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

Serine acetyltransferase 4

Gene

SAT4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme regulationi

Feedback inhibitions by L-Ser and acetyl-CoA.1 Publication

Kineticsi

  1. KM=39.5 mM for L-Ser (at pH 8 and 30 degrees Celsius)1 Publication
  2. KM=45.1 mM for acetyl-CoA (at pH 8 and 30 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

    • cysteine biosynthetic process from serine Source: InterPro
    • sulfate assimilation Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis

    Enzyme and pathway databases

    UniPathwayiUPA00136; UER00199.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine acetyltransferase 4 (EC:2.3.1.30)
    Short name:
    AtSAT-4
    Short name:
    AtSERAT3;2
    Gene namesi
    Name:SAT4
    Ordered Locus Names:At4g35640
    ORF Names:F8D20.150
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G35640.

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • cytosol Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 355355Serine acetyltransferase 4PRO_0000068692Add
    BLAST

    Proteomic databases

    PaxDbiQ8W2B8.
    PRIDEiQ8W2B8.

    PTM databases

    iPTMnetiQ8W2B8.

    Expressioni

    Tissue specificityi

    Localized in vascular tissues, particularly in phloem.1 Publication

    Inductioni

    By cadmium (Cd). Induced in roots and shoots under sulfur-deficient conditions.1 Publication

    Interactioni

    Subunit structurei

    Homomultimer.By similarity

    Protein-protein interaction databases

    BioGridi14998. 2 interactions.
    MINTiMINT-8061727.
    STRINGi3702.AT4G35640.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8W2B8.
    SMRiQ8W2B8. Positions 73-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi12 – 198Poly-Ser

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG410INAF. Eukaryota.
    COG1045. LUCA.
    HOGENOMiHOG000049437.
    InParanoidiQ8W2B8.
    KOiK00640.
    OMAiDEFPFER.
    PhylomeDBiQ8W2B8.

    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. 1 hit.
    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.

    Q8W2B8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MACINGENRD FSSSSSLSSL PMIVSRNFSA RDDGETGDEF PFERIFPVYA
    60 70 80 90 100
    RGTLNPVADP VLLDFTNSSY DPIWDSIREE AKLEAEEEPV LSSFLYASIL
    110 120 130 140 150
    SHDCLEQALS FVLANRLQNP TLLATQLMDI FCNVMVHDRG IQSSIRLDVQ
    160 170 180 190 200
    AFKDRDPACL SYSSAILHLK GYLALQAYRV AHKLWKQGRK LLALALQSRV
    210 220 230 240 250
    SEVFGIDIHP AARIGKGILL DHGTGVVIGE TAVIGDRVSI LHGVTLGGTG
    260 270 280 290 300
    KETGDRHPNI GDGALLGACV TILGNIKIGA GAMVAAGSLV LKDVPSHSMV
    310 320 330 340 350
    AGNPAKLIGF VDEQDPSMTM EHDATREFFQ NVAVAYRETI PNGSSVSGSC

    RERRH
    Length:355
    Mass (Da):38,424
    Last modified:March 1, 2002 - v1
    Checksum:i3BF39845776C0EC7
    GO

    Sequence cautioni

    The sequence CAA20034.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
    The sequence CAB80280.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF331847 Genomic DNA. Translation: AAL37489.1.
    AL031135 Genomic DNA. Translation: CAA20034.1. Sequence problems.
    AL161587 Genomic DNA. Translation: CAB80280.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE86543.1.
    BT004080 mRNA. Translation: AAO42107.1.
    BT005047 mRNA. Translation: AAO50580.1.
    PIRiT04669.
    RefSeqiNP_195289.3. NM_119729.4.
    UniGeneiAt.19734.
    At.71197.

    Genome annotation databases

    EnsemblPlantsiAT4G35640.1; AT4G35640.1; AT4G35640.
    GeneIDi829716.
    GrameneiAT4G35640.1; AT4G35640.1; AT4G35640.
    KEGGiath:AT4G35640.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF331847 Genomic DNA. Translation: AAL37489.1.
    AL031135 Genomic DNA. Translation: CAA20034.1. Sequence problems.
    AL161587 Genomic DNA. Translation: CAB80280.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE86543.1.
    BT004080 mRNA. Translation: AAO42107.1.
    BT005047 mRNA. Translation: AAO50580.1.
    PIRiT04669.
    RefSeqiNP_195289.3. NM_119729.4.
    UniGeneiAt.19734.
    At.71197.

    3D structure databases

    ProteinModelPortaliQ8W2B8.
    SMRiQ8W2B8. Positions 73-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi14998. 2 interactions.
    MINTiMINT-8061727.
    STRINGi3702.AT4G35640.1.

    PTM databases

    iPTMnetiQ8W2B8.

    Proteomic databases

    PaxDbiQ8W2B8.
    PRIDEiQ8W2B8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G35640.1; AT4G35640.1; AT4G35640.
    GeneIDi829716.
    GrameneiAT4G35640.1; AT4G35640.1; AT4G35640.
    KEGGiath:AT4G35640.

    Organism-specific databases

    TAIRiAT4G35640.

    Phylogenomic databases

    eggNOGiENOG410INAF. Eukaryota.
    COG1045. LUCA.
    HOGENOMiHOG000049437.
    InParanoidiQ8W2B8.
    KOiK00640.
    OMAiDEFPFER.
    PhylomeDBiQ8W2B8.

    Enzyme and pathway databases

    UniPathwayiUPA00136; UER00199.

    Miscellaneous databases

    PROiQ8W2B8.

    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. 1 hit.
    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. "Characterization of a new serine acetyltransferase (SAT4) from Arabidopsis thaliana."
      Buisson S., Droux M.
      Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.
    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. "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: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiSAT4_ARATH
    AccessioniPrimary (citable) accession number: Q8W2B8
    Secondary accession number(s): O81795
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: March 1, 2002
    Last modified: June 8, 2016
    This is version 87 of the entry and version 1 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.