ID   CYSK_MAIZE              Reviewed;         325 AA.
AC   P80608;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 130.
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;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. B73; TISSUE=Root;
RA   Brander K.A., Owttrim G.W., Brunold C.;
RT   "Isolation of a cDNA encoding a putative chloroplastic isoform of cysteine
RT   synthase from maize.";
RL   (er) Plant Gene Register PGR95-031(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 11-25.
RC   TISSUE=Coleoptile;
RX   AGRICOLA=IND20551642; DOI=10.1007/BF00224104;
RA   Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., Pernollet J.-C.,
RA   Zivy M., de Vienne D.;
RT   "The maize two dimensional gel protein database: towards an integrated
RT   genome analysis program.";
RL   Theor. Appl. Genet. 93:997-1005(1996).
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; X85803; CAA59798.1; -; mRNA.
DR   PIR; S52738; S52738.
DR   RefSeq; NP_001105469.2; NM_001111999.2.
DR   AlphaFoldDB; P80608; -.
DR   SMR; P80608; -.
DR   STRING; 4577.GRMZM2G005887_P03; -.
DR   PaxDb; P80608; -.
DR   PRIDE; P80608; -.
DR   GeneID; 542438; -.
DR   KEGG; zma:542438; -.
DR   MaizeGDB; 123922; -.
DR   eggNOG; KOG1252; Eukaryota.
DR   OrthoDB; 1016546at2759; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P80608; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central.
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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..325
FT                   /note="Cysteine synthase"
FT                   /id="PRO_0000167120"
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"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   325 AA;  34207 MW;  3213A69326D7CEED CRC64;
     MGEASPSIAK DVTELIGNTP LVYLNKVTDG CVGRSRAKLE SMEPCSSVKD RIGYSMITDA
     EEKGLITPGV SVLIEPTSGN TGIGLAFMAA AKGYKLTLTM PASMSMERRI ILKAFGAELV
     LTDPLLGMKG AVKKAEEIQA KTPNSYILQQ FENPANPKIH YETTGPEIWK ATAGKIDGLV
     SGIGTGGTIT GTGRYLREQN PNVKLYGVEP VESAVLNGGK PGPHKIQGIG AGFIPGVLDV
     DLLDETLQVS SDEAIETAKA LALKEGLLVG ISSGAAAAAA VRLAKRPENA GKLFVVVFPS
     FGERYLSSVL FQSIKKEAES MVVEP