ID   CYSKP_CAPAN             Reviewed;         374 AA.
AC   P31300;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 105.
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   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Lamuyo; TISSUE=Fruit;
RX   PubMed=1381358; DOI=10.1016/s0021-9258(19)37137-6;
RA   Roemer S., D'Harlingue A., Camara B., Schantz R., Kuntz M.;
RT   "Cysteine synthase from Capsicum annuum chromoplasts. Characterization and
RT   cDNA cloning of an up-regulated enzyme during fruit development.";
RL   J. Biol. Chem. 267:17966-17970(1992).
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: Plastid, chloroplast stroma. Plastid,
CC       chromoplast.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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DR   EMBL; X64874; CAA46086.1; -; mRNA.
DR   PIR; A43407; A43407.
DR   AlphaFoldDB; P31300; -.
DR   SMR; P31300; -.
DR   PRIDE; P31300; -.
DR   EnsemblPlants; PHT95606; PHT95606; T459_03488.
DR   Gramene; PHT95606; PHT95606; T459_03488.
DR   OMA; RTPVFKF; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000189700; Genome assembly.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0009509; C:chromoplast; 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   Amino-acid biosynthesis; Chloroplast; Chromoplast; Cysteine biosynthesis;
KW   Plastid; Pyridoxal phosphate; Transferase; Transit peptide.
FT   TRANSIT         1..50
FT                   /note="Chloroplast and chromoplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           51..374
FT                   /note="Cysteine synthase, chloroplastic/chromoplastic"
FT                   /id="PRO_0000006350"
FT   BINDING         139
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         243..247
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         108
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   374 AA;  39978 MW;  36A6D0CDCCEA23F1 CRC64;
     MASIINNPFT SLCCNTNKCE PNRICSLRSQ QSLVFDNVNR KVGFPSVVCK AVSVQTKSPT
     EIEGLNIAED VTQLIGNTPM VYLNTIVKGC VANIAAKLEI MEPCCSVKDR IGFSMISDAE
     EKGLISPGKT VLVEPTSGNT GIGLAFIAAS RGYKLILTMP ASMSLERRVI LKAFGAELVL
     TDPAKGMKGA VSKAEEILNN TPDAYILQQF DNPANPKIHY ETTGPEIWED TKGKIDILVA
     GIGTGGTISG TGRYLKEKNP NIKIIGVEPT ESNVLSGGKP GFIPGNLDQD VMDEVIEISS
     DEAVETAKQL ALQEGLLVGI SSGAAALAAI QVAKRPENAG KLIAVVFPSF GERYLSSILF
     QSIREECEKM KPEL