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Protein

Cysteine synthase, mitochondrial

Gene

OASC

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a cysteine synthase. Plays a role in the sulfide detoxification in mitochondria.3 Publications

Catalytic activityi

O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate.2 Publications

Cofactori

Kineticsi

  1. KM=0.98 mM for O(3)-acetyl-L-serine for the cysteine synthase activity2 Publications
  2. KM=0.43 mM for O(3)-acetyl-L-serine for the cysteine synthase activity2 Publications
  3. KM=4.7 µM for H2S for the cysteine synthase activity2 Publications
  1. Vmax=159 µmol/min/mg enzyme for L-cysteine for the cysteine synthase activity2 Publications
  2. Vmax=534 µmol/min/mg enzyme for L-cysteine for the cysteine synthase activity2 Publications
  3. Vmax=0.33 µmol/min/mg enzyme for H2S for the L-3-cyanoalanine synthase activity2 Publications

Pathwayi: L-cysteine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-cysteine from L-serine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Serine acetyltransferase 3, mitochondrial (SAT3), Serine acetyltransferase 5 (SAT5), Serine acetyltransferase 1, chloroplastic (SAT1), Serine acetyltransferase 2 (SAT2), Serine acetyltransferase 4 (SAT4)
  2. Bifunctional L-3-cyanoalanine synthase/cysteine synthase D2 (CYSD2), Bifunctional cystathionine gamma-lyase/cysteine synthase (DES1), Cysteine synthase, mitochondrial (OASC), Bifunctional L-3-cyanoalanine synthase/cysteine synthase D1 (CYSD1), Cysteine synthase, chloroplastic/chromoplastic (OASB), Cysteine synthase 1 (OASA1)
This subpathway is part of the pathway L-cysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-cysteine from L-serine, the pathway L-cysteine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei185 – 1851Pyridoxal phosphateBy similarity
Binding sitei377 – 3771Pyridoxal phosphateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Cysteine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciARA:GQT-2188-MONOMER.
ARA:GQT-2189-MONOMER.
MetaCyc:AT3G59760-MONOMER.
UniPathwayiUPA00136; UER00200.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine synthase, mitochondrial (EC:2.5.1.47)
Alternative name(s):
Beta-substituted Ala synthase 2;2
Short name:
ARAth-Bsas2;2
CSase C
Short name:
AtCS-C
Short name:
CS-C
O-acetylserine (thiol)-lyase
O-acetylserine sulfhydrylase
OAS-TL C
Gene namesi
Name:OASC
Synonyms:ACS 1
Ordered Locus Names:At3g59760
ORF Names:F24G16.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G59760.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

No visible phenotype but displays lower levels of thiols in roots (PubMed:18024555). Growth retardation (PubMed:18223034). Defects in root hair formation (PubMed:22511607).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 430Cysteine synthase, mitochondrialPRO_0000006353
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei154 – 1541N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiQ43725.
PRIDEiQ43725.

PTM databases

SwissPalmiQ43725.

Expressioni

Gene expression databases

ExpressionAtlasiQ43725. baseline and differential.
GenevisibleiQ43725. AT.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with SAT3. Component of the cysteine synthase complex (CSC) composed of two OAS-TL dimers and one SAT hexamer.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SAT3Q392184EBI-1633616,EBI-1633440

Protein-protein interaction databases

BioGridi10459. 4 interactions.
DIPiDIP-40500N.
IntActiQ43725. 3 interactions.
STRINGi3702.AT3G59760.1.

Structurei

Secondary structure

1
430
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi114 – 1163Combined sources
Helixi117 – 1204Combined sources
Beta strandi126 – 1283Combined sources
Helixi131 – 1333Combined sources
Beta strandi137 – 1448Combined sources
Helixi145 – 1473Combined sources
Helixi155 – 16713Combined sources
Turni173 – 1753Combined sources
Beta strandi177 – 1815Combined sources
Helixi185 – 19713Combined sources
Beta strandi200 – 2067Combined sources
Helixi211 – 2199Combined sources
Beta strandi223 – 2275Combined sources
Helixi229 – 2313Combined sources
Helixi232 – 24615Combined sources
Beta strandi250 – 2523Combined sources
Turni255 – 2573Combined sources
Helixi260 – 2678Combined sources
Helixi269 – 2768Combined sources
Beta strandi281 – 2877Combined sources
Beta strandi289 – 2913Combined sources
Helixi292 – 30413Combined sources
Beta strandi308 – 3158Combined sources
Helixi316 – 3183Combined sources
Helixi320 – 3223Combined sources
Turni345 – 3473Combined sources
Beta strandi349 – 3546Combined sources
Helixi356 – 37015Combined sources
Helixi376 – 38813Combined sources
Helixi392 – 3943Combined sources
Beta strandi398 – 4036Combined sources
Helixi407 – 4104Combined sources
Helixi414 – 4229Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AECX-ray2.40A/B1-430[»]
ProteinModelPortaliQ43725.
SMRiQ43725. Positions 102-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni289 – 2935Pyridoxal phosphate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi49 – 546Poly-Ser
Compositional biasi380 – 3856Poly-Ala

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1252. Eukaryota.
COG0031. LUCA.
HOGENOMiHOG000217394.
InParanoidiQ43725.
KOiK01738.
PhylomeDBiQ43725.

Family and domain databases

InterProiIPR005856. Cys_synth.
IPR005859. CysK.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01139. cysK. 1 hit.
TIGR01136. cysKM. 1 hit.
PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q43725-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVAMIMASRF NREAKLASQI LSTLLGNRSC YTSMAATSSS ALLLNPLTSS
60 70 80 90 100
SSSSTLRRFR CSPEISSLSF SSASDFSLAM KRQSRSFADG SERDPSVVCE
110 120 130 140 150
AVKRETGPDG LNIADNVSQL IGKTPMVYLN SIAKGCVANI AAKLEIMEPC
160 170 180 190 200
CSVKDRIGYS MVTDAEQKGF ISPGKSVLVE PTSGNTGIGL AFIAASRGYR
210 220 230 240 250
LILTMPASMS MERRVLLKAF GAELVLTDPA KGMTGAVQKA EEILKNTPDA
260 270 280 290 300
YMLQQFDNPA NPKIHYETTG PEIWDDTKGK VDIFVAGIGT GGTITGVGRF
310 320 330 340 350
IKEKNPKTQV IGVEPTESDI LSGGKPGPHK IQGIGAGFIP KNLDQKIMDE
360 370 380 390 400
VIAISSEEAI ETAKQLALKE GLMVGISSGA AAAAAIKVAK RPENAGKLIA
410 420 430
VVFPSFGERY LSTPLFQSIR EEVEKMQPEV
Length:430
Mass (Da):45,815
Last modified:January 16, 2004 - v3
Checksum:i9DDEB1B8E314E143
GO

Sequence cautioni

The sequence CAA57498.1 differs from that shown. Reason: Frameshift at positions 5, 424 and 426. Curated
The sequence CAB75795.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491Missing in CAA57498 (PubMed:10319184).Curated
Sequence conflicti49 – 491Missing in CAB71290 (PubMed:10940562).Curated
Sequence conflicti73 – 731A → G in CAA57498 (PubMed:10319184).Curated
Sequence conflicti195 – 1951Missing in CAA57498 (PubMed:10319184).Curated
Sequence conflicti314 – 3141E → R in CAA57498 (PubMed:10319184).Curated
Sequence conflicti356 – 3572SE → ISKL in CAA57498 (PubMed:10319184).Curated
Sequence conflicti385 – 3851Missing in CAA57498 (PubMed:10319184).Curated
Sequence conflicti409 – 4091Missing in CAA57498 (PubMed:10319184).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81973 mRNA. Translation: CAA57498.1. Frameshift.
AL138647 Genomic DNA. Translation: CAB75795.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79963.1.
AY099721 mRNA. Translation: AAM20572.1.
AY128885 mRNA. Translation: AAM91285.1.
AJ271727 mRNA. Translation: CAB71290.1.
PIRiT47800.
T52650.
RefSeqiNP_191535.2. NM_115838.5. [Q43725-1]
UniGeneiAt.25336.

Genome annotation databases

EnsemblPlantsiAT3G59760.3; AT3G59760.3; AT3G59760. [Q43725-1]
GeneIDi825145.
KEGGiath:AT3G59760.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81973 mRNA. Translation: CAA57498.1. Frameshift.
AL138647 Genomic DNA. Translation: CAB75795.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79963.1.
AY099721 mRNA. Translation: AAM20572.1.
AY128885 mRNA. Translation: AAM91285.1.
AJ271727 mRNA. Translation: CAB71290.1.
PIRiT47800.
T52650.
RefSeqiNP_191535.2. NM_115838.5. [Q43725-1]
UniGeneiAt.25336.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AECX-ray2.40A/B1-430[»]
ProteinModelPortaliQ43725.
SMRiQ43725. Positions 102-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi10459. 4 interactions.
DIPiDIP-40500N.
IntActiQ43725. 3 interactions.
STRINGi3702.AT3G59760.1.

PTM databases

SwissPalmiQ43725.

Proteomic databases

PaxDbiQ43725.
PRIDEiQ43725.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G59760.3; AT3G59760.3; AT3G59760. [Q43725-1]
GeneIDi825145.
KEGGiath:AT3G59760.

Organism-specific databases

TAIRiAT3G59760.

Phylogenomic databases

eggNOGiKOG1252. Eukaryota.
COG0031. LUCA.
HOGENOMiHOG000217394.
InParanoidiQ43725.
KOiK01738.
PhylomeDBiQ43725.

Enzyme and pathway databases

UniPathwayiUPA00136; UER00200.
BioCyciARA:GQT-2188-MONOMER.
ARA:GQT-2189-MONOMER.
MetaCyc:AT3G59760-MONOMER.

Miscellaneous databases

PROiQ43725.

Gene expression databases

ExpressionAtlasiQ43725. baseline and differential.
GenevisibleiQ43725. AT.

Family and domain databases

InterProiIPR005856. Cys_synth.
IPR005859. CysK.
IPR001216. P-phosphate_BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01139. cysK. 1 hit.
TIGR01136. cysKM. 1 hit.
PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression analyses of mitochondrial and plastidic isoforms of cysteine synthase (O-acetylserine(thiol)lyase) from Arabidopsis thaliana."
    Hesse H., Lipke J., Altmann T., Hofgen R.
    Amino Acids 16:113-131(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Flower.
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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."
    Jost R., Berkowitz O., Wirtz M., Hopkins L., Hawkesford M.J., Hell R.
    Gene 253:237-247(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-430, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH SAT3.
    Strain: cv. Columbia.
  6. "beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like protein in spinach and Arabidopsis."
    Hatzfeld Y., Maruyama A., Schmidt A., Noji M., Ishizawa K., Saito K.
    Plant Physiol. 123:1163-1171(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  7. "O-acetylserine (thiol) lyase: an enigmatic enzyme of plant cysteine biosynthesis revisited in Arabidopsis thaliana."
    Wirtz M., Droux M., Hell R.
    J. Exp. Bot. 55:1785-1798(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  8. "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
    Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
    Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.
  9. "Synthesis of the sulfur amino acids: cysteine and methionine."
    Wirtz M., Droux M.
    Photosyn. Res. 86:345-362(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  10. "Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family demonstrates compartment-specific differences in the regulation of cysteine synthesis."
    Heeg C., Kruse C., Jost R., Gutensohn M., Ruppert T., Wirtz M., Hell R.
    Plant Cell 20:168-185(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Physiological roles of the beta-substituted alanine synthase gene family in Arabidopsis."
    Watanabe M., Kusano M., Oikawa A., Fukushima A., Noji M., Saito K.
    Plant Physiol. 146:310-320(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, FUNCTION, DISRUPTION PHENOTYPE.
  12. "A mechanistic model of the cysteine synthase complex."
    Feldman-Salit A., Wirtz M., Hell R., Wade R.C.
    J. Mol. Biol. 386:37-59(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF THE CYSTEINE SYNTHASE COMPLEX.
  13. "Enzymes of cysteine synthesis show extensive and conserved modifications patterns that include N(alpha)-terminal acetylation."
    Wirtz M., Heeg C., Samami A.A., Ruppert T., Hell R.
    Amino Acids 39:1077-1086(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  14. Cited for: COMPONENT OF THE CYSTEINE SYNTHASE COMPLEX.
  15. "Mitochondrial cysteine synthase complex regulates O-acetylserine biosynthesis in plants."
    Wirtz M., Beard K.F., Lee C.P., Boltz A., Schwarzlaender M., Fuchs C., Meyer A.J., Heeg C., Sweetlove L.J., Ratcliffe R.G., Hell R.
    J. Biol. Chem. 287:27941-27947(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SAT3, COMPONENT OF THE CYSTEINE SYNTHASE COMPLEX.
  16. "Mitochondrial sulfide detoxification requires a functional isoform O-acetylserine(thiol)lyase C in Arabidopsis thaliana."
    Alvarez C., Garcia I., Romero L.C., Gotor C.
    Mol. Plant 5:1217-1226(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  17. "Direct targeting of Arabidopsis cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis."
    Wawrzynska A., Kurzyk A., Mierzwinska M., Plochocka D., Wieczorek G., Sirko A.
    Plant Sci. 207:148-157(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SAT3.

Entry informationi

Entry nameiCYSKM_ARATH
AccessioniPrimary (citable) accession number: Q43725
Secondary accession number(s): Q8L4A2, Q9M1Z8, Q9M440
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 16, 2004
Last modified: June 8, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.