CYSK1_ARATH
ID CYSK1_ARATH Reviewed; 322 AA.
AC P47998; O23343; Q1EC56; Q42570; Q94AS7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Cysteine synthase 1;
DE EC=2.5.1.47;
DE AltName: Full=At.OAS.5-8;
DE AltName: Full=Beta-substituted Ala synthase 1;1;
DE Short=ARAth-Bsas1;1;
DE AltName: Full=CSase A;
DE Short=AtCS-A;
DE AltName: Full=Cys-3A;
DE AltName: Full=O-acetylserine (thiol)-lyase 1;
DE Short=OAS-TL A;
DE AltName: Full=O-acetylserine sulfhydrylase;
DE AltName: Full=Protein ONSET OF LEAF DEATH 3;
GN Name=OASA1; Synonyms=OAS1, OASS, OLD3; OrderedLocusNames=At4g14880;
GN ORFNames=dl3480c;
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.
RA Hell R.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7729527; DOI=10.1016/0014-5793(95)00255-8;
RA Barroso C., Vega J.M., Gotor C.;
RT "A new member of the cytosolic O-acetylserine(thiol)lyase gene family in
RT Arabidopsis thaliana.";
RL FEBS Lett. 363:1-5(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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [7]
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 [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
RP ACETYLATION AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION
RP 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 [16]
RP MUTAGENESIS OF GLY-162, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=20429919; DOI=10.1186/1471-2229-10-80;
RA Shirzadian-Khorramabad R., Jing H.C., Everts G.E., Schippers J.H.,
RA Hille J., Dijkwel P.P.;
RT "A mutation in the cytosolic O-acetylserine (thiol) lyase induces a genome-
RT dependent early leaf death phenotype in Arabidopsis.";
RL BMC Plant Biol. 10:80-80(2010).
RN [17]
RP HOMODIMERIZATION, INTERACTION WITH SULTR1;2, AND ACTIVITY REGULATION.
RX PubMed=20529854; DOI=10.1074/jbc.m110.126888;
RA Shibagaki N., Grossman A.R.;
RT "Binding of cysteine synthase to the STAS domain of sulfate transporter and
RT its regulatory consequences.";
RL J. Biol. Chem. 285:25094-25102(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-46,
RP COFACTOR, SUBUNIT, INTERACTION WITH SAT1, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND MUTAGENESIS OF LYS-46; THR-74; SER-75; ASN-77; THR-78; GLN-147;
RP HIS-157; THR-182; THR-185; LYS-217; HIS-221; LYS-222 AND SER-269.
RX PubMed=16166087; DOI=10.1074/jbc.m505313200;
RA Bonner E.R., Cahoon R.E., Knapke S.M., Jez J.M.;
RT "Molecular basis of cysteine biosynthesis in plants: structural and
RT functional analysis of o-acetylserine sulfhydrylase from Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 280:38803-38813(2005).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 3-322, COFACTOR, SUBUNIT, AND
RP INTERACTION WITH SAT1.
RX PubMed=17194764; DOI=10.1105/tpc.106.047316;
RA Francois J.A., Kumaran S., Jez J.M.;
RT "Structural basis for interaction of O-acetylserine sulfhydrylase and
RT serine acetyltransferase in the Arabidopsis cysteine synthase complex.";
RL Plant Cell 18:3647-3655(2006).
CC -!- FUNCTION: Acts as a major cysteine synthase, probably involved in
CC maintaining organic sulfur level. {ECO:0000269|PubMed:18024555,
CC ECO:0000269|PubMed:18223034, ECO:0000269|PubMed:20429919}.
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 Evidence={ECO:0000269|PubMed:16166087, ECO:0000269|PubMed:17194764};
CC -!- ACTIVITY REGULATION: Interaction with the sulfate transporter SULTR1;2
CC enhances its catalytic activity. {ECO:0000269|PubMed:20529854}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 mM for O-acetylserine (at pH 7.0 and 25 degrees Celsius) for
CC the cysteine synthase activity {ECO:0000269|PubMed:10940562,
CC ECO:0000269|PubMed:15258168, ECO:0000269|PubMed:16166087};
CC KM=1.22 mM for O(3)-acetyl-L-serine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168,
CC ECO:0000269|PubMed:16166087};
CC KM=0.69 mM for O(3)-acetyl-L-serine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168,
CC ECO:0000269|PubMed:16166087};
CC KM=0.22 mM for Na(2)S (at pH 7.0 and 25 degrees Celsius) for the
CC cysteine synthase activity {ECO:0000269|PubMed:10940562,
CC ECO:0000269|PubMed:15258168, ECO:0000269|PubMed:16166087};
CC KM=5.6 uM for H(2)S for the cysteine synthase activity
CC {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168,
CC ECO:0000269|PubMed:16166087};
CC Vmax=225 umol/min/mg enzyme for L-cysteine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168,
CC ECO:0000269|PubMed:16166087};
CC Vmax=906 umol/min/mg enzyme for L-cysteine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168,
CC ECO:0000269|PubMed:16166087};
CC Vmax=0.43 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, ECO:0000269|PubMed:16166087};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2.
CC -!- SUBUNIT: Homodimer. Interacts with SAT1. Component of the cysteine
CC synthase complex (CSC) composed of two OAS-TL dimers and one SAT
CC hexamer. Interacts with SULTR1;2. {ECO:0000269|PubMed:16166087,
CC ECO:0000269|PubMed:17194764, ECO:0000269|PubMed:20529854}.
CC -!- INTERACTION:
CC P47998; Q9MAX3: SULTR1;2; NbExp=5; IntAct=EBI-1633418, EBI-8772960;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype but displays lower levels of
CC thiols in roots and leaves, and also an affected sulfur balance. Also
CC shows an increased sensitivity to cadmium stress.
CC {ECO:0000269|PubMed:18024555, ECO:0000269|PubMed:18223034,
CC ECO:0000269|PubMed:20429919}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; X80376; CAA56593.2; -; mRNA.
DR EMBL; X84097; CAA58893.1; -; mRNA.
DR EMBL; AJ272027; CAB72932.1; -; Genomic_DNA.
DR EMBL; Z97337; CAB10267.1; -; Genomic_DNA.
DR EMBL; AL161540; CAB78530.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83512.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83513.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83514.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83515.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66097.1; -; Genomic_DNA.
DR EMBL; AY045825; AAK76499.1; -; mRNA.
DR EMBL; BT025878; ABF85780.1; -; mRNA.
DR PIR; A71412; A71412.
DR PIR; S48694; S48694.
DR RefSeq; NP_001190732.1; NM_001203803.1.
DR RefSeq; NP_001190733.1; NM_001203804.1.
DR RefSeq; NP_001328013.1; NM_001340975.1.
DR RefSeq; NP_193224.1; NM_117574.4.
DR RefSeq; NP_849386.1; NM_179055.3.
DR PDB; 1Z7W; X-ray; 2.20 A; A=1-322.
DR PDB; 1Z7Y; X-ray; 2.70 A; A=1-322.
DR PDB; 2ISQ; X-ray; 2.80 A; A=3-322.
DR PDBsum; 1Z7W; -.
DR PDBsum; 1Z7Y; -.
DR PDBsum; 2ISQ; -.
DR AlphaFoldDB; P47998; -.
DR SMR; P47998; -.
DR BioGRID; 12442; 19.
DR IntAct; P47998; 5.
DR STRING; 3702.AT4G14880.4; -.
DR iPTMnet; P47998; -.
DR MetOSite; P47998; -.
DR PaxDb; P47998; -.
DR PRIDE; P47998; -.
DR ProteomicsDB; 222595; -.
DR EnsemblPlants; AT4G14880.1; AT4G14880.1; AT4G14880.
DR EnsemblPlants; AT4G14880.2; AT4G14880.2; AT4G14880.
DR EnsemblPlants; AT4G14880.3; AT4G14880.3; AT4G14880.
DR EnsemblPlants; AT4G14880.4; AT4G14880.4; AT4G14880.
DR EnsemblPlants; AT4G14880.5; AT4G14880.5; AT4G14880.
DR GeneID; 827145; -.
DR Gramene; AT4G14880.1; AT4G14880.1; AT4G14880.
DR Gramene; AT4G14880.2; AT4G14880.2; AT4G14880.
DR Gramene; AT4G14880.3; AT4G14880.3; AT4G14880.
DR Gramene; AT4G14880.4; AT4G14880.4; AT4G14880.
DR Gramene; AT4G14880.5; AT4G14880.5; AT4G14880.
DR KEGG; ath:AT4G14880; -.
DR Araport; AT4G14880; -.
DR TAIR; locus:2130419; AT4G14880.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_021018_1_0_1; -.
DR InParanoid; P47998; -.
DR OMA; HIAKDMT; -.
DR OrthoDB; 1016546at2759; -.
DR PhylomeDB; P47998; -.
DR BioCyc; MetaCyc:AT4G14880-MON; -.
DR BRENDA; 2.5.1.47; 399.
DR SABIO-RK; P47998; -.
DR UniPathway; UPA00136; UER00200.
DR EvolutionaryTrace; P47998; -.
DR PRO; PR:P47998; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P47998; baseline and differential.
DR Genevisible; P47998; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0007568; P:aging; IMP:TAIR.
DR GO; GO:0019344; P:cysteine biosynthetic process; IMP: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 GO; GO:0046686; P:response to cadmium ion; IDA: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 3D-structure; Acetylation; Amino-acid biosynthesis; Cysteine biosynthesis;
KW Cytoplasm; Phosphoprotein; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:20658158"
FT CHAIN 2..322
FT /note="Cysteine synthase 1"
FT /id="PRO_0000167116"
FT REGION 144..287
FT /note="SUTR1;2 binding"
FT /evidence="ECO:0000305|PubMed:20529854"
FT REGION 217..222
FT /note="SAT1 binding"
FT /evidence="ECO:0000305|PubMed:16166087"
FT BINDING 77
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:16166087,
FT ECO:0000269|PubMed:17194764, ECO:0007744|PDB:1Z7W,
FT ECO:0007744|PDB:2ISQ"
FT BINDING 181..185
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:16166087,
FT ECO:0000269|PubMed:17194764, ECO:0007744|PDB:1Z7W,
FT ECO:0007744|PDB:2ISQ"
FT BINDING 269
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:16166087,
FT ECO:0000269|PubMed:17194764, ECO:0007744|PDB:1Z7W,
FT ECO:0007744|PDB:2ISQ"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000305|PubMed:20658158"
FT MOD_RES 46
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:16166087,
FT ECO:0000269|PubMed:17194764, ECO:0007744|PDB:1Z7W,
FT ECO:0007744|PDB:2ISQ"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MUTAGEN 46
FT /note="K->A: No cysteine synthase activity."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 74
FT /note="T->A: Strong reduction of cysteine synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 74
FT /note="T->S: Reduction of cysteine synthase activity."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 75
FT /note="S->A,N,T: Strong reduction of cysteine synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 77
FT /note="N->A: Reduction of cysteine synthase activity."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 77
FT /note="N->D: Strong reduction of cysteine synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 78
FT /note="T->A,S: Reduction of cysteine synthase activity."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 147
FT /note="Q->A,E: Strong reduction of cysteine synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 157
FT /note="H->Q,N: Slight reduction of cysteine synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 162
FT /note="G->E: In old3-1; displays a early leaf death
FT phenotype. Abolishes cysteine synthase activity."
FT /evidence="ECO:0000269|PubMed:20429919"
FT MUTAGEN 182
FT /note="T->A,S: Slight reduction of cysteine synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 185
FT /note="T->A,S: Strong reduction of cysteine synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 217
FT /note="K->A: Impaired interaction with SAT1."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 221
FT /note="H->A: Impaired interaction with SAT1."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 222
FT /note="K->A: Impaired interaction with SAT1."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 269
FT /note="S->A: Strong reduction of cysteine synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:16166087"
FT MUTAGEN 269
FT /note="S->T: Reduction of cysteine synthase activity."
FT /evidence="ECO:0000269|PubMed:16166087"
FT CONFLICT 20
FT /note="Missing (in Ref. 8; AAK76499)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="A -> E (in Ref. 3; CAA58893)"
FT /evidence="ECO:0000305"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:1Z7W"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1Z7W"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:1Z7W"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1Z7W"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:1Z7W"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1Z7W"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 124..138
FT /evidence="ECO:0007829|PDB:1Z7W"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1Z7W"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:1Z7W"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:1Z7W"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:1Z7W"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:1Z7W"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:1Z7W"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 248..262
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:1Z7W"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:1Z7W"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2ISQ"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1Z7W"
FT HELIX 309..316
FT /evidence="ECO:0007829|PDB:1Z7W"
SQ SEQUENCE 322 AA; 33805 MW; 5B3E7F3D9DA5908B CRC64;
MASRIAKDVT ELIGNTPLVY LNNVAEGCVG RVAAKLEMME PCSSVKDRIG FSMISDAEKK
GLIKPGESVL IEPTSGNTGV GLAFTAAAKG YKLIITMPAS MSTERRIILL AFGVELVLTD
PAKGMKGAIA KAEEILAKTP NGYMLQQFEN PANPKIHYET TGPEIWKGTG GKIDGFVSGI
GTGGTITGAG KYLKEQNANV KLYGVEPVES AILSGGKPGP HKIQGIGAGF IPSVLNVDLI
DEVVQVSSDE SIDMARQLAL KEGLLVGISS GAAAAAAIKL AQRPENAGKL FVAIFPSFGE
RYLSTVLFDA TRKEAEAMTF EA
