ID   CYSKP_SOLTU             Reviewed;         386 AA.
AC   O81155;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Cysteine synthase, chloroplastic/chromoplastic;
DE            EC=2.5.1.47;
DE   AltName: Full=CSase B;
DE            Short=CS-B;
DE   AltName: Full=O-acetylserine (thiol)-lyase;
DE   AltName: Full=O-acetylserine sulfhydrylase;
DE   AltName: Full=OAS-TL B;
DE   Flags: Precursor;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Berolina;
RA   Hesse H., Hoefgen R.;
RT   "Isolation of cDNAs encoding cytosolic and plastidic cysteine synthase
RT   isoforms from Solanum tuberosum.";
RL   (er) Plant Gene Register PGR98-057(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: Plastid, chloroplast stroma {ECO:0000250}.
CC       Plastid, chromoplast {ECO:0000250}.
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; AF044173; AAC25636.1; -; mRNA.
DR   PIR; T07002; T07002.
DR   AlphaFoldDB; O81155; -.
DR   SMR; O81155; -.
DR   STRING; 4113.PGSC0003DMT400059624; -.
DR   eggNOG; KOG1252; Eukaryota.
DR   BRENDA; 2.5.1.47; 5757.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; O81155; baseline.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0009509; C:chromoplast; IEA:UniProtKB-SubCell.
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   GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IBA:GO_Central.
DR   GO; GO:0009860; P:pollen tube growth; 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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Chloroplast; Chromoplast; Cysteine biosynthesis;
KW   Plastid; Pyridoxal phosphate; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..52
FT                   /note="Chloroplast and chromoplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           53..386
FT                   /note="Cysteine synthase, chloroplastic/chromoplastic"
FT                   /id="PRO_0000006351"
FT   BINDING         141
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         245..249
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         110
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   386 AA;  41044 MW;  8EB3FEB2084D9594 CRC64;
     MASFINNPLT SLCNTKSERN NLFKISLYEA QSLGFSKLNG SRKVAFPSVV CKAVSVPTKS
     STEIEGLNIA EDVTQLIGNT PMVYLNTIAK GCVANIAAKL EIMEPCCSVK DRIGFSMIVD
     AEEKGLISPG KTVLVEPTSG NTGIGLAFIA ASRGYKLILT MPASMSLERR VILKAFGAEL
     VLTDPAKGMK GAVSKAEEIL NNTPDAYILQ QFDNPANPKI HYETTGPEIW EDTKGKIDIL
     VAGIGTGGTI TGTGRFLKEQ NPNIKIIGVE PTESNVLSGG KPGPHKIQGI GAGFIPGNLD
     QDVMDEVIEI SSDEAVETAR TLALQEGLLV GISSGAAALA AIQVGKRPEN AGKLIGVVFP
     SYGERYLSSI LFQSIREECE KMKPEL