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Q9M111

- SUS3_ARATH

UniProt

Q9M111 - SUS3_ARATH

Protein

Sucrose synthase 3

Gene

SUS3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways. Modulates metabolic homeostasis and direct carbon towards starch synthesis in developing seeds.1 Publication

    Catalytic activityi

    NDP-glucose + D-fructose = NDP + sucrose.

    Kineticsi

    1. KM=41.96 mM for D-fructose (synthetic reaction) at pH 9.42 Publications
    2. KM=0.2 mM for UDP-glucose (synthetic reaction) at pH 9.42 Publications
    3. KM=108.2 mM for sucrose (degradative reaction) at pH 62 Publications
    4. KM=48 mM for sucrose (degradative reaction) at pH 72 Publications
    5. KM=0.09 mM for UDP (degradative reaction) at pH 62 Publications
    6. KM=0.25 mM for UDP (degradative reaction) at pH 72 Publications
    7. KM=0.15 mM for ADP (degradative reaction) at pH 72 Publications

    Vmax=7.32 µmol/min/mg enzyme for synthetic reaction at pH 9.42 Publications

    Vmax=3.03 µmol/min/mg enzyme for degradative reaction at pH 62 Publications

    Vmax=950 µmol/min/mg enzyme for degradative reaction at pH 72 Publications

    pH dependencei

    Optimum pH is 6.0-7.0 for degradative reaction and 7.0 (PubMed:22184213) or 9.0-9.5 (PubMed:17257168) for synthetic reaction.2 Publications

    GO - Molecular functioni

    1. sucrose synthase activity Source: UniProtKB

    GO - Biological processi

    1. biosynthetic process Source: InterPro
    2. response to mannitol Source: UniProtKB
    3. response to water deprivation Source: UniProtKB
    4. seed maturation Source: TAIR
    5. starch metabolic process Source: TAIR
    6. sucrose metabolic process Source: TAIR

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciMetaCyc:AT4G02280-MONOMER.

    Protein family/group databases

    CAZyiGT4. Glycosyltransferase Family 4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sucrose synthase 3 (EC:2.4.1.13)
    Short name:
    AtSUS3
    Alternative name(s):
    Sucrose-UDP glucosyltransferase 3
    Gene namesi
    Name:SUS3
    Ordered Locus Names:At4g02280
    ORF Names:T2H3.8
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G02280.

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Diminution of the starch content of developing seeds and increased lipid accumulation early during seed development.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 809809Sucrose synthase 3PRO_0000418802Add
    BLAST

    Proteomic databases

    PRIDEiQ9M111.

    Expressioni

    Tissue specificityi

    Detected in the whole plant with highest expression in developing siliques, vasculature of cotyledons and stomatal guard cells. Also detected throughout the mature parts of the root but not in the expanding zone.3 Publications

    Developmental stagei

    Highly expressed in late-maturing seeds and in geminating seeds (at the protein level).2 Publications

    Inductioni

    By drought stress. By mannitol, an osmotic agent. Positively regulated by LEC2.2 Publications

    Gene expression databases

    ArrayExpressiQ9M111.
    GenevestigatoriQ9M111.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9M111.
    SMRiQ9M111. Positions 25-808.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni277 – 755479GT-B glycosyltransferaseBy similarityAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    HOGENOMiHOG000240125.
    InParanoidiQ9M111.
    KOiK00695.
    OMAiFERCKED.
    PhylomeDBiQ9M111.

    Family and domain databases

    InterProiIPR001296. Glyco_trans_1.
    IPR000368. Sucrose_synth.
    IPR012820. Sucrose_synthase_pln/cyn.
    [Graphical view]
    PANTHERiPTHR12526:SF27. PTHR12526:SF27. 1 hit.
    PfamiPF00534. Glycos_transf_1. 1 hit.
    PF00862. Sucrose_synth. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02470. sucr_synth. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9M111-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANPKLTRVL STRDRVQDTL SAHRNELVAL LSRYVDQGKG ILQPHNLIDE    50
    LESVIGDDET KKSLSDGPFG EILKSAMEAI VVPPFVALAV RPRPGVWEYV 100
    RVNVFELSVE QLTVSEYLRF KEELVDGPNS DPFCLELDFE PFNANVPRPS 150
    RSSSIGNGVQ FLNRHLSSVM FRNKDCLEPL LDFLRVHKYK GHPLMLNDRI 200
    QSISRLQIQL SKAEDHISKL SQETPFSEFE YALQGMGFEK GWGDTAGRVL 250
    EMMHLLSDIL QAPDPSSLEK FLGMVPMVFN VVILSPHGYF GQANVLGLPD 300
    TGGQVVYILD QVRALETEML LRIKRQGLDI SPSILIVTRL IPDAKGTTCN 350
    QRLERVSGTE HTHILRVPFR SEKGILRKWI SRFDVWPYLE NYAQDAASEI 400
    VGELQGVPDF IIGNYSDGNL VASLMAHRMG VTQCTIAHAL EKTKYPDSDI 450
    YWKDFDNKYH FSCQFTADLI AMNNADFIIT STYQEIAGTK NTVGQYESHG 500
    AFTLPGLYRV VHGIDVFDPK FNIVSPGADM TIYFPYSEET RRLTALHGSI 550
    EEMLYSPDQT DEHVGTLSDR SKPILFSMAR LDKVKNISGL VEMYSKNTKL 600
    RELVNLVVIA GNIDVNKSKD REEIVEIEKM HNLMKNYKLD GQFRWITAQT 650
    NRARNGELYR YIADTRGAFA QPAFYEAFGL TVVEAMTCGL PTFATCHGGP 700
    AEIIEHGLSG FHIDPYHPEQ AGNIMADFFE RCKEDPNHWK KVSDAGLQRI 750
    YERYTWKIYS ERLMTLAGVY GFWKYVSKLE RRETRRYLEM FYILKFRDLV 800
    KTVPSTADD 809
    Length:809
    Mass (Da):92,002
    Last modified:October 1, 2000 - v1
    Checksum:iBC5151F2FBF265D5
    GO

    Sequence cautioni

    The sequence AAC28175.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF075597 Genomic DNA. Translation: AAC28175.1. Sequence problems.
    AL161494 Genomic DNA. Translation: CAB80721.1.
    CP002687 Genomic DNA. Translation: AEE82150.1.
    AY051001 mRNA. Translation: AAK93678.1.
    AY056784 mRNA. Translation: AAL09730.1.
    AY142511 mRNA. Translation: AAN13112.1.
    PIRiB85029.
    T01420.
    RefSeqiNP_192137.1. NM_116461.3.
    UniGeneiAt.3877.

    Genome annotation databases

    EnsemblPlantsiAT4G02280.1; AT4G02280.1; AT4G02280.
    GeneIDi828081.
    KEGGiath:AT4G02280.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF075597 Genomic DNA. Translation: AAC28175.1 . Sequence problems.
    AL161494 Genomic DNA. Translation: CAB80721.1 .
    CP002687 Genomic DNA. Translation: AEE82150.1 .
    AY051001 mRNA. Translation: AAK93678.1 .
    AY056784 mRNA. Translation: AAL09730.1 .
    AY142511 mRNA. Translation: AAN13112.1 .
    PIRi B85029.
    T01420.
    RefSeqi NP_192137.1. NM_116461.3.
    UniGenei At.3877.

    3D structure databases

    ProteinModelPortali Q9M111.
    SMRi Q9M111. Positions 25-808.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GT4. Glycosyltransferase Family 4.

    Proteomic databases

    PRIDEi Q9M111.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G02280.1 ; AT4G02280.1 ; AT4G02280 .
    GeneIDi 828081.
    KEGGi ath:AT4G02280.

    Organism-specific databases

    TAIRi AT4G02280.

    Phylogenomic databases

    HOGENOMi HOG000240125.
    InParanoidi Q9M111.
    KOi K00695.
    OMAi FERCKED.
    PhylomeDBi Q9M111.

    Enzyme and pathway databases

    BioCyci MetaCyc:AT4G02280-MONOMER.

    Gene expression databases

    ArrayExpressi Q9M111.
    Genevestigatori Q9M111.

    Family and domain databases

    InterProi IPR001296. Glyco_trans_1.
    IPR000368. Sucrose_synth.
    IPR012820. Sucrose_synthase_pln/cyn.
    [Graphical view ]
    PANTHERi PTHR12526:SF27. PTHR12526:SF27. 1 hit.
    Pfami PF00534. Glycos_transf_1. 1 hit.
    PF00862. Sucrose_synth. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02470. sucr_synth. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "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.
    4. "Structure and expression profile of the sucrose synthase multigene family in Arabidopsis."
      Baud S., Vaultier M.N., Rochat C.
      J. Exp. Bot. 55:397-409(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
    5. Cited for: BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    6. "Localization of sucrose synthase in developing seed and siliques of Arabidopsis thaliana reveals diverse roles for SUS during development."
      Fallahi H., Scofield G.N., Badger M.R., Chow W.S., Furbank R.T., Ruan Y.L.
      J. Exp. Bot. 59:3283-3295(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Arabidopsis sucrose synthase 2 and 3 modulate metabolic homeostasis and direct carbon towards starch synthesis in developing seeds."
      Angeles-Nunez J.G., Tiessen A.
      Planta 232:701-718(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "Regulation of AtSUS2 and AtSUS3 by glucose and the transcription factor LEC2 in different tissues and at different stages of Arabidopsis seed development."
      Angeles-Nunez J.G., Tiessen A.
      Plant Mol. Biol. 78:377-392(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY LEC2.
    9. "Sucrose synthase activity in the sus1/sus2/sus3/sus4 Arabidopsis mutant is sufficient to support normal cellulose and starch production."
      Baroja-Fernandez E., Munoz F.J., Li J., Bahaji A., Almagro G., Montero M., Etxeberria E., Hidalgo M., Sesma M.T., Pozueta-Romero J.
      Proc. Natl. Acad. Sci. U.S.A. 109:321-326(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiSUS3_ARATH
    AccessioniPrimary (citable) accession number: Q9M111
    Secondary accession number(s): Q9SBD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 90 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3