CYSK1_CAEEL
ID CYSK1_CAEEL Reviewed; 341 AA.
AC Q93244;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cysteine synthase 1 {ECO:0000305};
DE EC=2.5.1.47 {ECO:0000269|PubMed:24100226};
DE AltName: Full=O-acetylserine (thiol)-lyase 1 {ECO:0000305|PubMed:24100226};
DE Short=OAS-TL {ECO:0000305|PubMed:24100226};
GN Name=cysl-1 {ECO:0000312|WormBase:C17G1.7};
GN ORFNames=C17G1.7 {ECO:0000312|WormBase:C17G1.7};
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 MUTAGENESIS OF SER-144; GLY-181; GLY-229; SER-272 AND
RP THR-295.
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, INTERACTION WITH EGL-9, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP PRO-75; ALA-88; GLY-181; GLY-183 AND ARG-259.
RX PubMed=22405203; DOI=10.1016/j.neuron.2011.12.037;
RA Ma D.K., Vozdek R., Bhatla N., Horvitz H.R.;
RT "CYSL-1 interacts with the O2-sensing hydroxylase EGL-9 to promote H2S-
RT modulated hypoxia-induced behavioral plasticity in C. elegans.";
RL Neuron 73:925-940(2012).
RN [4] {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).
CC -!- FUNCTION: Catalyzes the formation of cysteine and acetate from O-
CC acetylserine and hydrogen sulfide (PubMed:24100226, PubMed:22405203).
CC By metabolizing hydrogen sulfide produced by cysl-2-mediated cyanide
CC assimilation, mediates resistance to P.aeruginosa infection
CC (PubMed:21840852). Mediates survival in high levels of hydrogen sulfide
CC (PubMed:22405203). By sequestering egl-9, which in turn promotes hif-1-
CC mediated transcription, regulates behavioral responses to hypoxia
CC (PubMed:22405203). {ECO:0000269|PubMed:21840852,
CC ECO:0000269|PubMed:22405203, 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=7.4 mM for O-acetylserine {ECO:0000269|PubMed:22405203};
CC KM=1 mM for O-acetylserine (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:24100226};
CC KM=4.6 mM for sulfide {ECO:0000269|PubMed:22405203};
CC KM=1.7 mM for sulfide (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:24100226};
CC KM=9.3 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 (PubMed:24100226). Interacts with egl-9 (via C-
CC terminus); the interaction is enhanced by hydrogen disulfide and
CC activates hif-1-mediated transcription (PubMed:22405203).
CC {ECO:0000269|PubMed:22405203, ECO:0000269|PubMed:24100226}.
CC -!- INTERACTION:
CC Q93244; G5EBV0: egl-9; NbExp=3; IntAct=EBI-2413537, EBI-2004151;
CC -!- TISSUE SPECIFICITY: Expressed in AVM sensory neuron, BDU interneurons,
CC pharyngeal I1 interneurons and M2 motor neurons.
CC {ECO:0000269|PubMed:22405203}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; Z78415; CAB01676.2; -; Genomic_DNA.
DR PIR; T19367; T19367.
DR RefSeq; NP_509670.2; NM_077269.4.
DR AlphaFoldDB; Q93244; -.
DR SMR; Q93244; -.
DR IntAct; Q93244; 2.
DR STRING; 6239.C17G1.7; -.
DR EPD; Q93244; -.
DR PaxDb; Q93244; -.
DR PeptideAtlas; Q93244; -.
DR EnsemblMetazoa; C17G1.7.1; C17G1.7.1; WBGene00007653.
DR GeneID; 181209; -.
DR UCSC; C17G1.7.1; c. elegans.
DR CTD; 181209; -.
DR WormBase; C17G1.7; CE39223; WBGene00007653; cysl-1.
DR eggNOG; KOG1252; Eukaryota.
DR GeneTree; ENSGT00970000196576; -.
DR HOGENOM; CLU_021018_1_0_1; -.
DR InParanoid; Q93244; -.
DR OMA; RTPVFKF; -.
DR OrthoDB; 1016546at2759; -.
DR PhylomeDB; Q93244; -.
DR BRENDA; 2.5.1.47; 1045.
DR SABIO-RK; Q93244; -.
DR UniPathway; UPA00136; UER00200.
DR PRO; PR:Q93244; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00007653; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; HDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; HDA:WormBase.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:WormBase.
DR GO; GO:0019899; F:enzyme binding; IPI: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 GO; GO:0001666; P:response to hypoxia; IMP: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..341
FT /note="Cysteine synthase 1"
FT /id="PRO_0000433013"
FT BINDING 79
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P9WP55"
FT BINDING 183..187
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P9WP55"
FT BINDING 271
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P9WP55"
FT MOD_RES 48
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P9WP55"
FT MUTAGEN 75
FT /note="P->L: In n5537; severe loss of protein stability."
FT /evidence="ECO:0000269|PubMed:22405203"
FT MUTAGEN 88
FT /note="A->V: In n5522; severe loss of protein stability."
FT /evidence="ECO:0000269|PubMed:22405203"
FT MUTAGEN 144
FT /note="S->F: In mr26; susceptible to high levels of
FT hydrogen sulfide."
FT /evidence="ECO:0000269|PubMed:21840852"
FT MUTAGEN 181
FT /note="G->E: In n5521 and mr23; severe loss of protein
FT stability. Susceptible to high levels of hydrogen sulfide."
FT /evidence="ECO:0000269|PubMed:21840852,
FT ECO:0000269|PubMed:22405203"
FT MUTAGEN 183
FT /note="G->R: In n5515; severe loss of protein stability."
FT /evidence="ECO:0000269|PubMed:22405203"
FT MUTAGEN 229
FT /note="G->E: In mr33; susceptible to high levels of
FT hydrogen sulfide."
FT /evidence="ECO:0000269|PubMed:21840852"
FT MUTAGEN 259
FT /note="R->K: In n5519; no loss of protein stability. No
FT effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:22405203"
FT MUTAGEN 272
FT /note="S->F: In mr29; susceptible to high levels of
FT hydrogen sulfide."
FT /evidence="ECO:0000269|PubMed:21840852"
FT MUTAGEN 295
FT /note="T->I: In mr39; susceptible to high levels of
FT hydrogen sulfide."
FT /evidence="ECO:0000269|PubMed:21840852"
SQ SEQUENCE 341 AA; 35903 MW; CC8AF917CEABBA2F CRC64;
MADRNSIGEN AAALIGNTPM VYINKLTKGL PGTVAVKIEY MNPAGSVKDR IGAAMLAAAE
KDGTVIPGVT TLIEPTSGNT GIALAFVAAA KGYRCIVTMP ASMSGERRTL LKAYGSEVVL
TDPAKGMKGA IDMANQLKEN IPGSIILAQF DNPNNPLVHY QTTGPEIWRQ TKGTVDAVVF
GVGTGGTITG VGRYLQEQNP GVRVFAVEPE ESAILSGRPA GPHKIQGIGA GFAPAVLDTK
IYEDVIRIHS DEAIVMAQRL SYEEGLLGGI SSGANVAAAL QLAARPEMAG KLIVTCLPSC
GERYMTSPLY TDIRESAMAL AVESLEANLK KLCLHNYDIM E
