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Protein

Amidophosphoribosyltransferase 2, chloroplastic

Gene

ASE2

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

Functioni

Catalyzes the first committed step of 'de novo purine biosynthesis from glutamine. Required for chloroplast biogenesis and cell division. Confers sensitivity to the phenyltriazole acetic acid compound [5-(4-chlorophenyl)-1-isopropyl-1H-[1,2,4]triazol-3-yl]-acetic acid (DAS734), a bleaching herbicide.3 Publications

Catalytic activityi

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity
  • Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Enzyme regulationi

Inhibited by the phenyltriazole acetic acid compound [5-(4-chlorophenyl)-1-isopropyl-1H-[1,2,4]triazol-3-yl]-acetic acid (DAS734), a bleaching herbicide.1 Publication

Kineticsi

  1. KM=1.34 mM for glutamine1 Publication

    Pathway: IMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Amidophosphoribosyltransferase 2, chloroplastic (ASE2), Amidophosphoribosyltransferase 1, chloroplastic (ASE1), Amidophosphoribosyltransferase 3, chloroplastic (ASE3)
    2. Phosphoribosylamine--glycine ligase, chloroplastic (PUR2)
    This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei87 – 871NucleophilePROSITE-ProRule annotation
    Metal bindingi323 – 3231Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi469 – 4691Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi520 – 5201Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi523 – 5231Iron-sulfur (4Fe-4S)By similarity

    GO - Molecular functioni

    • amidophosphoribosyltransferase activity Source: TAIR
    • iron-sulfur cluster binding Source: UniProtKB-KW
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
    • chloroplast organization Source: TAIR
    • glutamine metabolic process Source: UniProtKB-KW
    • nucleoside metabolic process Source: InterPro
    • purine nucleobase biosynthetic process Source: InterPro
    • purine nucleotide biosynthetic process Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

    Iron, Iron-sulfur, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT4G34740-MONOMER.
    BRENDAi2.4.2.14. 399.
    ReactomeiREACT_350544. Purine ribonucleoside monophosphate biosynthesis.
    UniPathwayiUPA00074; UER00124.

    Protein family/group databases

    MEROPSiC44.A01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Amidophosphoribosyltransferase 2, chloroplastic (EC:2.4.2.14)
    Short name:
    AtATase2
    Short name:
    AtPURF2
    Short name:
    PRPP2
    Alternative name(s):
    Glutamine phosphoribosylpyrophosphate amidotransferase 2
    Short name:
    AtGPRAT2
    Protein CHLOROPLAST IMPORT APPARATUS 1
    Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS
    Gene namesi
    Name:ASE2
    Synonyms:CIA1, DOV1, GPRAT2, PURF2
    Ordered Locus Names:At4g34740
    ORF Names:T4L20.320
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G34740.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    • chloroplast stroma Source: TAIR
    • plastid stroma Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Disruption phenotypei

    Strong growth retardation and severe chlorosis in leaves; white leaves, but green cotyledons. Leaves missing the palisade mesophyll layer, due to reduced cell number and size. Abnormal thylakoid membrane in chloroplasts, probably due to photo-oxidative damage. Defective in protein import into chloroplasts.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi187 – 1871H → T in cia1-2; small plants with white leaves showing an irregular mosaic of green sectors. 1 Publication
    Mutagenesisi264 – 2641R → K: Strong resistance to the bleaching herbicides DAS073 and DAS734. 1 Publication
    Mutagenesisi265 – 2651P → S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494. 1 Publication
    Mutagenesisi371 – 3711G → S: Low resistance to the bleaching herbicides DAS073 and DAS734. 1 Publication
    Mutagenesisi476 – 4761P → S: Resistance to the bleaching herbicides DAS073 and DAS734. 1 Publication
    Mutagenesisi494 – 4941Y → F: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with S-265. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5353ChloroplastSequence AnalysisAdd
    BLAST
    Chaini54 – 561508Amidophosphoribosyltransferase 2, chloroplasticPRO_0000420282Add
    BLAST

    Proteomic databases

    PRIDEiQ9STG9.

    Expressioni

    Tissue specificityi

    Mostly expressed in leaves, and, to a lower extent, in cotyledons.3 Publications

    Interactioni

    Protein-protein interaction databases

    BioGridi14908. 4 interactions.
    IntActiQ9STG9. 4 interactions.
    STRINGi3702.AT4G34740.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9STG9.
    SMRiQ9STG9. Positions 87-537.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini87 – 307221Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.Curated
    Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Glutamine amidotransferase, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0034.
    HOGENOMiHOG000033688.
    InParanoidiQ9STG9.
    KOiK00764.
    OMAiIRDYIGC.
    PhylomeDBiQ9STG9.

    Family and domain databases

    Gene3Di3.40.50.2020. 1 hit.
    3.60.20.10. 1 hit.
    HAMAPiMF_01931. PurF.
    InterProiIPR017932. GATase_2_dom.
    IPR000583. GATase_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    IPR005854. PurF.
    [Graphical view]
    PfamiPF13537. GATase_7. 1 hit.
    PF00156. Pribosyltran. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000485. Amd_phspho_trans. 1 hit.
    SUPFAMiSSF53271. SSF53271. 1 hit.
    SSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR01134. purF. 1 hit.
    PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
    PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9STG9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAATSSISSS LSLNAKPNKL SNNNNNNKPH RFLRNPFLNP SSSSFSPLPA
    60 70 80 90 100
    SISSSSSSPS FPLRVSNPLT LLAADNDDYD EKPREECGVV GIYGDSEASR
    110 120 130 140 150
    LCYLALHALQ HRGQEGAGIV TVSKDKVLQT ITGVGLVSEV FSESKLDQLP
    160 170 180 190 200
    GDIAIGHVRY STAGSSMLKN VQPFVAGYRF GSVGVAHNGN LVNYTKLRAD
    210 220 230 240 250
    LEENGSIFNT SSDTEVVLHL IAISKARPFF MRIVDACEKL QGAYSMVFVT
    260 270 280 290 300
    EDKLVAVRDP HGFRPLVMGR RSNGAVVFAS ETCALDLIEA TYEREVYPGE
    310 320 330 340 350
    VLVVDKDGVK CQCLMPHPEP KQCIFEHIYF SLPNSIVFGR SVYESRHVFG
    360 370 380 390 400
    EILATESPVD CDVVIAVPDS GVVAALGYAA KAGVAFQQGL IRSHYVGRTF
    410 420 430 440 450
    IEPSQKIRDF GVKLKLSPVR GVLEGKRVVV VDDSIVRGTT SSKIVRLLRE
    460 470 480 490 500
    AGAKEVHMRI ASPPIIASCY YGVDTPSSNE LISNRMSVDE IRDYIGCDSL
    510 520 530 540 550
    AFLSFETLKK HLGEDSRSFC YACFTGDYPV KPTEDKVKRG GDFIDDGLVG
    560
    GIHNIEGGWV R
    Length:561
    Mass (Da):61,030
    Last modified:May 1, 2000 - v1
    Checksum:iAE52BD02CE304796
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51S → C in AAW28080 (Ref. 1) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY842241 Genomic DNA. Translation: AAW28080.1.
    AL023094 Genomic DNA. Translation: CAA18853.1.
    AL161586 Genomic DNA. Translation: CAB80191.1.
    CP002687 Genomic DNA. Translation: AEE86417.1.
    AY065123 mRNA. Translation: AAL38299.1.
    AY081611 mRNA. Translation: AAM10173.1.
    D28869 mRNA. Translation: BAA06024.1.
    PIRiT05294.
    RefSeqiNP_195200.1. NM_119640.2.
    UniGeneiAt.21088.

    Genome annotation databases

    EnsemblPlantsiAT4G34740.1; AT4G34740.1; AT4G34740.
    GeneIDi829626.
    KEGGiath:AT4G34740.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY842241 Genomic DNA. Translation: AAW28080.1.
    AL023094 Genomic DNA. Translation: CAA18853.1.
    AL161586 Genomic DNA. Translation: CAB80191.1.
    CP002687 Genomic DNA. Translation: AEE86417.1.
    AY065123 mRNA. Translation: AAL38299.1.
    AY081611 mRNA. Translation: AAM10173.1.
    D28869 mRNA. Translation: BAA06024.1.
    PIRiT05294.
    RefSeqiNP_195200.1. NM_119640.2.
    UniGeneiAt.21088.

    3D structure databases

    ProteinModelPortaliQ9STG9.
    SMRiQ9STG9. Positions 87-537.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi14908. 4 interactions.
    IntActiQ9STG9. 4 interactions.
    STRINGi3702.AT4G34740.1.

    Protein family/group databases

    MEROPSiC44.A01.

    Proteomic databases

    PRIDEiQ9STG9.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G34740.1; AT4G34740.1; AT4G34740.
    GeneIDi829626.
    KEGGiath:AT4G34740.

    Organism-specific databases

    GeneFarmi2374. 186.
    TAIRiAT4G34740.

    Phylogenomic databases

    eggNOGiCOG0034.
    HOGENOMiHOG000033688.
    InParanoidiQ9STG9.
    KOiK00764.
    OMAiIRDYIGC.
    PhylomeDBiQ9STG9.

    Enzyme and pathway databases

    UniPathwayiUPA00074; UER00124.
    BioCyciARA:AT4G34740-MONOMER.
    BRENDAi2.4.2.14. 399.
    ReactomeiREACT_350544. Purine ribonucleoside monophosphate biosynthesis.

    Miscellaneous databases

    PROiQ9STG9.

    Family and domain databases

    Gene3Di3.40.50.2020. 1 hit.
    3.60.20.10. 1 hit.
    HAMAPiMF_01931. PurF.
    InterProiIPR017932. GATase_2_dom.
    IPR000583. GATase_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    IPR005854. PurF.
    [Graphical view]
    PfamiPF13537. GATase_7. 1 hit.
    PF00156. Pribosyltran. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000485. Amd_phspho_trans. 1 hit.
    SUPFAMiSSF53271. SSF53271. 1 hit.
    SSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR01134. purF. 1 hit.
    PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
    PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Purine biosynthesis links chloroplast development and altered metal homeostasis in Arabidopsis thaliana."
      Maurer A., Rogers E.E.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. En-1.
    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. "Two amidophosphoribosyltransferase genes of Arabidopsis thaliana expressed in different organs."
      Ito T., Shiraishi H., Okada K., Shimura Y.
      Plant Mol. Biol. 26:529-533(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-561, TISSUE SPECIFICITY.
      Strain: cv. Landsberg erecta.
      Tissue: Flower, Leaf and Root.
    6. "Molecular analysis of 'de novo' purine biosynthesis in solanaceous species and in Arabidopsis thaliana."
      van der Graaff E., Hooykaas P., Lein W., Lerchl J., Kunze G., Sonnewald U., Boldt R.
      Front. Biosci. 9:1803-1816(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
      Strain: cv. C24.
    7. "Characterization of Arabidopsis glutamine phosphoribosyl pyrophosphate amidotransferase-deficient mutants."
      Hung W.-F., Chen L.-J., Boldt R., Sun C.-W., Li H.-M.
      Plant Physiol. 135:1314-1323(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF HIS-187, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
    8. "Chemical genetic identification of glutamine phosphoribosylpyrophosphate amidotransferase as the target for a novel bleaching herbicide in Arabidopsis."
      Walsh T.A., Bauer T., Neal R., Merlo A.O., Schmitzer P.R., Hicks G.R., Honma M., Matsumura W., Wolff K., Davies J.P.
      Plant Physiol. 144:1292-1304(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ARG-264; PRO-265; GLY-371; PRO-476 AND TYR-494, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
      Strain: cv. Columbia.
    9. "Sorting signals, N-terminal modifications and abundance of the chloroplast proteome."
      Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J.
      PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    10. "AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins."
      Ferro M., Brugiere S., Salvi D., Seigneurin-Berny D., Court M., Moyet L., Ramus C., Miras S., Mellal M., Le Gall S., Kieffer-Jaquinod S., Bruley C., Garin J., Joyard J., Masselon C., Rolland N.
      Mol. Cell. Proteomics 9:1063-1084(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    11. "Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering."
      Olinares P.D., Ponnala L., van Wijk K.J.
      Mol. Cell. Proteomics 9:1594-1615(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiASE2_ARATH
    AccessioniPrimary (citable) accession number: Q9STG9
    Secondary accession number(s): Q39000, Q5MAT8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2012
    Last sequence update: May 1, 2000
    Last modified: June 24, 2015
    This is version 115 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

    External Data

    Dasty 3

    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 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.