CYSK3_CAEEL
ID CYSK3_CAEEL Reviewed; 337 AA.
AC O01592; H2L0J5; Q86NC6;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cysteine synthase 3 {ECO:0000305};
DE EC=2.5.1.47 {ECO:0000269|PubMed:24100226};
DE AltName: Full=O-acetylserine (thiol)-lyase 3 {ECO:0000305|PubMed:24100226};
DE Short=OAS-TL {ECO:0000305|PubMed:24100226};
GN Name=cysl-3 {ECO:0000312|WormBase:R08E5.2};
GN ORFNames=R08E5.2 {ECO:0000312|WormBase:R08E5.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24100226; DOI=10.1016/j.bbapap.2013.09.020;
RA Vozdek R., Hnizda A., Krijt J., Sera L., Kozich V.;
RT "Biochemical properties of nematode O-acetylserine(thiol)lyase paralogs
RT imply their distinct roles in hydrogen sulfide homeostasis.";
RL Biochim. Biophys. Acta 1834:2691-2701(2013).
CC -!- FUNCTION: Primarily catalyzes the formation of cysteine and acetate
CC from O-acetylserine and hydrogen sulfide. Can also catalyze the
CC formation of cysteine and acetate from S-sulfocysteine and hydrogen
CC sulfide and the formation of cyanoalanine and hydrogen sulfide from
CC either S-sulfocysteine or O-acetylserine and hydrogen cyanide.
CC {ECO:0000269|PubMed:24100226}.
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:24100226};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:24100226};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.7 mM for O-acetylserine (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:24100226};
CC KM=6.5 mM for S-sulfocysteine (at 25 degrees Celsius, pH 8.5 and in
CC absence of dithiothreitol) {ECO:0000269|PubMed:24100226};
CC KM=1.6 mM for sulfide (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:24100226};
CC KM=2.4 mM for cyanide (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:24100226};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24100226}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; FO081677; CCD73276.1; -; Genomic_DNA.
DR PIR; C89009; C89009.
DR RefSeq; NP_504046.1; NM_071645.5.
DR AlphaFoldDB; O01592; -.
DR SMR; O01592; -.
DR STRING; 6239.R08E5.2a; -.
DR EPD; O01592; -.
DR PaxDb; O01592; -.
DR PeptideAtlas; O01592; -.
DR EnsemblMetazoa; R08E5.2.1; R08E5.2.1; WBGene00019962.
DR GeneID; 259617; -.
DR KEGG; cel:CELE_R08E5.2; -.
DR UCSC; R08E5.2a; c. elegans.
DR CTD; 259617; -.
DR WormBase; R08E5.2; CE12574; WBGene00019962; cysl-3.
DR eggNOG; KOG1252; Eukaryota.
DR GeneTree; ENSGT00970000196093; -.
DR InParanoid; O01592; -.
DR OMA; GIRRWPE; -.
DR OrthoDB; 1016546at2759; -.
DR PhylomeDB; O01592; -.
DR SABIO-RK; O01592; -.
DR UniPathway; UPA00136; UER00200.
DR PRO; PR:O01592; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00019962; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:WormBase.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IDA:WormBase.
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; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..337
FT /note="Cysteine synthase 3"
FT /id="PRO_0000433015"
FT BINDING 78
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P9WP55"
FT BINDING 182..186
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P9WP55"
FT BINDING 270
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P9WP55"
FT MOD_RES 47
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P9WP55"
SQ SEQUENCE 337 AA; 36268 MW; 605581D269D90188 CRC64;
MSRELMVQDS GDTIGNTPLV LLRNISKGLD ARIAVKVEYL NPSCSVKDRI AKSMVDEAEK
AGTIVPGKTV LVEGTSGNLG IALAHIGKIR GYKVILVMPA TMSVERRAML RAYGAEVILS
DPAEGHPGVI KKVEMLVDKL PNAHCLDQFS NPANPAAHYR TTGPEIWRQT EGKVDIVCFG
VGSSGTVTGV GRYLREQNPN IEIYPVEPYE SSVLSGLPRG PHKIQGIGAG IVPGNVDRSL
FTEILRIKSD DAMQMARRLA DEEAILGGIS SGANVVAAVE LASRPENKGK LIVTTVNSFA
ERYFTTELYS DVLNEVSQLT FSSDDEAMGI AKKYLGL
