CYSK_CITLA
ID CYSK_CITLA Reviewed; 325 AA.
AC Q43317;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cysteine synthase {ECO:0000303|PubMed:8280125};
DE Short=CSase;
DE EC=2.5.1.47 {ECO:0000269|PubMed:8280125, ECO:0000269|PubMed:9013806};
DE AltName: Full=Beta-PA/CSase;
DE EC=2.5.1.51 {ECO:0000269|PubMed:8280125, ECO:0000269|PubMed:9013806};
DE AltName: Full=Beta-pyrazolylalanine synthase {ECO:0000303|PubMed:8280125};
DE EC=4.2.1.50 {ECO:0000269|PubMed:8280125, ECO:0000269|PubMed:9013806};
DE AltName: Full=L-mimosine synthase;
DE EC=2.5.1.52 {ECO:0000269|PubMed:9013806};
DE AltName: Full=O-acetylserine (thiol)-lyase;
DE Short=OAS-TL;
DE AltName: Full=O-acetylserine sulfhydrylase;
OS Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Citrullus.
OX NCBI_TaxID=3654;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seedling;
RX PubMed=8041362; DOI=10.1007/bf00280187;
RA Noji M., Murakoshi I., Saito K.;
RT "Molecular cloning of a cysteine synthase cDNA from Citrullus vulgaris
RT (watermelon) by genetic complementation in an Escherichia coli Cys-
RT auxotroph.";
RL Mol. Gen. Genet. 244:57-66(1994).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8280125; DOI=10.1006/bbrc.1993.2592;
RA Noji M., Murakoshi I., Saito K.;
RT "Evidence for identity of beta-pyrazolealanine synthase with cysteine
RT synthase in watermelon: formation of beta-pyrazole-alanine by cloned
RT cysteine synthase in vitro and in vivo.";
RL Biochem. Biophys. Res. Commun. 197:1111-1117(1993).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9013806; DOI=10.1248/bpb.20.47;
RA Saito K., Kimura N., Ikegami F., Noji M.;
RT "Production of plant non-protein amino acids by recombinant enzymes of
RT sequential biosynthetic reactions in bacteria.";
RL Biol. Pharm. Bull. 20:47-53(1997).
CC -!- FUNCTION: Produces L-cysteine from O-acetyl-L-serine and hydrogen
CC sulfide. Can also use pyrazole and 3,4-dihydroxypyridine instead of the
CC hydrogen sulfide to produce two plant specific non-protein amino acids
CC beta-pyrazolylalanine and L-mimosine. {ECO:0000269|PubMed:8280125,
CC ECO:0000269|PubMed:9013806}.
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 Evidence={ECO:0000269|PubMed:8280125, ECO:0000269|PubMed:9013806};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O-acetyl-L-serine + pyrazole = 3-(pyrazol-1-yl)-L-alanine +
CC acetate + H(+); Xref=Rhea:RHEA:13117, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17241, ChEBI:CHEBI:30089, ChEBI:CHEBI:57747,
CC ChEBI:CHEBI:58340; EC=2.5.1.51; Evidence={ECO:0000269|PubMed:8280125,
CC ECO:0000269|PubMed:9013806};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine + pyrazole = 3-(pyrazol-1-yl)-L-alanine + H2O;
CC Xref=Rhea:RHEA:24512, ChEBI:CHEBI:15377, ChEBI:CHEBI:17241,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57747; EC=4.2.1.50;
CC Evidence={ECO:0000269|PubMed:8280125, ECO:0000269|PubMed:9013806};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxypyridine + O-acetyl-L-serine = 3-(3,4-
CC dihydroxypyridin-1-yl)-L-alanine + acetate + H(+);
CC Xref=Rhea:RHEA:12693, ChEBI:CHEBI:15378, ChEBI:CHEBI:29053,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:58340, ChEBI:CHEBI:77848; EC=2.5.1.52;
CC Evidence={ECO:0000269|PubMed:9013806};
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. {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; D28777; BAA05965.1; -; mRNA.
DR PIR; S46438; S46438.
DR AlphaFoldDB; Q43317; -.
DR SMR; Q43317; -.
DR PRIDE; Q43317; -.
DR EnsemblPlants; Cla97C02G042210.1; Cla97C02G042210.1; Cla97C02G042210.
DR Gramene; Cla97C02G042210.1; Cla97C02G042210.1; Cla97C02G042210.
DR KEGG; ag:BAA05965; -.
DR UniPathway; UPA00136; UER00200.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047458; F:beta-pyrazolylalanine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050461; F:L-mimosine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050234; F:pyrazolylalanine 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; Lyase;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..325
FT /note="Cysteine synthase"
FT /id="PRO_0000167119"
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; 34343 MW; 4A91E6F8AFB5F539 CRC64;
MADAKSTIAK DVTELIGNTP LVYLNRVVDG CVARVAAKLE MMEPCSSVKD RIGYSMISDA
ENKGLITPGE SVLIEPTSGN TGIGLAFIAA AKGYRLIICM PASMSLERRT ILRAFGAELV
LTDPARGMKG AVQKAEEIKA KTPNSYILQQ FENPANPKIH YETTGPEIWR GSGGKIDALV
SGIGTGGTVT GAGKYLKEQN PNIKLYGVEP VESAILSGGK PGPHKIQGIG AGFIPGVLDV
NLLDEVIQVS SEESIETAKL LALKEGLLVG ISSGAAAAAA IRIAKRPENA GKLIVAVFPS
FGERYLSTVL FESVKRETEN MVFEP
