CYSKP_ARATH
ID CYSKP_ARATH Reviewed; 392 AA.
AC P47999; O22828; Q42568;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Cysteine synthase, chloroplastic/chromoplastic;
DE EC=2.5.1.47;
DE AltName: Full=At.OAS.7-4;
DE AltName: Full=Beta-substituted Ala synthase 2;1;
DE Short=ARAth-Bsas2;1;
DE AltName: Full=CSase B;
DE Short=AtCS-B;
DE Short=CS-B;
DE AltName: Full=O-acetylserine (thiol)-lyase;
DE AltName: Full=O-acetylserine sulfhydrylase;
DE AltName: Full=OAS-TL B;
DE AltName: Full=cpACS1;
DE Flags: Precursor;
GN Name=OASB; OrderedLocusNames=At2g43750; ORFNames=F18O19.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8082776; DOI=10.1016/0014-5793(94)00872-8;
RA Hell R., Bork C., Bogdanova N., Frolov I., Hauschild R.;
RT "Isolation and characterization of two cDNAs encoding for compartment
RT specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis
RT thaliana.";
RL FEBS Lett. 351:257-262(1994).
RN [2]
RP SEQUENCE REVISION [MRNA].
RA Hell R.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=7610184; DOI=10.1104/pp.108.2.851;
RA Hesse H., Altmann T.;
RT "Molecular cloning of a cysteine synthase cDNA from Arabidopsis thaliana.";
RL Plant Physiol. 108:851-852(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=10940562; DOI=10.1016/s0378-1119(00)00261-4;
RA Jost R., Berkowitz O., Wirtz M., Hopkins L., Hawkesford M.J., Hell R.;
RT "Genomic and functional characterization of the oas gene family encoding O-
RT acetylserine (thiol) lyases, enzymes catalyzing the final step in cysteine
RT biosynthesis in Arabidopsis thaliana.";
RL Gene 253:237-247(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NOMENCLATURE.
RX PubMed=10889265; DOI=10.1104/pp.123.3.1163;
RA Hatzfeld Y., Maruyama A., Schmidt A., Noji M., Ishizawa K., Saito K.;
RT "beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like
RT protein in spinach and Arabidopsis.";
RL Plant Physiol. 123:1163-1171(2000).
RN [10]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15258168; DOI=10.1093/jxb/erh201;
RA Wirtz M., Droux M., Hell R.;
RT "O-acetylserine (thiol) lyase: an enigmatic enzyme of plant cysteine
RT biosynthesis revisited in Arabidopsis thaliana.";
RL J. Exp. Bot. 55:1785-1798(2004).
RN [11]
RP REVIEW.
RX PubMed=16307301; DOI=10.1007/s11120-005-8810-9;
RA Wirtz M., Droux M.;
RT "Synthesis of the sulfur amino acids: cysteine and methionine.";
RL Photosyn. Res. 86:345-362(2005).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18223034; DOI=10.1105/tpc.107.056747;
RA Heeg C., Kruse C., Jost R., Gutensohn M., Ruppert T., Wirtz M., Hell R.;
RT "Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family
RT demonstrates compartment-specific differences in the regulation of cysteine
RT synthesis.";
RL Plant Cell 20:168-185(2008).
RN [13]
RP GENE FAMILY, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18024555; DOI=10.1104/pp.107.106831;
RA Watanabe M., Kusano M., Oikawa A., Fukushima A., Noji M., Saito K.;
RT "Physiological roles of the beta-substituted alanine synthase gene family
RT in Arabidopsis.";
RL Plant Physiol. 146:310-320(2008).
RN [14]
RP ACETYLATION AT ALA-61, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20658158; DOI=10.1007/s00726-010-0694-0;
RA Wirtz M., Heeg C., Samami A.A., Ruppert T., Hell R.;
RT "Enzymes of cysteine synthesis show extensive and conserved modifications
RT patterns that include N(alpha)-terminal acetylation.";
RL Amino Acids 39:1077-1086(2010).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-61, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER LYS-60, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Acts as a major cysteine synthase.
CC {ECO:0000269|PubMed:18024555, ECO:0000269|PubMed:18223034}.
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:10940562, ECO:0000269|PubMed:15258168};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.81 mM for O(3)-acetyl-L-serine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168};
CC KM=0.31 mM for O(3)-acetyl-L-serine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168};
CC KM=3.0 uM for H(2)S for the cysteine synthase activity
CC {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168};
CC Vmax=171 umol/min/mg enzyme for L-cysteine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168};
CC Vmax=592 umol/min/mg enzyme for L-cysteine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168};
CC Vmax=0.37 umol/min/mg enzyme for H(2)S for the L-3-cyanoalanine
CC synthase activity {ECO:0000269|PubMed:10940562,
CC ECO:0000269|PubMed:15258168};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2.
CC -!- SUBUNIT: Homodimer. Component of the cysteine synthase complex (CSC)
CC composed of two OAS-TL dimers and one SAT hexamer (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid,
CC chromoplast.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:18024555, ECO:0000269|PubMed:18223034}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; X80377; CAA56594.2; -; mRNA.
DR EMBL; X81698; CAA57344.1; -; mRNA.
DR EMBL; AJ271728; CAB71292.1; -; Genomic_DNA.
DR EMBL; AC002333; AAB64031.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10317.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10318.1; -; Genomic_DNA.
DR EMBL; AY065375; AAL38816.1; -; mRNA.
DR EMBL; AY096681; AAM20315.1; -; mRNA.
DR EMBL; AY086156; AAM63361.1; -; mRNA.
DR PIR; A84870; A84870.
DR PIR; S48695; S48695.
DR RefSeq; NP_001189745.1; NM_001202816.1.
DR RefSeq; NP_181903.1; NM_129937.4.
DR AlphaFoldDB; P47999; -.
DR SMR; P47999; -.
DR BioGRID; 4314; 7.
DR IntAct; P47999; 1.
DR STRING; 3702.AT2G43750.1; -.
DR iPTMnet; P47999; -.
DR MetOSite; P47999; -.
DR SWISS-2DPAGE; P47999; -.
DR PaxDb; P47999; -.
DR PRIDE; P47999; -.
DR ProteomicsDB; 222775; -.
DR EnsemblPlants; AT2G43750.1; AT2G43750.1; AT2G43750.
DR EnsemblPlants; AT2G43750.2; AT2G43750.2; AT2G43750.
DR GeneID; 818978; -.
DR Gramene; AT2G43750.1; AT2G43750.1; AT2G43750.
DR Gramene; AT2G43750.2; AT2G43750.2; AT2G43750.
DR KEGG; ath:AT2G43750; -.
DR Araport; AT2G43750; -.
DR TAIR; locus:2043964; AT2G43750.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_021018_1_1_1; -.
DR InParanoid; P47999; -.
DR OMA; ELMEPCC; -.
DR OrthoDB; 1016546at2759; -.
DR PhylomeDB; P47999; -.
DR BioCyc; MetaCyc:AT2G43750-MON; -.
DR BRENDA; 2.5.1.47; 399.
DR UniPathway; UPA00136; UER00200.
DR PRO; PR:P47999; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P47999; baseline and differential.
DR Genevisible; P47999; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009509; C:chromoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; TAS:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:TAIR.
DR GO; GO:0019344; P:cysteine biosynthetic process; IDA:TAIR.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central.
DR GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IGI:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IGI:TAIR.
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 Acetylation; Amino-acid biosynthesis; Chloroplast; Chromoplast;
KW Cysteine biosynthesis; Plastid; Pyridoxal phosphate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast and chromoplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 61..392
FT /note="Cysteine synthase, chloroplastic/chromoplastic"
FT /id="PRO_0000006349"
FT BINDING 147
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 251..255
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:20658158,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 116
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 232
FT /note="G -> N (in Ref. 3; CAA57344)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="P -> T (in Ref. 3; CAA57344)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 41656 MW; B1220F01E8E31A12 CRC64;
MAATSSSAFL LNPLTSRHRP FKYSPELSSL SLSSRKAAAF DVSSAAFTLK RQSRSDVVCK
AVSIKPEAGV EGLNIADNAA QLIGKTPMVY LNNVVKGCVA SVAAKLEIME PCCSVKDRIG
YSMITDAEEK GLITPGKSVL VESTSGNTGI GLAFIAASKG YKLILTMPAS MSLERRVLLR
AFGAELVLTE PAKGMTGAIQ KAEEILKKTP NSYMLQQFDN PANPKIHYET TGPEIWEDTR
GKIDILVAGI GTGGTITGVG RFIKERKPEL KVIGVEPTES AILSGGKPGP HKIQGIGAGF
VPKNLDLAIV DEYIAISSEE AIETSKQLAL QEGLLVGISS GAAAAAAIQV AKRPENAGKL
IAVVFPSFGE RYLSTQLFQS IREECEQMQP EL
