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Protein

Cysteine synthase, chloroplastic/chromoplastic

Gene

OASB

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.2 Publications

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=0.81 mM for O(3)-acetyl-L-serine for the cysteine synthase activity2 Publications
  2. KM=0.31 mM for O(3)-acetyl-L-serine for the cysteine synthase activity2 Publications
  3. KM=3.0 µM for H2S for the cysteine synthase activity2 Publications
  1. Vmax=171 µmol/min/mg enzyme for L-cysteine for the cysteine synthase activity2 Publications
  2. Vmax=592 µmol/min/mg enzyme for L-cysteine for the cysteine synthase activity2 Publications
  3. Vmax=0.37 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 sitei147 – 1471Pyridoxal phosphateBy similarity
Binding sitei339 – 3391Pyridoxal phosphateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • cysteine biosynthetic process Source: TAIR
  • cysteine biosynthetic process from serine Source: GO_Central
  • double fertilization forming a zygote and endosperm Source: TAIR
  • pollen tube growth Source: TAIR
  • response to cadmium ion Source: TAIR
  • response to cytokinin 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-2305-MONOMER.
MetaCyc:AT2G43750-MONOMER.
UniPathwayiUPA00136; UER00200.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine synthase, chloroplastic/chromoplastic (EC:2.5.1.47)
Alternative name(s):
At.OAS.7-4
Beta-substituted Ala synthase 2;1
Short name:
ARAth-Bsas2;1
CSase B
Short name:
AtCS-B
Short name:
CS-B
O-acetylserine (thiol)-lyase
O-acetylserine sulfhydrylase
OAS-TL B
cpACS1
Gene namesi
Name:OASB
Ordered Locus Names:At2g43750
ORF Names:F18O19.14
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G43750.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
  • chromoplast Source: UniProtKB-SubCell
  • endosome Source: TAIR
  • Golgi apparatus Source: TAIR
  • mitochondrion Source: TAIR
  • plastid Source: TAIR
  • trans-Golgi network Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Chromoplast, Plastid

Pathology & Biotechi

Disruption phenotypei

No visible phenotype.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6060Chloroplast and chromoplastCombined sourcesAdd
BLAST
Chaini61 – 392332Cysteine synthase, chloroplastic/chromoplasticPRO_0000006349Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611N-acetylalanineCombined sources1 Publication
Modified residuei116 – 1161N6-(pyridoxal phosphate)lysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP47999.
PRIDEiP47999.

2D gel databases

SWISS-2DPAGEP47999.

PTM databases

iPTMnetiP47999.

Expressioni

Gene expression databases

ExpressionAtlasiP47999. baseline and differential.
GenevisibleiP47999. AT.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi4314. 4 interactions.
IntActiP47999. 1 interaction.
STRINGi3702.AT2G43750.1.

Structurei

3D structure databases

ProteinModelPortaliP47999.
SMRiP47999. Positions 72-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni251 – 2555Pyridoxal phosphate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi342 – 3476Poly-Ala

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1252. Eukaryota.
COG0031. LUCA.
HOGENOMiHOG000217394.
InParanoidiP47999.
KOiK01738.
OMAiLSTPMFS.
PhylomeDBiP47999.

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.

P47999-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATSSSAFL LNPLTSRHRP FKYSPELSSL SLSSRKAAAF DVSSAAFTLK
60 70 80 90 100
RQSRSDVVCK AVSIKPEAGV EGLNIADNAA QLIGKTPMVY LNNVVKGCVA
110 120 130 140 150
SVAAKLEIME PCCSVKDRIG YSMITDAEEK GLITPGKSVL VESTSGNTGI
160 170 180 190 200
GLAFIAASKG YKLILTMPAS MSLERRVLLR AFGAELVLTE PAKGMTGAIQ
210 220 230 240 250
KAEEILKKTP NSYMLQQFDN PANPKIHYET TGPEIWEDTR GKIDILVAGI
260 270 280 290 300
GTGGTITGVG RFIKERKPEL KVIGVEPTES AILSGGKPGP HKIQGIGAGF
310 320 330 340 350
VPKNLDLAIV DEYIAISSEE AIETSKQLAL QEGLLVGISS GAAAAAAIQV
360 370 380 390
AKRPENAGKL IAVVFPSFGE RYLSTQLFQS IREECEQMQP EL
Length:392
Mass (Da):41,656
Last modified:December 1, 2000 - v2
Checksum:iB1220F01E8E31A12
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti232 – 2321G → N in CAA57344 (PubMed:7610184).Curated
Sequence conflicti288 – 2881P → T in CAA57344 (PubMed:7610184).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80377 mRNA. Translation: CAA56594.2.
X81698 mRNA. Translation: CAA57344.1.
AJ271728 Genomic DNA. Translation: CAB71292.1.
AC002333 Genomic DNA. Translation: AAB64031.1.
CP002685 Genomic DNA. Translation: AEC10317.1.
CP002685 Genomic DNA. Translation: AEC10318.1.
AY065375 mRNA. Translation: AAL38816.1.
AY096681 mRNA. Translation: AAM20315.1.
AY086156 mRNA. Translation: AAM63361.1.
PIRiA84870.
S48695.
RefSeqiNP_001189745.1. NM_001202816.1.
NP_181903.1. NM_129937.3.
UniGeneiAt.20491.
At.72689.

Genome annotation databases

EnsemblPlantsiAT2G43750.1; AT2G43750.1; AT2G43750.
AT2G43750.2; AT2G43750.2; AT2G43750.
GeneIDi818978.
GrameneiAT2G43750.1; AT2G43750.1; AT2G43750.
AT2G43750.2; AT2G43750.2; AT2G43750.
KEGGiath:AT2G43750.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80377 mRNA. Translation: CAA56594.2.
X81698 mRNA. Translation: CAA57344.1.
AJ271728 Genomic DNA. Translation: CAB71292.1.
AC002333 Genomic DNA. Translation: AAB64031.1.
CP002685 Genomic DNA. Translation: AEC10317.1.
CP002685 Genomic DNA. Translation: AEC10318.1.
AY065375 mRNA. Translation: AAL38816.1.
AY096681 mRNA. Translation: AAM20315.1.
AY086156 mRNA. Translation: AAM63361.1.
PIRiA84870.
S48695.
RefSeqiNP_001189745.1. NM_001202816.1.
NP_181903.1. NM_129937.3.
UniGeneiAt.20491.
At.72689.

3D structure databases

ProteinModelPortaliP47999.
SMRiP47999. Positions 72-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4314. 4 interactions.
IntActiP47999. 1 interaction.
STRINGi3702.AT2G43750.1.

PTM databases

iPTMnetiP47999.

2D gel databases

SWISS-2DPAGEP47999.

Proteomic databases

PaxDbiP47999.
PRIDEiP47999.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G43750.1; AT2G43750.1; AT2G43750.
AT2G43750.2; AT2G43750.2; AT2G43750.
GeneIDi818978.
GrameneiAT2G43750.1; AT2G43750.1; AT2G43750.
AT2G43750.2; AT2G43750.2; AT2G43750.
KEGGiath:AT2G43750.

Organism-specific databases

TAIRiAT2G43750.

Phylogenomic databases

eggNOGiKOG1252. Eukaryota.
COG0031. LUCA.
HOGENOMiHOG000217394.
InParanoidiP47999.
KOiK01738.
OMAiLSTPMFS.
PhylomeDBiP47999.

Enzyme and pathway databases

UniPathwayiUPA00136; UER00200.
BioCyciARA:GQT-2305-MONOMER.
MetaCyc:AT2G43750-MONOMER.

Miscellaneous databases

PROiP47999.

Gene expression databases

ExpressionAtlasiP47999. baseline and differential.
GenevisibleiP47999. 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 [MRNA].
  3. "Molecular cloning of a cysteine synthase cDNA from Arabidopsis thaliana."
    Hesse H., Altmann T.
    Plant Physiol. 108:851-852(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  6. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  7. "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.
  8. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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-61, IDENTIFICATION BY MASS SPECTROMETRY.
  15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-61, CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER LYS-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCYSKP_ARATH
AccessioniPrimary (citable) accession number: P47999
Secondary accession number(s): O22828, Q42568
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 1, 2000
Last modified: February 17, 2016
This is version 139 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.