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Protein

Serine acetyltransferase 1, chloroplastic

Gene

SAT1

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

Functioni

May be involved in detoxification process by mediating the production of glutathione.

Catalytic activityi

Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine.

Kineticsi

  1. KM=1.64 mM for L-Ser (at pH 8 and 37 degrees Celsius)1 Publication
  2. KM=0.16 mM for acetyl-CoA (at pH 8 and 37 degrees Celsius)1 Publication

    Pathwayi: L-cysteine biosynthesis

    This protein is involved in step 1 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.

    GO - Molecular functioni

    • serine O-acetyltransferase activity Source: TAIR

    GO - Biological processi

    • cellular response to sulfate starvation Source: TAIR
    • cysteine biosynthetic process from serine Source: InterPro
    • response to cold Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis

    Enzyme and pathway databases

    BioCyciARA:AT1G55920-MONOMER.
    MetaCyc:AT1G55920-MONOMER.
    BRENDAi2.3.1.30. 399.
    SABIO-RKQ42588.
    UniPathwayiUPA00136; UER00199.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine acetyltransferase 1, chloroplastic (EC:2.3.1.30)
    Short name:
    AtSAT-1
    Alternative name(s):
    AtSERAT2;1
    SAT-p
    Gene namesi
    Name:SAT1
    Synonyms:SAT5
    Ordered Locus Names:At1g55920
    ORF Names:F14J16.18
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 1

    Organism-specific databases

    TAIRiAT1G55920.

    Subcellular locationi

    • Plastidchloroplast 1 Publication
    • Cytoplasm 1 Publication

    • Note: First chloroplastic and progressively cytoplasmic during aging.

    GO - Cellular componenti

    • chloroplast Source: TAIR
    • cytosol Source: TAIR
    • nucleus Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Cytoplasm, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 314314Serine acetyltransferase 1, chloroplasticPRO_0000068690Add
    BLAST

    Proteomic databases

    PaxDbiQ42588.
    PRIDEiQ42588.

    Expressioni

    Tissue specificityi

    Mostly expressed in leaves. Localized in cortex, trichomes and vascular tissues, particularly in phloem.4 Publications

    Inductioni

    By cadmium (Cd). Not induced under sulfur-deficient conditions. Repressed in trichomes in response to NaCl treatment.3 Publications

    Gene expression databases

    GenevisibleiQ42588. AT.

    Interactioni

    Subunit structurei

    Homomultimer (By similarity). Interacts with OASA1 and CYP20-3. Component of the cysteine synthase complex (CSC) composed of two OAS-TL dimers and one SAT hexamer.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi27268. 2 interactions.
    DIPiDIP-40647N.
    IntActiQ42588. 1 interaction.
    STRINGi3702.AT1G55920.1.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ISQX-ray2.80B307-314[»]
    ProteinModelPortaliQ42588.
    SMRiQ42588. Positions 48-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ42588.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG410INAF. Eukaryota.
    COG1045. LUCA.
    HOGENOMiHOG000049437.
    InParanoidiQ42588.
    KOiK00640.
    OMAiYASITSH.
    PhylomeDBiQ42588.

    Family and domain databases

    InterProiIPR001451. Hexapep.
    IPR018357. Hexapep_transf_CS.
    IPR010493. Ser_AcTrfase_N.
    IPR005881. Ser_O-AcTrfase.
    IPR011004. Trimer_LpxA-like.
    [Graphical view]
    PfamiPF00132. Hexapep. 2 hits.
    PF06426. SATase_N. 1 hit.
    [Graphical view]
    SMARTiSM00971. SATase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51161. SSF51161. 1 hit.
    TIGRFAMsiTIGR01172. cysE. 1 hit.
    PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q42588-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATCIDTCRT GNTQDDDSRF CCIKNFFRPG FSVNRKIHHT QIEDDDDVWI
    60 70 80 90 100
    KMLEEAKSDV KQEPILSNYY YASITSHRSL ESALAHILSV KLSNLNLPSN
    110 120 130 140 150
    TLFELFISVL EESPEIIEST KQDLIAVKER DPACISYVHC FLGFKGFLAC
    160 170 180 190 200
    QAHRIAHTLW KQNRKIVALL IQNRVSESFA VDIHPGAKIG KGILLDHATG
    210 220 230 240 250
    VVIGETAVVG DNVSILHGVT LGGTGKQSGD RHPKIGDGVL IGAGSCILGN
    260 270 280 290 300
    ITIGEGAKIG SGSVVVKDVP ARTTAVGNPA RLIGGKENPR KHDKIPCLTM
    310
    DQTSYLTEWS DYVI
    Length:314
    Mass (Da):34,251
    Last modified:January 24, 2006 - v2
    Checksum:i78FACE3DA5CE04B0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61D → H in AAC37474 (PubMed:8867790).Curated
    Sequence conflicti24 – 252KN → NK in AAC37474 (PubMed:8867790).Curated
    Sequence conflicti54 – 541E → K in AAC37474 (PubMed:8867790).Curated
    Sequence conflicti57 – 571K → E in AAC37474 (PubMed:8867790).Curated
    Sequence conflicti85 – 851A → G in AAC37474 (PubMed:8867790).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L42212 mRNA. Translation: AAC37474.1.
    L34076 Genomic RNA. Translation: AAA58608.1.
    Z34888 Genomic DNA. Translation: CAA84371.1.
    AC002304 Genomic DNA. Translation: AAF79319.1.
    CP002684 Genomic DNA. Translation: AEE33320.1.
    BT008309 mRNA. Translation: AAP37668.1.
    AK227691 mRNA. Translation: BAE99678.1.
    PIRiS67482.
    S71181.
    RefSeqiNP_175988.1. NM_104470.2.
    UniGeneiAt.24052.

    Genome annotation databases

    EnsemblPlantsiAT1G55920.1; AT1G55920.1; AT1G55920.
    GeneIDi842043.
    GrameneiAT1G55920.1; AT1G55920.1; AT1G55920.
    KEGGiath:AT1G55920.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L42212 mRNA. Translation: AAC37474.1.
    L34076 Genomic RNA. Translation: AAA58608.1.
    Z34888 Genomic DNA. Translation: CAA84371.1.
    AC002304 Genomic DNA. Translation: AAF79319.1.
    CP002684 Genomic DNA. Translation: AEE33320.1.
    BT008309 mRNA. Translation: AAP37668.1.
    AK227691 mRNA. Translation: BAE99678.1.
    PIRiS67482.
    S71181.
    RefSeqiNP_175988.1. NM_104470.2.
    UniGeneiAt.24052.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ISQX-ray2.80B307-314[»]
    ProteinModelPortaliQ42588.
    SMRiQ42588. Positions 48-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi27268. 2 interactions.
    DIPiDIP-40647N.
    IntActiQ42588. 1 interaction.
    STRINGi3702.AT1G55920.1.

    Proteomic databases

    PaxDbiQ42588.
    PRIDEiQ42588.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT1G55920.1; AT1G55920.1; AT1G55920.
    GeneIDi842043.
    GrameneiAT1G55920.1; AT1G55920.1; AT1G55920.
    KEGGiath:AT1G55920.

    Organism-specific databases

    TAIRiAT1G55920.

    Phylogenomic databases

    eggNOGiENOG410INAF. Eukaryota.
    COG1045. LUCA.
    HOGENOMiHOG000049437.
    InParanoidiQ42588.
    KOiK00640.
    OMAiYASITSH.
    PhylomeDBiQ42588.

    Enzyme and pathway databases

    UniPathwayiUPA00136; UER00199.
    BioCyciARA:AT1G55920-MONOMER.
    MetaCyc:AT1G55920-MONOMER.
    BRENDAi2.3.1.30. 399.
    SABIO-RKQ42588.

    Miscellaneous databases

    EvolutionaryTraceiQ42588.
    PROiQ42588.

    Gene expression databases

    GenevisibleiQ42588. AT.

    Family and domain databases

    InterProiIPR001451. Hexapep.
    IPR018357. Hexapep_transf_CS.
    IPR010493. Ser_AcTrfase_N.
    IPR005881. Ser_O-AcTrfase.
    IPR011004. Trimer_LpxA-like.
    [Graphical view]
    PfamiPF00132. Hexapep. 2 hits.
    PF06426. SATase_N. 1 hit.
    [Graphical view]
    SMARTiSM00971. SATase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51161. SSF51161. 1 hit.
    TIGRFAMsiTIGR01172. cysE. 1 hit.
    PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Serine acetyltransferase from Arabidopsis thaliana can functionally complement the cysteine requirement of a cysE mutant strain of Escherichia coli."
      Murillo M., Foglia R., Diller A., Lee S., Leustek T.
      Cell. Mol. Biol. Res. 41:425-433(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: cv. Columbia.
    2. "Subcellular distribution of serine acetyltransferase from Pisum sativum and characterization of an Arabidopsis thaliana putative cytosolic isoform."
      Ruffet M.-L., Lebrun M., Droux M., Douce R.
      Eur. J. Biochem. 227:500-509(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Columbia.
    3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "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.
    6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    7. "Isoform-dependent differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana."
      Noji M., Inoue K., Kimura N., Gouda A., Saito K.
      J. Biol. Chem. 273:32739-32745(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
    8. Cited for: TISSUE SPECIFICITY, INDUCTION.
    9. "The serine acetyltransferase gene family in Arabidopsis thaliana and the regulation of its expression by cadmium."
      Howarth J.R., Dominguez-Solis J.R., Gutierrez-Alcala G., Wray J.L., Romero L.C., Gotor C.
      Plant Mol. Biol. 51:589-598(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
      Strain: cv. Columbia.
    10. "Characterization and expression analysis of a serine acetyltransferase gene family involved in a key step of the sulfur assimilation pathway in Arabidopsis."
      Kawashima C.G., Berkowitz O., Hell R., Noji M., Saito K.
      Plant Physiol. 137:220-230(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, NOMENCLATURE.
    11. "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: INTERACTION WITH OASA1.
    12. "A cyclophilin links redox and light signals to cysteine biosynthesis and stress responses in chloroplasts."
      Dominguez-Solis J.R., He Z., Lima A., Ting J., Buchanan B.B., Luan S.
      Proc. Natl. Acad. Sci. U.S.A. 105:16386-16391(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CYP20-3.
    13. "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 307-314, INTERACTION WITH OASA1.

    Entry informationi

    Entry nameiSAT1_ARATH
    AccessioniPrimary (citable) accession number: Q42588
    Secondary accession number(s): Q0WT70, Q43297
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: January 24, 2006
    Last modified: February 17, 2016
    This is version 113 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.