Lett. 328:111-114(1993).
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   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 2/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Leaves and roots.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D10476; BAA01279.1; -; mRNA.
DR   PIR; S35094; S35094.
DR   AlphaFoldDB; Q00834; -.
DR   SMR; Q00834; -.
DR   PRIDE; Q00834; -.
DR   OrthoDB; 1016546at2759; -.
DR   SABIO-RK; Q00834; -.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW   Direct protein sequencing; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..325
FT                   /note="Cysteine synthase"
FT                   /id="PRO_0000167125"
FT   BINDING         80
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         184..188
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         49
FT                   /note="N6-(pyridoxal phosphate)lysine"
SQ   SEQUENCE   325 AA;  34187 MW;  161B46F7B670DEE6 CRC64;
     MVEEKAFIAK DVTELIGKTP LVYLNTVADG CVARVAAKLE GMEPCSSVKD RIGFSMITDA
     EKSGLITPGE SVLIEPTSGN TGIGLAFIAA AKGYKLIITM PASMSLERRT ILRAFGAELI
     LTDPAKGMKG AVQKAEEIRD KTPNSYILQQ FENPANPKVH YETTGPEIWK GTGGKIDIFV
     SGIGTGGTIT GAGKYLKEQN PDVKLIGLEP VESAVLSGGK PGPHKIQGLG AGFIPGVLDV
     NIIDEVVQIS SEESIEMAKL LALKEGLLVG ISSGAAAAAA IKVAKRPENA GKLIVAVFPS
     FGERYLSSVL FDSVRKEAES MVIES