CYSK2_CAEEL
ID CYSK2_CAEEL Reviewed; 337 AA.
AC O45679;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Bifunctional L-3-cyanoalanine synthase/cysteine synthase {ECO:0000250|UniProtKB:Q9S757};
DE Short=CAS {ECO:0000305|PubMed:21840852};
DE EC=2.5.1.47 {ECO:0000269|PubMed:24100226};
DE EC=4.4.1.9 {ECO:0000269|PubMed:24100226};
DE AltName: Full=O-acetylserine (thiol)-lyase 2 {ECO:0000305|PubMed:24100226};
DE Short=OAS-TL {ECO:0000305|PubMed:24100226};
GN Name=cysl-2 {ECO:0000312|WormBase:K10H10.2};
GN ORFNames=K10H10.2 {ECO:0000312|WormBase:K10H10.2};
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, AND INDUCTION BY HYDROGEN SULFIDE AND CYANIDE.
RX PubMed=21840852; DOI=10.1534/genetics.111.129841;
RA Budde M.W., Roth M.B.;
RT "The response of Caenorhabditis elegans to hydrogen sulfide and hydrogen
RT cyanide.";
RL Genetics 189:521-532(2011).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
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).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=24260346; DOI=10.1371/journal.pone.0080135;
RA Qabazard B., Ahmed S., Li L., Arlt V.M., Moore P.K., Sturzenbaum S.R.;
RT "C. elegans aging is modulated by hydrogen sulfide and the
RT sulfhydrylase/cysteine synthase cysl-2.";
RL PLoS ONE 8:E80135-E80135(2013).
CC -!- FUNCTION: Primarily catalyzes the formation of cyanoalanine and
CC hydrogen sulfide from cysteine and hydrogen cyanide. Can also catalyze,
CC although less efficiently, the formation of cyanoalanine and hydrogen
CC sulfide from either S-sulfocysteine or O-acetylserine and hydrogen
CC cyanide and the formation of cysteine from either S-sulfocysteine or O-
CC acetylserine and hydrogen sulfide (PubMed:24100226). By catalyzing the
CC assimilation of cyanide produced by P.aeruginosa, mediates resistance
CC to infection (PubMed:21840852). Involved in fertility, growth and aging
CC (PubMed:24260346). Does not mediate survival in high levels of hydrogen
CC sulfide (PubMed:21840852). {ECO:0000269|PubMed:21840852,
CC ECO:0000269|PubMed:24100226, ECO:0000269|PubMed:24260346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen cyanide + L-cysteine = 3-cyano-L-alanine + H(+) +
CC hydrogen sulfide; Xref=Rhea:RHEA:17821, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18407, ChEBI:CHEBI:29919, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:77860; EC=4.4.1.9;
CC Evidence={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=1.9 mM for O-acetylserine (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:24100226};
CC KM=0.4 mM for S-sulfocysteine (at 25 degrees Celsius, pH 8.5 and in
CC absence of dithiothreitol) {ECO:0000269|PubMed:24100226};
CC KM=1.2 mM for cysteine (at 25 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:24100226};
CC KM=1.4 mM for sulfide (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:24100226};
CC KM=0.8 mM for cyanide (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:24100226};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24100226}.
CC -!- INDUCTION: By hydrogen sulfide or cyanide (PubMed:21840852). By
CC morpholin-4-ium 4-methoxyphenyl (morpholino) phosphinodithioate
CC (GYY4137) (PubMed:24260346). {ECO:0000269|PubMed:21840852,
CC ECO:0000269|PubMed:24260346}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; Z83236; CAB05778.1; -; Genomic_DNA.
DR PIR; T23591; T23591.
DR RefSeq; NP_497008.1; NM_064607.4.
DR AlphaFoldDB; O45679; -.
DR SMR; O45679; -.
DR DIP; DIP-25454N; -.
DR IntAct; O45679; 1.
DR STRING; 6239.K10H10.2.1; -.
DR World-2DPAGE; 0011:O45679; -.
DR EPD; O45679; -.
DR PaxDb; O45679; -.
DR PeptideAtlas; O45679; -.
DR EnsemblMetazoa; K10H10.2.1; K10H10.2.1; WBGene00010759.
DR GeneID; 175107; -.
DR KEGG; cel:CELE_K10H10.2; -.
DR UCSC; K10H10.2.1; c. elegans.
DR CTD; 175107; -.
DR WormBase; K10H10.2; CE16252; WBGene00010759; cysl-2.
DR eggNOG; KOG1252; Eukaryota.
DR GeneTree; ENSGT00970000196576; -.
DR HOGENOM; CLU_021018_1_0_1; -.
DR InParanoid; O45679; -.
DR OMA; FWDSGER; -.
DR OrthoDB; 1016546at2759; -.
DR PhylomeDB; O45679; -.
DR BRENDA; 2.5.1.47; 1045.
DR SABIO-RK; O45679; -.
DR PRO; PR:O45679; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00010759; 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:0050017; F:L-3-cyanoalanine 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; Lyase; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..337
FT /note="Bifunctional L-3-cyanoalanine synthase/cysteine
FT synthase"
FT /id="PRO_0000433014"
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; 36154 MW; 8DE4681F8001F228 CRC64;
MSRELMVETG GELIGNTPLL KLNKIGKDLG ASIAVKVEYM NPACSVKDRI AFNMIDTAEK
AGLITPGKTV LIEPTSGNMG IALAYCGKLR GYKVILTMPA SMSIERRCLL KAYGAEVILT
DPATAVKGAV QRAEELRDVI PNAYILNQFG NPANPEAHYK TTGPEIWRQT QGKVDIVCFG
VGSGGTCTGV GRFLKEKNPS VQVFPVEPFE SSVINGLPHS PHKIQGMGTG MIPDILDLTL
FSEALRVHSD DAIAMAKKLA DEESILGGIS SGANVCAAVQ LAKRPENKGK LIVTTVNSFG
ERYLSTALYA ELRDNAANMK QLNLDDSIKI AKEYLGI
