CYSKP_SPIOL
ID CYSKP_SPIOL Reviewed; 383 AA.
AC P32260; Q33137;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
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;
GN Name=CYSK;
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].
RX PubMed=8405359; DOI=10.1016/0014-5793(93)80127-g;
RA Saito K., Tatsuguchi K., Murakoshi I., Hirano H.;
RT "cDNA cloning and expression of cysteine synthase B localized in
RT chloroplasts of Spinacia oleracea.";
RL FEBS Lett. 324:247-252(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=8424655; DOI=10.1006/abbi.1993.1030;
RA Rolland N., Droux M., Lebrun M., Douce R.;
RT "O-acetylserine(thiol)lyase from spinach (Spinacia oleracea L.) leaf: cDNA
RT cloning, characterization, and overexpression in Escherichia coli of the
RT chloroplast isoform.";
RL Arch. Biochem. Biophys. 300:213-222(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Marathon; TISSUE=Leaf;
RX PubMed=8278530; DOI=10.1104/pp.102.3.1057;
RA Hell R., Schuster G., Gruissem W.;
RT "An O-acetylserine (thiol) lyase cDNA from spinach.";
RL Plant Physiol. 102:1057-1058(1993).
RN [4]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX PubMed=8617276; DOI=10.1111/j.1432-1033.1996.00272.x;
RA Rolland N., Ruffet M.-L., Job D., Douce R., Droux M.;
RT "Spinach chloroplast O-acetylserine (thiol)-lyase exhibits two
RT catalytically non-equivalent pyridoxal-5'-phosphate-containing active
RT sites.";
RL Eur. J. Biochem. 236:272-282(1996).
RN [5]
RP PROTEIN SEQUENCE OF 53-65, AND CHARACTERIZATION.
RX PubMed=1375015; DOI=10.1016/0003-9861(92)90531-z;
RA Droux M., Martin J., Sajus P., Douce R.;
RT "Purification and characterization of O-acetylserine (thiol) lyase from
RT spinach chloroplasts.";
RL Arch. Biochem. Biophys. 295:379-390(1992).
RN [6]
RP DISCUSSION OF SEQUENCE.
RX PubMed=7916619; DOI=10.1042/bj2930829;
RA Rolland N., Job D., Douce R.;
RT "Common sequence motifs coding for higher-plant and prokaryotic O-
RT acetylserine (thiol)-lyases: bacterial origin of a chloroplast transit
RT peptide?";
RL Biochem. J. 293:829-833(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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for O-acetylserine;
CC KM=0.25 mM for sulfide;
CC pH dependence:
CC Optimum pH is 7.5 to 8.5.;
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; D14722; BAA03542.1; -; mRNA.
DR EMBL; X66860; CAA47329.1; -; mRNA.
DR EMBL; L05184; AAA16973.1; -; mRNA.
DR PIR; S29733; S29733.
DR PIR; T09000; T09000.
DR AlphaFoldDB; P32260; -.
DR SMR; P32260; -.
DR PRIDE; P32260; -.
DR OrthoDB; 1016546at2759; -.
DR SABIO-RK; P32260; -.
DR UniPathway; UPA00136; UER00200.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Chloroplast; Chromoplast; Cysteine biosynthesis;
KW Direct protein sequencing; Plastid; Pyridoxal phosphate; Transferase;
KW Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast and chromoplast"
FT /evidence="ECO:0000269|PubMed:1375015"
FT CHAIN 53..383
FT /note="Cysteine synthase, chloroplastic/chromoplastic"
FT /id="PRO_0000006352"
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 331
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 CONFLICT 12
FT /note="L -> I (in Ref. 1; BAA03542)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="E -> EKESYLE (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 252..258
FT /note="GRYLKER -> DGTSKNA (in Ref. 3; AAA16973)"
FT /evidence="ECO:0000305"
FT CONFLICT 274..280
FT /note="ILSGGKP -> YFLVESA (in Ref. 3; AAA16973)"
FT /evidence="ECO:0000305"
FT CONFLICT 334..335
FT /note="AA -> RG (in Ref. 3; AAA16973)"
FT /evidence="ECO:0000305"
FT CONFLICT 334..335
FT /note="AA -> RR (in Ref. 2; CAA47329)"
FT /evidence="ECO:0000305"
FT CONFLICT 379..380
FT /note="NM -> KL (in Ref. 3; AAA16973)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="E -> EI (in Ref. 3; AAA16973)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 40637 MW; CE3725796D3A3F93 CRC64;
MASLVNNAYA ALRTSKLELR EVKNLANFRV GPPSSLSCNN FKKVSSSPIT CKAVSLSPPS
TIEGLNIAED VSQLIGKTPM VYLNNVSKGS VANIAAKLES MEPCCSVKDR IGYSMIDDAE
QKGVITPGKT TLVEPTSGNT GIGLAFIAAA RGYKITLTMP ASMSMERRVI LKAFGAELVL
TDPAKGMKGA VEKAEEILKK TPDSYMLQQF DNPANPKIHY ETTGPEIWED TKGKVDIFVA
GIGTGGTISG VGRYLKERNP GVQVIGIEPT ESNILSGGKP GPHKIQGLGA GFVPSNLDLG
VMDEVIEVSS EEAVEMAKQL AMKEGLLVGI SSGAAAAAAV RIGKRPENAG KLIAVVFPSF
GERYLSSILF QSIREECENM KPE
