Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cysteine synthase 1

Gene

OASA1

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 major cysteine synthase, probably involved in maintaining organic sulfur level.3 Publications

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate2 Publications

Enzyme regulationi

Interaction with the sulfate transporter SULTR1;2 enhances its catalytic activity.1 Publication

Kineticsi

  1. KM=1.4 mM for O-acetylserine (at pH 7.0 and 25 degrees Celsius) for the cysteine synthase activity3 Publications
  2. KM=1.22 mM for O(3)-acetyl-L-serine for the cysteine synthase activity3 Publications
  3. KM=0.69 mM for O(3)-acetyl-L-serine for the cysteine synthase activity3 Publications
  4. KM=0.22 mM for Na2S (at pH 7.0 and 25 degrees Celsius) for the cysteine synthase activity3 Publications
  5. KM=5.6 µM for H2S for the cysteine synthase activity3 Publications
  1. Vmax=225 µmol/min/mg enzyme for L-cysteine for the cysteine synthase activity3 Publications
  2. Vmax=906 µmol/min/mg enzyme for L-cysteine for the cysteine synthase activity3 Publications
  3. Vmax=0.43 µmol/min/mg enzyme for H2S for the L-3-cyanoalanine synthase activity3 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 sitei77 – 771Pyridoxal phosphateCombined sources2 Publications
Binding sitei269 – 2691Pyridoxal phosphateCombined sources2 Publications

GO - Molecular functioni

  • cysteine synthase activity Source: TAIR
  • pyridoxal phosphate binding Source: GO_Central
  • transferase activity Source: UniProtKB-KW

GO - Biological processi

  • aging Source: TAIR
  • cysteine biosynthetic process Source: TAIR
  • cysteine biosynthetic process from serine Source: TAIR
  • double fertilization forming a zygote and endosperm Source: TAIR
  • pollen tube growth Source: TAIR
  • response to cadmium ion Source: TAIR
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-1813-MONOMER.
ARA:GQT-1814-MONOMER.
ARA:GQT-1815-MONOMER.
MetaCyc:AT4G14880-MONOMER.
BRENDAi2.5.1.47. 399.
SABIO-RKP47998.
UniPathwayiUPA00136; UER00200.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine synthase 1 (EC:2.5.1.47)
Alternative name(s):
At.OAS.5-8
Beta-substituted Ala synthase 1;1
Short name:
ARAth-Bsas1;1
CSase A
Short name:
AtCS-A
Cys-3A
O-acetylserine (thiol)-lyase 1
Short name:
OAS-TL A
O-acetylserine sulfhydrylase
Protein ONSET OF LEAF DEATH 3
Gene namesi
Name:OASA1
Synonyms:OAS1, OASS, OLD3
Ordered Locus Names:At4g14880
ORF Names:dl3480c
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G14880.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • cytosol Source: TAIR
  • membrane Source: TAIR
  • nucleus Source: TAIR
  • peroxisome Source: TAIR
  • plasma membrane Source: TAIR
  • vacuolar membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

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.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461K → A: No cysteine synthase activity. 1 Publication
Mutagenesisi74 – 741T → A: Strong reduction of cysteine synthase activity. 1 Publication
Mutagenesisi74 – 741T → S: Reduction of cysteine synthase activity. 1 Publication
Mutagenesisi75 – 751S → A, N or T: Strong reduction of cysteine synthase activity. 1 Publication
Mutagenesisi77 – 771N → A: Reduction of cysteine synthase activity. 1 Publication
Mutagenesisi77 – 771N → D: Strong reduction of cysteine synthase activity. 1 Publication
Mutagenesisi78 – 781T → A or S: Reduction of cysteine synthase activity. 1 Publication
Mutagenesisi147 – 1471Q → A or E: Strong reduction of cysteine synthase activity. 1 Publication
Mutagenesisi157 – 1571H → Q or N: Slight reduction of cysteine synthase activity. 1 Publication
Mutagenesisi162 – 1621G → E in old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity. 1 Publication
Mutagenesisi182 – 1821T → A or S: Slight reduction of cysteine synthase activity. 1 Publication
Mutagenesisi185 – 1851T → A or S: Strong reduction of cysteine synthase activity. 1 Publication
Mutagenesisi217 – 2171K → A: Impaired interaction with SAT1. 1 Publication
Mutagenesisi221 – 2211H → A: Impaired interaction with SAT1. 1 Publication
Mutagenesisi222 – 2221K → A: Impaired interaction with SAT1. 1 Publication
Mutagenesisi269 – 2691S → A: Strong reduction of cysteine synthase activity. 1 Publication
Mutagenesisi269 – 2691S → T: Reduction of cysteine synthase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 322321Cysteine synthase 1PRO_0000167116Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei46 – 461N6-(pyridoxal phosphate)lysineCombined sources2 Publications
Modified residuei178 – 1781PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP47998.
PRIDEiP47998.

PTM databases

iPTMnetiP47998.

Expressioni

Gene expression databases

GenevisibleiP47998. AT.

Interactioni

Subunit structurei

Homodimer. Interacts with SAT1. Component of the cysteine synthase complex (CSC) composed of two OAS-TL dimers and one SAT hexamer. Interacts with SULTR1;2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SULTR1;2Q9MAX35EBI-1633418,EBI-8772960

Protein-protein interaction databases

BioGridi12442. 8 interactions.
IntActiP47998. 5 interactions.
MINTiMINT-8061212.
STRINGi3702.AT4G14880.1.

Structurei

Secondary structure

1
322
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 124Combined sources
Beta strandi18 – 203Combined sources
Helixi23 – 253Combined sources
Beta strandi29 – 368Combined sources
Helixi37 – 393Combined sources
Helixi46 – 5914Combined sources
Turni65 – 673Combined sources
Beta strandi69 – 735Combined sources
Helixi77 – 8913Combined sources
Beta strandi92 – 987Combined sources
Helixi103 – 1119Combined sources
Beta strandi115 – 1195Combined sources
Helixi121 – 1233Combined sources
Helixi124 – 13815Combined sources
Beta strandi142 – 1443Combined sources
Turni147 – 1493Combined sources
Helixi152 – 1598Combined sources
Helixi161 – 1688Combined sources
Turni169 – 1713Combined sources
Beta strandi175 – 1795Combined sources
Beta strandi181 – 1833Combined sources
Helixi184 – 19613Combined sources
Beta strandi201 – 2077Combined sources
Helixi208 – 2103Combined sources
Helixi212 – 2143Combined sources
Helixi237 – 2393Combined sources
Beta strandi241 – 2466Combined sources
Helixi248 – 26215Combined sources
Helixi268 – 28114Combined sources
Helixi284 – 2863Combined sources
Beta strandi290 – 2956Combined sources
Helixi299 – 3024Combined sources
Beta strandi303 – 3053Combined sources
Helixi306 – 3083Combined sources
Helixi309 – 3168Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z7WX-ray2.20A1-322[»]
1Z7YX-ray2.70A1-322[»]
2ISQX-ray2.80A3-322[»]
ProteinModelPortaliP47998.
SMRiP47998. Positions 3-322.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47998.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 287144SUTR1;2 binding1 PublicationAdd
BLAST
Regioni181 – 1855Pyridoxal phosphate bindingCombined sources2 Publications
Regioni217 – 2226SAT1 binding1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1252. Eukaryota.
COG0031. LUCA.
InParanoidiP47998.
KOiK01738.
OMAiMGGANER.
PhylomeDBiP47998.

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.

P47998-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRIAKDVT ELIGNTPLVY LNNVAEGCVG RVAAKLEMME PCSSVKDRIG
60 70 80 90 100
FSMISDAEKK GLIKPGESVL IEPTSGNTGV GLAFTAAAKG YKLIITMPAS
110 120 130 140 150
MSTERRIILL AFGVELVLTD PAKGMKGAIA KAEEILAKTP NGYMLQQFEN
160 170 180 190 200
PANPKIHYET TGPEIWKGTG GKIDGFVSGI GTGGTITGAG KYLKEQNANV
210 220 230 240 250
KLYGVEPVES AILSGGKPGP HKIQGIGAGF IPSVLNVDLI DEVVQVSSDE
260 270 280 290 300
SIDMARQLAL KEGLLVGISS GAAAAAAIKL AQRPENAGKL FVAIFPSFGE
310 320
RYLSTVLFDA TRKEAEAMTF EA
Length:322
Mass (Da):33,805
Last modified:December 1, 2000 - v2
Checksum:i5B3E7F3D9DA5908B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201Missing in AAK76499 (PubMed:14593172).Curated
Sequence conflicti273 – 2731A → E in CAA58893 (PubMed:7729527).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80376 mRNA. Translation: CAA56593.2.
X84097 mRNA. Translation: CAA58893.1.
AJ272027 Genomic DNA. Translation: CAB72932.1.
Z97337 Genomic DNA. Translation: CAB10267.1.
AL161540 Genomic DNA. Translation: CAB78530.1.
CP002687 Genomic DNA. Translation: AEE83512.1.
CP002687 Genomic DNA. Translation: AEE83513.1.
CP002687 Genomic DNA. Translation: AEE83514.1.
CP002687 Genomic DNA. Translation: AEE83515.1.
AY045825 mRNA. Translation: AAK76499.1.
BT025878 mRNA. Translation: ABF85780.1.
PIRiA71412.
S48694.
RefSeqiNP_001190732.1. NM_001203803.1.
NP_001190733.1. NM_001203804.1.
NP_193224.1. NM_117574.3.
NP_849386.1. NM_179055.3.
UniGeneiAt.30.
At.34389.

Genome annotation databases

EnsemblPlantsiAT4G14880.1; AT4G14880.1; AT4G14880.
AT4G14880.2; AT4G14880.2; AT4G14880.
AT4G14880.3; AT4G14880.3; AT4G14880.
AT4G14880.4; AT4G14880.4; AT4G14880.
GeneIDi827145.
GrameneiAT4G14880.1; AT4G14880.1; AT4G14880.
AT4G14880.2; AT4G14880.2; AT4G14880.
AT4G14880.3; AT4G14880.3; AT4G14880.
AT4G14880.4; AT4G14880.4; AT4G14880.
KEGGiath:AT4G14880.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80376 mRNA. Translation: CAA56593.2.
X84097 mRNA. Translation: CAA58893.1.
AJ272027 Genomic DNA. Translation: CAB72932.1.
Z97337 Genomic DNA. Translation: CAB10267.1.
AL161540 Genomic DNA. Translation: CAB78530.1.
CP002687 Genomic DNA. Translation: AEE83512.1.
CP002687 Genomic DNA. Translation: AEE83513.1.
CP002687 Genomic DNA. Translation: AEE83514.1.
CP002687 Genomic DNA. Translation: AEE83515.1.
AY045825 mRNA. Translation: AAK76499.1.
BT025878 mRNA. Translation: ABF85780.1.
PIRiA71412.
S48694.
RefSeqiNP_001190732.1. NM_001203803.1.
NP_001190733.1. NM_001203804.1.
NP_193224.1. NM_117574.3.
NP_849386.1. NM_179055.3.
UniGeneiAt.30.
At.34389.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z7WX-ray2.20A1-322[»]
1Z7YX-ray2.70A1-322[»]
2ISQX-ray2.80A3-322[»]
ProteinModelPortaliP47998.
SMRiP47998. Positions 3-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi12442. 8 interactions.
IntActiP47998. 5 interactions.
MINTiMINT-8061212.
STRINGi3702.AT4G14880.1.

PTM databases

iPTMnetiP47998.

Proteomic databases

PaxDbiP47998.
PRIDEiP47998.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G14880.1; AT4G14880.1; AT4G14880.
AT4G14880.2; AT4G14880.2; AT4G14880.
AT4G14880.3; AT4G14880.3; AT4G14880.
AT4G14880.4; AT4G14880.4; AT4G14880.
GeneIDi827145.
GrameneiAT4G14880.1; AT4G14880.1; AT4G14880.
AT4G14880.2; AT4G14880.2; AT4G14880.
AT4G14880.3; AT4G14880.3; AT4G14880.
AT4G14880.4; AT4G14880.4; AT4G14880.
KEGGiath:AT4G14880.

Organism-specific databases

TAIRiAT4G14880.

Phylogenomic databases

eggNOGiKOG1252. Eukaryota.
COG0031. LUCA.
InParanoidiP47998.
KOiK01738.
OMAiMGGANER.
PhylomeDBiP47998.

Enzyme and pathway databases

UniPathwayiUPA00136; UER00200.
BioCyciARA:GQT-1813-MONOMER.
ARA:GQT-1814-MONOMER.
ARA:GQT-1815-MONOMER.
MetaCyc:AT4G14880-MONOMER.
BRENDAi2.5.1.47. 399.
SABIO-RKP47998.

Miscellaneous databases

EvolutionaryTraceiP47998.
PROiP47998.

Gene expression databases

GenevisibleiP47998. 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. "Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis thaliana."
    Hell R., Bork C., Bogdanova N., Frolov I., Hauschild R.
    FEBS Lett. 351:257-262(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Leaf.
  2. Hell R.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "A new member of the cytosolic O-acetylserine(thiol)lyase gene family in Arabidopsis thaliana."
    Barroso C., Vega J.M., Gotor C.
    FEBS Lett. 363:1-5(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "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 [GENOMIC DNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: cv. Columbia.
  5. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
    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.
    Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  6. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    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.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  7. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  8. "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.
  9. "Arabidopsis ORF clones."
    Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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: ACETYLATION AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
  16. "A mutation in the cytosolic O-acetylserine (thiol) lyase induces a genome-dependent early leaf death phenotype in Arabidopsis."
    Shirzadian-Khorramabad R., Jing H.C., Everts G.E., Schippers J.H., Hille J., Dijkwel P.P.
    BMC Plant Biol. 10:80-80(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-162, DISRUPTION PHENOTYPE, FUNCTION.
  17. "Binding of cysteine synthase to the STAS domain of sulfate transporter and its regulatory consequences."
    Shibagaki N., Grossman A.R.
    J. Biol. Chem. 285:25094-25102(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, INTERACTION WITH SULTR1;2, ENZYME REGULATION.
  18. "Identification of phosphoproteins in Arabidopsis thaliana leaves using polyethylene glycol fractionation, immobilized metal-ion affinity chromatography, two-dimensional gel electrophoresis and mass spectrometry."
    Aryal U.K., Krochko J.E., Ross A.R.
    J. Proteome Res. 11:425-437(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Molecular basis of cysteine biosynthesis in plants: structural and functional analysis of o-acetylserine sulfhydrylase from Arabidopsis thaliana."
    Bonner E.R., Cahoon R.E., Knapke S.M., Jez J.M.
    J. Biol. Chem. 280:38803-38813(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-46, COFACTOR, SUBUNIT, INTERACTION WITH SAT1, BIOPHYSICOCHEMICAL PROPERTIES, 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.
  20. "Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex."
    Francois J.A., Kumaran S., Jez J.M.
    Plant Cell 18:3647-3655(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 3-322, COFACTOR, SUBUNIT, INTERACTION WITH SAT1.

Entry informationi

Entry nameiCYSK1_ARATH
AccessioniPrimary (citable) accession number: P47998
Secondary accession number(s): O23343
, Q1EC56, Q42570, Q94AS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 1, 2000
Last modified: February 17, 2016
This is version 143 of the entry and version 2 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.