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Cysteine synthase 1 (EC 2.5.1.47) (At.OAS.5-8) (Beta-substituted Ala synthase 1;1) (ARAth-Bsas1;1) (CSase A) (AtCS-A) (Cys-3A) (O-acetylserine (thiol)-lyase 1) (OAS-TL A) (O-acetylserine sulfhydrylase) (Protein ONSET OF LEAF DEATH 3)

 CYSK1_ARATH             Reviewed;         322 AA.
P47998; O23343; Q1EC56; Q42570; Q94AS7;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
25-OCT-2017, entry version 152.
RecName: Full=Cysteine synthase 1;
EC=2.5.1.47;
AltName: Full=At.OAS.5-8;
AltName: Full=Beta-substituted Ala synthase 1;1;
Short=ARAth-Bsas1;1;
AltName: Full=CSase A;
Short=AtCS-A;
AltName: Full=Cys-3A;
AltName: Full=O-acetylserine (thiol)-lyase 1;
Short=OAS-TL A;
AltName: Full=O-acetylserine sulfhydrylase;
AltName: Full=Protein ONSET OF LEAF DEATH 3;
Name=OASA1; Synonyms=OAS1, OASS, OLD3; OrderedLocusNames=At4g14880;
ORFNames=dl3480c;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=8082776; DOI=10.1016/0014-5793(94)00872-8;
Hell R., Bork C., Bogdanova N., Frolov I., Hauschild R.;
"Isolation and characterization of two cDNAs encoding for compartment
specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis
thaliana.";
FEBS Lett. 351:257-262(1994).
[2]
SEQUENCE REVISION.
Hell R.;
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7729527; DOI=10.1016/0014-5793(95)00255-8;
Barroso C., Vega J.M., Gotor C.;
"A new member of the cytosolic O-acetylserine(thiol)lyase gene family
in Arabidopsis thaliana.";
FEBS Lett. 363:1-5(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=cv. Columbia;
PubMed=10940562; DOI=10.1016/S0378-1119(00)00261-4;
Jost R., Berkowitz O., Wirtz M., Hopkins L., Hawkesford M.J., Hell R.;
"Genomic and functional characterization of the oas gene family
encoding O-acetylserine (thiol) lyases, enzymes catalyzing the final
step in cysteine biosynthesis in Arabidopsis thaliana.";
Gene 253:237-247(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9461215; DOI=10.1038/35140;
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L.,
Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P.,
Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N.,
Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A.,
Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S.,
Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B.,
Mueller-Auer S., Silvey M., James R., Monfort A., Pons A.,
Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P.,
Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T.,
Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W.,
Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W.,
Klosterman S., Schueller C., Chalwatzis N.;
"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of
Arabidopsis thaliana.";
Nature 391:485-488(1998).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[7]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[10]
NOMENCLATURE.
PubMed=10889265; DOI=10.1104/pp.123.3.1163;
Hatzfeld Y., Maruyama A., Schmidt A., Noji M., Ishizawa K., Saito K.;
"beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like
protein in spinach and Arabidopsis.";
Plant Physiol. 123:1163-1171(2000).
[11]
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15258168; DOI=10.1093/jxb/erh201;
Wirtz M., Droux M., Hell R.;
"O-acetylserine (thiol) lyase: an enigmatic enzyme of plant cysteine
biosynthesis revisited in Arabidopsis thaliana.";
J. Exp. Bot. 55:1785-1798(2004).
[12]
REVIEW.
PubMed=16307301; DOI=10.1007/s11120-005-8810-9;
Wirtz M., Droux M.;
"Synthesis of the sulfur amino acids: cysteine and methionine.";
Photosyn. Res. 86:345-362(2005).
[13]
FUNCTION, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18223034; DOI=10.1105/tpc.107.056747;
Heeg C., Kruse C., Jost R., Gutensohn M., Ruppert T., Wirtz M.,
Hell R.;
"Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family
demonstrates compartment-specific differences in the regulation of
cysteine synthesis.";
Plant Cell 20:168-185(2008).
[14]
GENE FAMILY, FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18024555; DOI=10.1104/pp.107.106831;
Watanabe M., Kusano M., Oikawa A., Fukushima A., Noji M., Saito K.;
"Physiological roles of the beta-substituted alanine synthase gene
family in Arabidopsis.";
Plant Physiol. 146:310-320(2008).
[15]
ACETYLATION AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20658158; DOI=10.1007/s00726-010-0694-0;
Wirtz M., Heeg C., Samami A.A., Ruppert T., Hell R.;
"Enzymes of cysteine synthesis show extensive and conserved
modifications patterns that include N(alpha)-terminal acetylation.";
Amino Acids 39:1077-1086(2010).
[16]
MUTAGENESIS OF GLY-162, DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=20429919; DOI=10.1186/1471-2229-10-80;
Shirzadian-Khorramabad R., Jing H.C., Everts G.E., Schippers J.H.,
Hille J., Dijkwel P.P.;
"A mutation in the cytosolic O-acetylserine (thiol) lyase induces a
genome-dependent early leaf death phenotype in Arabidopsis.";
BMC Plant Biol. 10:80-80(2010).
[17]
HOMODIMERIZATION, INTERACTION WITH SULTR1;2, AND ENZYME REGULATION.
PubMed=20529854; DOI=10.1074/jbc.M110.126888;
Shibagaki N., Grossman A.R.;
"Binding of cysteine synthase to the STAS domain of sulfate
transporter and its regulatory consequences.";
J. Biol. Chem. 285:25094-25102(2010).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22092075; DOI=10.1021/pr200917t;
Aryal U.K., Krochko J.E., Ross A.R.;
"Identification of phosphoproteins in Arabidopsis thaliana leaves
using polyethylene glycol fractionation, immobilized metal-ion
affinity chromatography, two-dimensional gel electrophoresis and mass
spectrometry.";
J. Proteome Res. 11:425-437(2012).
[19]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-46,
COFACTOR, SUBUNIT, INTERACTION WITH SAT1, BIOPHYSICOCHEMICAL
PROPERTIES, AND MUTAGENESIS OF LYS-46; THR-74; SER-75; ASN-77; THR-78;
GLN-147; HIS-157; THR-182; THR-185; LYS-217; HIS-221; LYS-222 AND
SER-269.
PubMed=16166087; DOI=10.1074/jbc.M505313200;
Bonner E.R., Cahoon R.E., Knapke S.M., Jez J.M.;
"Molecular basis of cysteine biosynthesis in plants: structural and
functional analysis of o-acetylserine sulfhydrylase from Arabidopsis
thaliana.";
J. Biol. Chem. 280:38803-38813(2005).
[20]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 3-322, COFACTOR, SUBUNIT, AND
INTERACTION WITH SAT1.
PubMed=17194764; DOI=10.1105/tpc.106.047316;
Francois J.A., Kumaran S., Jez J.M.;
"Structural basis for interaction of O-acetylserine sulfhydrylase and
serine acetyltransferase in the Arabidopsis cysteine synthase
complex.";
Plant Cell 18:3647-3655(2006).
-!- FUNCTION: Acts as a major cysteine synthase, probably involved in
maintaining organic sulfur level. {ECO:0000269|PubMed:18024555,
ECO:0000269|PubMed:18223034, ECO:0000269|PubMed:20429919}.
-!- CATALYTIC ACTIVITY: O-acetyl-L-serine + hydrogen sulfide = L-
cysteine + acetate. {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:16166087,
ECO:0000269|PubMed:17194764};
-!- ENZYME REGULATION: Interaction with the sulfate transporter
SULTR1;2 enhances its catalytic activity.
{ECO:0000269|PubMed:20529854}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.4 mM for O-acetylserine (at pH 7.0 and 25 degrees Celsius)
for the cysteine synthase activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168, ECO:0000269|PubMed:16166087};
KM=1.22 mM for O(3)-acetyl-L-serine for the cysteine synthase
activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168, ECO:0000269|PubMed:16166087};
KM=0.69 mM for O(3)-acetyl-L-serine for the cysteine synthase
activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168, ECO:0000269|PubMed:16166087};
KM=0.22 mM for Na(2)S (at pH 7.0 and 25 degrees Celsius) for the
cysteine synthase activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168, ECO:0000269|PubMed:16166087};
KM=5.6 uM for H(2)S for the cysteine synthase activity
{ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168,
ECO:0000269|PubMed:16166087};
Vmax=225 umol/min/mg enzyme for L-cysteine for the cysteine
synthase activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168, ECO:0000269|PubMed:16166087};
Vmax=906 umol/min/mg enzyme for L-cysteine for the cysteine
synthase activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168, ECO:0000269|PubMed:16166087};
Vmax=0.43 umol/min/mg enzyme for H(2)S for the L-3-cyanoalanine
synthase activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168, ECO:0000269|PubMed:16166087};
-!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-
cysteine from L-serine: step 2/2.
-!- SUBUNIT: Homodimer. Interacts with SAT1. Component of the cysteine
synthase complex (CSC) composed of two OAS-TL dimers and one SAT
hexamer. Interacts with SULTR1;2. {ECO:0000269|PubMed:16166087,
ECO:0000269|PubMed:17194764, ECO:0000269|PubMed:20529854}.
-!- INTERACTION:
Q9MAX3:SULTR1;2; NbExp=5; IntAct=EBI-1633418, EBI-8772960;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: No visible phenotype but displays lower
levels of thiols in roots and leaves, and also an affected sulfur
balance. Also shows an increased sensitivity to cadmium stress.
{ECO:0000269|PubMed:18024555, ECO:0000269|PubMed:18223034,
ECO:0000269|PubMed:20429919}.
-!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
synthase family. {ECO:0000305}.
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EMBL; X80376; CAA56593.2; -; mRNA.
EMBL; X84097; CAA58893.1; -; mRNA.
EMBL; AJ272027; CAB72932.1; -; Genomic_DNA.
EMBL; Z97337; CAB10267.1; -; Genomic_DNA.
EMBL; AL161540; CAB78530.1; -; Genomic_DNA.
EMBL; CP002687; AEE83512.1; -; Genomic_DNA.
EMBL; CP002687; AEE83513.1; -; Genomic_DNA.
EMBL; CP002687; AEE83514.1; -; Genomic_DNA.
EMBL; CP002687; AEE83515.1; -; Genomic_DNA.
EMBL; CP002687; ANM66097.1; -; Genomic_DNA.
EMBL; AY045825; AAK76499.1; -; mRNA.
EMBL; BT025878; ABF85780.1; -; mRNA.
PIR; A71412; A71412.
PIR; S48694; S48694.
RefSeq; NP_001190732.1; NM_001203803.1.
RefSeq; NP_001190733.1; NM_001203804.1.
RefSeq; NP_001328013.1; NM_001340975.1.
RefSeq; NP_193224.1; NM_117574.4.
RefSeq; NP_849386.1; NM_179055.3.
UniGene; At.30; -.
UniGene; At.34389; -.
PDB; 1Z7W; X-ray; 2.20 A; A=1-322.
PDB; 1Z7Y; X-ray; 2.70 A; A=1-322.
PDB; 2ISQ; X-ray; 2.80 A; A=3-322.
PDBsum; 1Z7W; -.
PDBsum; 1Z7Y; -.
PDBsum; 2ISQ; -.
ProteinModelPortal; P47998; -.
SMR; P47998; -.
BioGrid; 12442; 8.
IntAct; P47998; 5.
MINT; MINT-8061212; -.
STRING; 3702.AT4G14880.1; -.
iPTMnet; P47998; -.
PaxDb; P47998; -.
PRIDE; P47998; -.
EnsemblPlants; AT4G14880.1; AT4G14880.1; AT4G14880.
EnsemblPlants; AT4G14880.2; AT4G14880.2; AT4G14880.
EnsemblPlants; AT4G14880.3; AT4G14880.3; AT4G14880.
EnsemblPlants; AT4G14880.4; AT4G14880.4; AT4G14880.
EnsemblPlants; AT4G14880.5; AT4G14880.5; AT4G14880.
GeneID; 827145; -.
Gramene; AT4G14880.1; AT4G14880.1; AT4G14880.
Gramene; AT4G14880.2; AT4G14880.2; AT4G14880.
Gramene; AT4G14880.3; AT4G14880.3; AT4G14880.
Gramene; AT4G14880.4; AT4G14880.4; AT4G14880.
Gramene; AT4G14880.5; AT4G14880.5; AT4G14880.
KEGG; ath:AT4G14880; -.
Araport; AT4G14880; -.
TAIR; locus:2130419; AT4G14880.
eggNOG; KOG1252; Eukaryota.
eggNOG; COG0031; LUCA.
InParanoid; P47998; -.
KO; K01738; -.
OMA; WDSGERY; -.
OrthoDB; EOG09360FNG; -.
PhylomeDB; P47998; -.
BioCyc; MetaCyc:AT4G14880-MONOMER; -.
BRENDA; 2.5.1.47; 399.
SABIO-RK; P47998; -.
UniPathway; UPA00136; UER00200.
EvolutionaryTrace; P47998; -.
PRO; PR:P47998; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; P47998; baseline and differential.
Genevisible; P47998; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0004124; F:cysteine synthase activity; IDA:TAIR.
GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0007568; P:aging; IMP:TAIR.
GO; GO:0019344; P:cysteine biosynthetic process; IMP:TAIR.
GO; GO:0006535; P:cysteine biosynthetic process from serine; TAS:TAIR.
GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IGI:TAIR.
GO; GO:0009860; P:pollen tube growth; IGI:TAIR.
GO; GO:0046686; P:response to cadmium ion; IDA:TAIR.
InterPro; IPR005856; Cys_synth.
InterPro; IPR005859; CysK.
InterPro; IPR001216; P-phosphate_BS.
InterPro; IPR001926; PLP-dep.
InterPro; IPR036052; Trypto_synt_PLP_dependent.
Pfam; PF00291; PALP; 1.
SUPFAM; SSF53686; SSF53686; 1.
TIGRFAMs; TIGR01139; cysK; 1.
TIGRFAMs; TIGR01136; cysKM; 1.
PROSITE; PS00901; CYS_SYNTHASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Amino-acid biosynthesis; Complete proteome;
Cysteine biosynthesis; Cytoplasm; Phosphoprotein; Pyridoxal phosphate;
Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000305|PubMed:20658158}.
CHAIN 2 322 Cysteine synthase 1.
/FTId=PRO_0000167116.
REGION 144 287 SUTR1;2 binding.
{ECO:0000305|PubMed:20529854}.
REGION 181 185 Pyridoxal phosphate binding.
{ECO:0000244|PDB:1Z7W,
ECO:0000244|PDB:2ISQ,
ECO:0000269|PubMed:16166087,
ECO:0000269|PubMed:17194764}.
REGION 217 222 SAT1 binding.
{ECO:0000305|PubMed:16166087}.
BINDING 77 77 Pyridoxal phosphate.
{ECO:0000244|PDB:1Z7W,
ECO:0000244|PDB:2ISQ,
ECO:0000269|PubMed:16166087,
ECO:0000269|PubMed:17194764}.
BINDING 269 269 Pyridoxal phosphate.
{ECO:0000244|PDB:1Z7W,
ECO:0000244|PDB:2ISQ,
ECO:0000269|PubMed:16166087,
ECO:0000269|PubMed:17194764}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000305|PubMed:20658158}.
MOD_RES 46 46 N6-(pyridoxal phosphate)lysine.
{ECO:0000244|PDB:1Z7W,
ECO:0000244|PDB:2ISQ,
ECO:0000269|PubMed:16166087,
ECO:0000269|PubMed:17194764}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000244|PubMed:22092075}.
MUTAGEN 46 46 K->A: No cysteine synthase activity.
{ECO:0000269|PubMed:16166087}.
MUTAGEN 74 74 T->A: Strong reduction of cysteine
synthase activity.
{ECO:0000269|PubMed:16166087}.
MUTAGEN 74 74 T->S: Reduction of cysteine synthase
activity. {ECO:0000269|PubMed:16166087}.
MUTAGEN 75 75 S->A,N,T: Strong reduction of cysteine
synthase activity.
{ECO:0000269|PubMed:16166087}.
MUTAGEN 77 77 N->A: Reduction of cysteine synthase
activity. {ECO:0000269|PubMed:16166087}.
MUTAGEN 77 77 N->D: Strong reduction of cysteine
synthase activity.
{ECO:0000269|PubMed:16166087}.
MUTAGEN 78 78 T->A,S: Reduction of cysteine synthase
activity. {ECO:0000269|PubMed:16166087}.
MUTAGEN 147 147 Q->A,E: Strong reduction of cysteine
synthase activity.
{ECO:0000269|PubMed:16166087}.
MUTAGEN 157 157 H->Q,N: Slight reduction of cysteine
synthase activity.
{ECO:0000269|PubMed:16166087}.
MUTAGEN 162 162 G->E: In old3-1; displays a early leaf
death phenotype. Abolishes cysteine
synthase activity.
{ECO:0000269|PubMed:20429919}.
MUTAGEN 182 182 T->A,S: Slight reduction of cysteine
synthase activity.
{ECO:0000269|PubMed:16166087}.
MUTAGEN 185 185 T->A,S: Strong reduction of cysteine
synthase activity.
{ECO:0000269|PubMed:16166087}.
MUTAGEN 217 217 K->A: Impaired interaction with SAT1.
{ECO:0000269|PubMed:16166087}.
MUTAGEN 221 221 H->A: Impaired interaction with SAT1.
{ECO:0000269|PubMed:16166087}.
MUTAGEN 222 222 K->A: Impaired interaction with SAT1.
{ECO:0000269|PubMed:16166087}.
MUTAGEN 269 269 S->A: Strong reduction of cysteine
synthase activity.
{ECO:0000269|PubMed:16166087}.
MUTAGEN 269 269 S->T: Reduction of cysteine synthase
activity. {ECO:0000269|PubMed:16166087}.
CONFLICT 20 20 Missing (in Ref. 8; AAK76499).
{ECO:0000305}.
CONFLICT 273 273 A -> E (in Ref. 3; CAA58893).
{ECO:0000305}.
HELIX 9 12 {ECO:0000244|PDB:1Z7W}.
STRAND 18 20 {ECO:0000244|PDB:1Z7W}.
HELIX 23 25 {ECO:0000244|PDB:1Z7W}.
STRAND 29 36 {ECO:0000244|PDB:1Z7W}.
HELIX 37 39 {ECO:0000244|PDB:1Z7W}.
HELIX 46 59 {ECO:0000244|PDB:1Z7W}.
TURN 65 67 {ECO:0000244|PDB:1Z7W}.
STRAND 69 73 {ECO:0000244|PDB:1Z7W}.
HELIX 77 89 {ECO:0000244|PDB:1Z7W}.
STRAND 92 98 {ECO:0000244|PDB:1Z7W}.
HELIX 103 111 {ECO:0000244|PDB:1Z7W}.
STRAND 115 119 {ECO:0000244|PDB:1Z7W}.
HELIX 121 123 {ECO:0000244|PDB:1Z7W}.
HELIX 124 138 {ECO:0000244|PDB:1Z7W}.
STRAND 142 144 {ECO:0000244|PDB:1Z7W}.
TURN 147 149 {ECO:0000244|PDB:1Z7W}.
HELIX 152 159 {ECO:0000244|PDB:1Z7W}.
HELIX 161 168 {ECO:0000244|PDB:1Z7W}.
TURN 169 171 {ECO:0000244|PDB:1Z7W}.
STRAND 175 179 {ECO:0000244|PDB:1Z7W}.
STRAND 181 183 {ECO:0000244|PDB:1Z7W}.
HELIX 184 196 {ECO:0000244|PDB:1Z7W}.
STRAND 201 207 {ECO:0000244|PDB:1Z7W}.
HELIX 208 210 {ECO:0000244|PDB:1Z7W}.
HELIX 212 214 {ECO:0000244|PDB:1Z7W}.
HELIX 237 239 {ECO:0000244|PDB:1Z7W}.
STRAND 241 246 {ECO:0000244|PDB:1Z7W}.
HELIX 248 262 {ECO:0000244|PDB:1Z7W}.
HELIX 268 281 {ECO:0000244|PDB:1Z7W}.
HELIX 284 286 {ECO:0000244|PDB:1Z7W}.
STRAND 290 295 {ECO:0000244|PDB:1Z7W}.
HELIX 299 302 {ECO:0000244|PDB:1Z7W}.
STRAND 303 305 {ECO:0000244|PDB:2ISQ}.
HELIX 306 308 {ECO:0000244|PDB:1Z7W}.
HELIX 309 316 {ECO:0000244|PDB:1Z7W}.
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


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