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Q9FIE8 (UXS3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-glucuronic acid decarboxylase 3

EC=4.1.1.35
Alternative name(s):
UDP-XYL synthase 3
UDP-glucuronate decarboxylase 3
Short name=UGD
Short name=UXS-3
Gene names
Name:UXS3
Ordered Locus Names:At5g59290
ORF Names:MNC17.20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis. Ref.1 Ref.7

Catalytic activity

UDP-D-glucuronate = UDP-D-xylose + CO2.

Cofactor

NAD. Ref.1

Pathway

Nucleotide-sugar biosynthesis; UDP-alpha-D-xylose biosynthesis; UDP-alpha-D-xylose from UDP-alpha-D-glucuronate: step 1/1.

Subcellular location

Cytoplasm Ref.6.

Tissue specificity

Ubiquitous. Ref.1

Sequence similarities

Belongs to the sugar epimerase family. UDP-glucuronic acid decarboxylase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.51 mM for UDP-D-glucuronate at 30 degrees Celsius Ref.1

pH dependence:

Optimum pH is 5.5 at 30 degrees Celsius.

Temperature dependence:

Optimum temperature is 30 degrees Celsius.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandNAD
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processUDP-D-xylose biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionUDP-glucuronate decarboxylase activity

Inferred from electronic annotation. Source: EC

coenzyme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9FIE8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342UDP-glucuronic acid decarboxylase 3
PRO_0000421984

Regions

Nucleotide binding61 – 8626NAD By similarity
Nucleotide binding173 – 1775NAD By similarity
Nucleotide binding215 – 2195Substrate By similarity
Nucleotide binding232 – 2398Substrate By similarity
Nucleotide binding299 – 3035Substrate By similarity

Sites

Active site1731Proton acceptor By similarity
Binding site1701Substrate By similarity
Binding site2021Substrate By similarity
Binding site2141NAD By similarity

Experimental info

Sequence conflict461V → D in AAK53026. Ref.4
Sequence conflict461V → D in AAM16219. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 5E2AA6C9A13CEBD8

FASTA34238,569
        10         20         30         40         50         60 
MAATSEKQNT TKPPPSPSPL RNSKFCQPNM RILISGGAGF IGSHLVDKLM ENEKNEVVVA 

        70         80         90        100        110        120 
DNYFTGSKEN LKKWIGHPRF ELIRHDVTEP LLIEVDRIYH LACPASPIFY KYNPVKTIKT 

       130        140        150        160        170        180 
NVIGTLNMLG LAKRVGARIL LTSTSEVYGD PLIHPQPESY WGNVNPIGVR SCYDEGKRVA 

       190        200        210        220        230        240 
ETLMFDYHRQ HGIEIRIARI FNTYGPRMNI DDGRVVSNFI AQALRGEALT VQKPGTQTRS 

       250        260        270        280        290        300 
FCYVSDMVDG LIRLMEGNDT GPINIGNPGE FTMVELAETV KELINPSIEI KMVENTPDDP 

       310        320        330        340 
RQRKPDISKA KEVLGWEPKV KLREGLPLME EDFRLRLNVP RN 

« Hide

References

« Hide 'large scale' references
[1]"Biosynthesis of UDP-xylose. Cloning and characterization of a novel Arabidopsis gene family, UXS, encoding soluble and putative membrane-bound UDP-glucuronic acid decarboxylase isoforms."
Harper A.D., Bar-Peled M.
Plant Physiol. 130:2188-2198(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones."
Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., Tabata S.
DNA Res. 5:379-391(1998) [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. expand/collapse author list , 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]"Biosynthesis of UDP-xylose: characterization of membrane-bound AtUxs2."
Pattathil S., Harper A.D., Bar-Peled M.
Planta 221:538-548(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Reconstruction of de novo pathway for synthesis of UDP-glucuronic acid and UDP-xylose from intrinsic UDP-glucose in Saccharomyces cerevisiae."
Oka T., Jigami Y.
FEBS J. 273:2645-2657(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF387789 mRNA. Translation: AAK70882.1.
AB016890 Genomic DNA. Translation: BAB09774.1.
CP002688 Genomic DNA. Translation: AED97166.1.
AF375442 mRNA. Translation: AAK53026.1.
AY093958 mRNA. Translation: AAM16219.1.
AY088443 mRNA. Translation: AAM65979.1.
IPIIPI00542582.
IPI00846930.
RefSeqNP_200737.1. NM_125319.2.
UniGeneAt.24136.

3D structure databases

ProteinModelPortalQ9FIE8.
SMRQ9FIE8. Positions 31-326.
ModBaseSearch...

Proteomic databases

PaxDbQ9FIE8.
PRIDEQ9FIE8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G59290.1; AT5G59290.1; AT5G59290.
GeneID836047.
KEGGath:AT5G59290.

Organism-specific databases

TAIRAt5g59290.

Phylogenomic databases

eggNOGCOG0451.
HOGENOMHOG000168004.
InParanoidQ9FIE8.
PhylomeDBQ9FIE8.
ProtClustDBCLSN2683686.

Enzyme and pathway databases

BioCycARA:AT5G59290-MONOMER.
MetaCyc:AT5G59290-MONOMER.
UniPathwayUPA00796; UER00771.

Gene expression databases

ArrayExpressQ9FIE8.
GenevestigatorQ9FIE8.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR001509. Epimerase_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01370. Epimerase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUXS3_ARATH
AccessionPrimary (citable) accession number: Q9FIE8
Secondary accession number(s): Q94JQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: March 1, 2001
Last modified: May 29, 2013
This is version 78 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families