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O81312 (GAE3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-glucuronate 4-epimerase 3
EC=5.1.3.6
Alternative name(s):
UDP-glucuronic acid epimerase 3
Gene names
Name:GAE3
Ordered Locus Names:At4g00110
ORF Names:F6N15.16
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the synthesis of the negatively charged monosaccharide that forms the backbone of pectic cell wall components.

Catalytic activity

UDP-glucuronate = UDP-D-galacturonate.

Subunit structure

Homodimer By similarity.

Subcellular location

Golgi apparatus › Golgi stack membrane; Multi-pass membrane protein Potential.

Tissue specificity

In roots, leaves, siliques, flowers, pollen and stems. Ref.5 Ref.6

Sequence similarities

Belongs to the sugar epimerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430UDP-glucuronate 4-epimerase 3
PRO_0000292598

Regions

Transmembrane29 – 4921Helical; Potential
Transmembrane90 – 11021Helical; Potential
Nucleotide binding92 – 12332NAD By similarity
Compositional bias216 – 2194Poly-Ser

Sites

Active site2421Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
O81312 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 0A57C1CB45BBAC02

FASTA43047,690
        10         20         30         40         50         60 
MKQMSHLDDI PSTPGKFKPY FHRTRWQSSV AKLAFWSLVF VGLIFIFFYR SPVSSNPADP 

        70         80         90        100        110        120 
SRRSLRTYSW GGPAWEKRVR SSARLRTRRG FSVLVTGAAG FVGTHVSAAL KRRGDGVLGL 

       130        140        150        160        170        180 
DNFNDYYDPS LKRARQALLE RSGVFVVEGD INDAALLKKL FEVVPFTHVM HLAAQAGVRY 

       190        200        210        220        230        240 
AMENPSSYVH SNIAGFVNLL EVCKSANPQP AIVWASSSSV YGLNTKVPFS EKDRTDQPAS 

       250        260        270        280        290        300 
LYAATKKAGE EIAHTYNHIY GLSLTGLRFF TVYGPWGRPD MAYFFFTRDI LKGKAISIFE 

       310        320        330        340        350        360 
GVNHGTVARD FTYIDDIVKG CLGALDTAEK STGSGGKKRG AAQLRVFNLG NTSPVPVTDL 

       370        380        390        400        410        420 
VTILERLLKV KAKRNIMKLP RNGDVQFTHA NISSAQRELG YKPTTDLQTG LKKFARWYLG 

       430 
YYNGGKKAAS

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 10617198] [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]"Arabidopsis ORF clones."
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Molecular genetics of nucleotide sugar interconversion pathways in plants."
Reiter W.-D., Vanzin G.F.
Plant Mol. Biol. 47:95-113(2001) [PubMed: 11554483] [Abstract]
Cited for: IDENTIFICATION, NOMENCLATURE.
[5]"The biosynthesis of D-galacturonate in plants. Functional cloning and characterization of a membrane-anchored UDP-D-glucuronate 4-epimerase from Arabidopsis."
Moelhoej M., Verma R., Reiter W.-D.
Plant Physiol. 135:1221-1230(2004) [PubMed: 15247385] [Abstract]
Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
[6]"Identification and characterization of a UDP-D-glucuronate 4-epimerase in Arabidopsis."
Usadel B., Schlueter U., Moelhoej M., Gipmans M., Verma R., Kossmann J., Reiter W.-D., Pauly M.
FEBS Lett. 569:327-331(2004) [PubMed: 15225656] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF069299 Genomic DNA. Translation: AAC19298.1.
AL161471 Genomic DNA. Translation: CAB80769.1.
CP002687 Genomic DNA. Translation: AEE81824.1.
BT026487 mRNA. Translation: ABH04594.1.
IPIIPI00527699.
PIRT01339.
RefSeqNP_191922.1. NM_116228.2.
UniGeneAt.27610.

3D structure databases

HSSPHSSP built from PDB template 1EK6 based on UniProtKB Q14376.
ProteinModelPortalO81312.
SMRO81312. Positions 89-423.
ModBaseSearch...

Protein-protein interaction databases

STRINGO81312.

Proteomic databases

PRIDEO81312.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G00110.1; AT4G00110.1; AT4G00110.
GeneID828145.
GenomeReviewsGene locus AT4G00110 in contig CT486007_GR.
KEGGath:AT4G00110.
NMPDRfig|3702.1.peg.17763.

Organism-specific databases

TAIRAt4g00110.

Phylogenomic databases

eggNOGKOG1371.
HOGENOMHBG755066.
InParanoidO81312.
OMASFANNIM.
PhylomeDBO81312.
ProtClustDBCLSN2679288.

Gene expression databases

ArrayExpressO81312.
GenevestigatorO81312.

Family and domain databases

InterProIPR001509. Epimerase_deHydtase.
IPR016040. NAD(P)-bd_dom.
IPR008089. Nuc_sugar_epim.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK08679.
PfamPF01370. Epimerase. 1 hit.
[Graphical view]
PRINTSPR01713. NUCEPIMERASE.
ProtoNetSearch...

Entry information

Entry nameGAE3_ARATH
AccessionPrimary (citable) accession number: O81312
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: November 1, 1998
Last modified: December 14, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents