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Protein

UDP-glucose 4-epimerase 2

Gene

UGE2

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

Functioni

Catalyzes the interconversion between UDP-glucose and UDP-galactose. Cooperates with UGE3 in pollen development and with UGE4 in cell wall carbohydrate biosynthesis and growth.4 Publications

Catalytic activityi

UDP-alpha-D-glucose = UDP-alpha-D-galactose.

Cofactori

NAD+By similarity

Enzyme regulationi

Enhanced activity by NaCl. Enhanced activity by NAD+. Strongly inhibited by UDP.1 Publication

Kineticsi

  1. KM=0.09 mM for UDP-glucose2 Publications
  2. KM=0.13 mM for UDP-galactose2 Publications
  3. KM=0.095 mM for UDP-galactose2 Publications
  4. KM=0.34 mM for UDP-xylose2 Publications

    pH dependencei

    Optimum pH is 7.0-9.0.2 Publications

    Temperature dependencei

    Optimum temperature is 40 degrees Celsius.2 Publications

    Pathwayi: galactose metabolism

    This protein is involved in the pathway galactose metabolism, which is part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the pathway galactose metabolism and in Carbohydrate metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei129 – 1291SubstrateBy similarity
    Active sitei153 – 1531Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi4 – 3532NADBy similarityAdd
    BLAST

    GO - Molecular functioni

    • UDP-glucose 4-epimerase activity Source: TAIR

    GO - Biological processi

    • cell wall biogenesis Source: TAIR
    • cell wall organization Source: UniProtKB-KW
    • galactose metabolic process Source: UniProtKB-UniPathway
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism, Cell wall biogenesis/degradation, Galactose metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BRENDAi5.1.3.2. 399.
    5.1.3.5. 399.
    ReactomeiR-ATH-70370. Galactose catabolism.
    SABIO-RKQ9T0A7.
    UniPathwayiUPA00214.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-glucose 4-epimerase 2 (EC:5.1.3.2)
    Short name:
    AtUGE2
    Alternative name(s):
    UDP-galactose 4-epimerase 2
    Gene namesi
    Name:UGE2
    Ordered Locus Names:At4g23920
    ORF Names:T32A16.90
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G23920.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Uge2 and uge3 double mutant is almost completely sterile. Uge2 and uge4 double mutant displays a reduction in rosette and root growth, hypocotyl elongation, and secondary hypocotyl thickening (PubMed:17496119).1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 350350UDP-glucose 4-epimerase 2PRO_0000183195Add
    BLAST

    Proteomic databases

    PaxDbiQ9T0A7.
    PRIDEiQ9T0A7.

    Expressioni

    Tissue specificityi

    Ubiquitous. Most highly expressed in stems and flowers.4 Publications

    Gene expression databases

    GenevisibleiQ9T0A7. AT.

    Interactioni

    Subunit structurei

    homodimer. Heterodimer.1 Publication

    Protein-protein interaction databases

    BioGridi13781. 2 interactions.
    IntActiQ9T0A7. 2 interactions.
    STRINGi3702.AT4G23920.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9T0A7.
    SMRiQ9T0A7. Positions 1-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1371. Eukaryota.
    COG1087. LUCA.
    HOGENOMiHOG000168001.
    InParanoidiQ9T0A7.
    KOiK01784.
    OMAiCGCKVYN.
    PhylomeDBiQ9T0A7.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR005886. GalE.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF16363. GDP_Man_Dehyd. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01179. galE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9T0A7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAKSVLVTGG AGYIGSHTVL QLLEGGYSAV VVDNYDNSSA ASLQRVKKLA
    60 70 80 90 100
    GENGNRLSFH QVDLRDRPAL EKIFSETKFD AVIHFAGLKA VGESVEKPLL
    110 120 130 140 150
    YYNNNIVGTV TLLEVMAQYG CKNLVFSSSA TVYGWPKEVP CTEESPISAT
    160 170 180 190 200
    NPYGRTKLFI EEICRDVHRS DSEWKIILLR YFNPVGAHPS GYIGEDPLGV
    210 220 230 240 250
    PNNLMPYVQQ VAVGRRPHLT VFGTDYKTKD GTGVRDYIHV MDLADGHIAA
    260 270 280 290 300
    LRKLDDLKIS CEVYNLGTGN GTSVLEMVAA FEKASGKKIP LVMAGRRPGD
    310 320 330 340 350
    AEVVYASTEK AERELNWKAK NGIEEMCRDL WNWASNNPYG YNSSSNGSSS
    Length:350
    Mass (Da):38,382
    Last modified:May 1, 2000 - v1
    Checksum:i79BC9886F3126D5C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541G → R in AAM61178 (Ref. 5) Curated
    Sequence conflicti110 – 1101V → I in AAM61178 (Ref. 5) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL078468 Genomic DNA. Translation: CAB43892.1.
    AL161560 Genomic DNA. Translation: CAB81310.1.
    CP002687 Genomic DNA. Translation: AEE84827.1.
    AK118722 mRNA. Translation: BAC43316.1.
    BT008539 mRNA. Translation: AAP40366.1.
    AY084615 mRNA. Translation: AAM61178.1.
    PIRiT08911.
    RefSeqiNP_194123.1. NM_118524.2.
    UniGeneiAt.3390.

    Genome annotation databases

    EnsemblPlantsiAT4G23920.1; AT4G23920.1; AT4G23920.
    GeneIDi828492.
    GrameneiAT4G23920.1; AT4G23920.1; AT4G23920.
    KEGGiath:AT4G23920.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL078468 Genomic DNA. Translation: CAB43892.1.
    AL161560 Genomic DNA. Translation: CAB81310.1.
    CP002687 Genomic DNA. Translation: AEE84827.1.
    AK118722 mRNA. Translation: BAC43316.1.
    BT008539 mRNA. Translation: AAP40366.1.
    AY084615 mRNA. Translation: AAM61178.1.
    PIRiT08911.
    RefSeqiNP_194123.1. NM_118524.2.
    UniGeneiAt.3390.

    3D structure databases

    ProteinModelPortaliQ9T0A7.
    SMRiQ9T0A7. Positions 1-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi13781. 2 interactions.
    IntActiQ9T0A7. 2 interactions.
    STRINGi3702.AT4G23920.1.

    Proteomic databases

    PaxDbiQ9T0A7.
    PRIDEiQ9T0A7.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G23920.1; AT4G23920.1; AT4G23920.
    GeneIDi828492.
    GrameneiAT4G23920.1; AT4G23920.1; AT4G23920.
    KEGGiath:AT4G23920.

    Organism-specific databases

    TAIRiAT4G23920.

    Phylogenomic databases

    eggNOGiKOG1371. Eukaryota.
    COG1087. LUCA.
    HOGENOMiHOG000168001.
    InParanoidiQ9T0A7.
    KOiK01784.
    OMAiCGCKVYN.
    PhylomeDBiQ9T0A7.

    Enzyme and pathway databases

    UniPathwayiUPA00214.
    BRENDAi5.1.3.2. 399.
    5.1.3.5. 399.
    ReactomeiR-ATH-70370. Galactose catabolism.
    SABIO-RKQ9T0A7.

    Miscellaneous databases

    PROiQ9T0A7.

    Gene expression databases

    GenevisibleiQ9T0A7. AT.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR005886. GalE.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF16363. GDP_Man_Dehyd. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01179. galE. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      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. "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].
    6. "Genetic and biochemical characterization of UDP sugar 4-epimerases in Arabidopsis thaliana."
      Verma R., Burget E.G., Reiter W.-D.
      (In) Proceedings of the 12th international conference on Arabidopsis research, abstract#156, Madison (2001)
      Cited for: TISSUE SPECIFICITY, FUNCTION.
    7. "Molecular genetics of nucleotide sugar interconversion pathways in plants."
      Reiter W.-D., Vanzin G.F.
      Plant Mol. Biol. 47:95-113(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY.
    8. "Galactose biosynthesis in Arabidopsis: genetic evidence for substrate channeling from UDP-D-galactose into cell wall polymers."
      Seifert G.J., Barber C., Wells B., Dolan L., Roberts K.
      Curr. Biol. 12:1840-1845(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, TISSUE SPECIFICITY.
    9. "Distinct properties of the five UDP-D-glucose/UDP-D-galactose 4-epimerase isoforms of Arabidopsis thaliana."
      Barber C., Roesti J., Rawat A., Findlay K., Roberts K., Seifert G.J.
      J. Biol. Chem. 281:17276-17285(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
    10. "UDP-glucose 4-epimerase isoforms UGE2 and UGE4 cooperate in providing UDP-galactose for cell wall biosynthesis and growth of Arabidopsis thaliana."
      Roesti J., Barton C.J., Albrecht S., Dupree P., Pauly M., Findlay K., Roberts K., Seifert G.J.
      Plant Cell 19:1565-1579(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, FUNCTION.
    11. "Bifunctional cytosolic UDP-glucose 4-epimerases catalyse the interconversion between UDP-D-xylose and UDP-L-arabinose in plants."
      Kotake T., Takata R., Verma R., Takaba M., Yamaguchi D., Orita T., Kaneko S., Matsuoka K., Koyama T., Reiter W.D., Tsumuraya Y.
      Biochem. J. 424:169-177(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiUGE2_ARATH
    AccessioniPrimary (citable) accession number: Q9T0A7
    Secondary accession number(s): Q541V9, Q8LFW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: February 17, 2016
    This is version 129 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.