ID   CYSK_DICDI              Reviewed;         378 AA.
AC   Q54CN7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Cysteine synthase;
DE            Short=CSase;
DE            EC=2.5.1.47;
DE   AltName: Full=O-acetylserine (thiol)-lyase;
DE            Short=OAS-TL;
DE   AltName: Full=O-acetylserine sulfhydrylase;
GN   Name=cysK; ORFNames=DDB_G0292840;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 2/2.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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DR   EMBL; AAFI02000197; EAL60969.1; -; Genomic_DNA.
DR   RefSeq; XP_629379.1; XM_629377.1.
DR   AlphaFoldDB; Q54CN7; -.
DR   SMR; Q54CN7; -.
DR   STRING; 44689.DDB0230066; -.
DR   PaxDb; Q54CN7; -.
DR   EnsemblProtists; EAL60969; EAL60969; DDB_G0292840.
DR   GeneID; 8628897; -.
DR   KEGG; ddi:DDB_G0292840; -.
DR   dictyBase; DDB_G0292840; cysK.
DR   eggNOG; KOG1481; Eukaryota.
DR   HOGENOM; CLU_021018_1_0_1; -.
DR   InParanoid; Q54CN7; -.
DR   OMA; WMADYGF; -.
DR   PhylomeDB; Q54CN7; -.
DR   UniPathway; UPA00136; UER00200.
DR   PRO; PR:Q54CN7; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004124; F:cysteine synthase activity; ISS:dictyBase.
DR   GO; GO:0019344; P:cysteine biosynthetic process; ISS:dictyBase.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   Gene3D; 3.40.50.1100; -; 2.
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   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..378
FT                   /note="Cysteine synthase"
FT                   /id="PRO_0000328233"
FT   REGION          10..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         215..219
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         79
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  41101 MW;  56CDA9DF8ABD272D CRC64;
     MFSSIYGYFN SEGDSNQQQN NNNNSNNNLK ESVFHSGISN GIIETVGNTP LIRIKSLSEA
     TGCEIYGKAE FMNPGGSPKD RVAREIILDG EKKGLLKKGS TIVEATAGST GISLTMLGKS
     RGYNVQLFIP DNVSKEKVDL LEMLGAETKI VPIVGMNNAN HFMHCAYQRC LGDDMAFYAN
     QFDNLSNFNA HYNGTAKEIW EQTKGDVDGF VAAAGTGGTV AGISSYLKEV NPNIQNWLID
     PPGSGLYSLV NTGVIFHPKD RLVVEKLGPR SFYEGVGVNK KTENFNKASL NGAFRGTEEE
     GVDMAHYLLK HDGLFLGGSS ALNCVGAVKL ARKLGPGKTI VTVLCDSGHR YTSRLYSKSW
     LNDHNFQVSD LSNLNFVK