CYSK1_ORYSJ
ID CYSK1_ORYSJ Reviewed; 321 AA.
AC Q9XEA6; Q0ILS7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
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=RCS1; OrderedLocusNames=Os12g0625000, LOC_Os12g42980;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=10095115; DOI=10.1016/s0378-1119(99)00019-0;
RA Nakamura T., Yamaguchi Y., Sano H.;
RT "Four rice genes encoding cysteine synthase: isolation and differential
RT responses to sulfur, nitrogen and light.";
RL Gene 229:155-161(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
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 -!- 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; AF073695; AAD23907.1; -; mRNA.
DR EMBL; AP008218; BAF30338.1; -; Genomic_DNA.
DR EMBL; AP014968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q9XEA6; -.
DR SMR; Q9XEA6; -.
DR STRING; 4530.OS12T0625000-01; -.
DR PaxDb; Q9XEA6; -.
DR PRIDE; Q9XEA6; -.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_021018_1_1_1; -.
DR InParanoid; Q9XEA6; -.
DR BRENDA; 2.5.1.47; 4460.
DR PlantReactome; R-OSA-1119331; Cysteine biosynthesis I.
DR UniPathway; UPA00136; UER00200.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q9XEA6; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..321
FT /note="Cysteine synthase"
FT /id="PRO_0000167121"
FT BINDING 77
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 181..185
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 321 AA; 33838 MW; 9DCC3A2D961C7FD6 CRC64;
MGETIAKDVT ELIGNTPLVY LNRVTDGCVG RVAAKLESME PCSSVKDRIG YSMITDAEEK
GLITPGKSVL IEPTSGNTGI GLAFMAAAKG YRLVLTMPAS MSMERRIILK AFGAELILTD
PLLGMKGAVQ KAEELAAKTN NSFILQQFEN PANPKIHYET TGPEIWKGTG GKVDGLVSGI
GTGGTITGAG RYLREQNPDI KIYGVEPVES AVLSGGKPGP HKIQGIGAGF VPGVLDVDLI
NETVQVSSDE AIEMAKALAL KEGLLVGISS GAAAAAAVRL AQRPENEGKL FVVVFPSFGE
RYLSSVLFQS IKKEAENMVV E