UDP-glucose 6-dehydrogenase 2 - Arabidopsis thaliana (Mouse-ear cress)

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Q9LIA8 (UGDH2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
UDP-glucose 6-dehydrogenase 2
Short name=UDP-Glc dehydrogenase 2
Short name=UDP-GlcDH 2
Short name=UDPGDH 2
EC=1.1.1.22

Alternative name(s):
At-UGD2

Gene names

Name:	UGD2
Synonyms:	UGD
Ordered Locus Names:	At3g29360
ORF Names:	MUO10.18, MUO10_6

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. Required for the formation of cell wall ingrowths on the outer cell walls of nematode-induced syncytia. Ref.8 Ref.13 Ref.14
Catalytic activity	UDP-glucose + 2 NAD⁺ + H₂O = UDP-glucuronate + 2 NADH.
Enzyme regulation	Inhibited by UDP-xylose. Ref.11
Pathway	Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
Tissue specificity	Preferentially expressed in roots. Ref.8
Developmental stage	Restricted expression to the primary root in young seedlings. Later detected in hypocotyl, leaves but with the strongest expression in the root system. Ref.8 Ref.11
Post-translational modification	Phosphorylation level varies significantly during early response to general elicitors.
Disruption phenotype	No visible phenotype. Displays smaller nematode-induced syncytia. The UGD2 UGD3 double mutant displays a strong dwarf phenotype and often develops seedlings with severe root defects; cell walls have an altered sugar composition (Ref.13). The UGD2 UGD3 double mutant displays abnormal nematode-induced syncytia (Ref.14). Ref.13 Ref.14
Sequence similarities	Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: K_M=43 µM for NAD⁺ Ref.11 K_M=123 µM for UDP-glucose

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-glucuronate biosynthetic process Inferred from direct assay Ref.11. Source: UniProtKB cell wall pectin metabolic process Inferred from genetic interaction Ref.13. Source: TAIR
Cellular_component	cytosol Inferred from direct assay PubMed 18433157 PubMed 21166475. Source: TAIR nucleus Inferred from direct assay PubMed 18433157. Source: TAIR
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro UDP-glucose 6-dehydrogenase activity Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 480

480

UDP-glucose 6-dehydrogenase 2

PRO_0000312027

Regions

Nucleotide binding

8 – 13

NAD By similarity

Nucleotide binding

86 – 90

NAD By similarity

Nucleotide binding

127 – 128

NAD By similarity

Nucleotide binding

272 – 275

NAD By similarity

Region

157 – 161

Substrate binding By similarity

Region

216 – 223

Substrate binding By similarity

Region

256 – 269

Substrate binding By similarity

Region

334 – 335

Substrate binding By similarity

Sites

Active site

272

Nucleophile By similarity

Binding site

NAD By similarity

Binding site

NAD By similarity

Binding site

161

NAD By similarity

Binding site

342

NAD By similarity

Binding site

447

Substrate By similarity

Amino acid modifications

Modified residue

393

Phosphoserine Ref.12

Experimental info

Sequence conflict

V → I in AAL11570. Ref.3

Sequence conflict

178

G → R in AAL11570. Ref.3

Sequence conflict

193

N → D in AAM67208. Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

Q9LIA8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D6281D20442CBADF
Show »

FASTA

480

53,173

        10         20         30         40         50         60 
MVKICCIGAG YVGGPTMAVI ALKCPDVEVA VVDISVPRIN AWNSDTLPIY EPGLDDVVKQ 

        70         80         90        100        110        120 
CRGKNLFFST DVEKHVREAD IVFVSVNTPT KTRGLGAGKA ADLTYWESAA RMIADVSVSD 

       130        140        150        160        170        180 
KIVVEKSTVP VKTAEAIEKI LTHNSKGIKF QILSNPEFLA EGTAIKDLFN PDRVLIGGRE 

       190        200        210        220        230        240 
TPEGFKAVQT LKNVYAHWVP EGQIITTNLW SAELSKLAAN AFLAQRISSV NAMSALCEAT 

       250        260        270        280        290        300 
GADVTQVSYA VGTDSRIGPK FLNSSVGFGG SCFQKDILNL VYICECNGLP EVAEYWKQVI 

       310        320        330        340        350        360 
KINDYQKSRF VNRVVSSMFN SVSNKKIAVL GFAFKKDTGD TRETPAIDVC KGLLEDKARL 

       370        380        390        400        410        420 
SIYDPQVTED QIQRDLSMNK FDWDHPLHLQ PMSPTTVKQV TVTWDAYEAT KDAHGICIMT 

       430        440        450        460        470        480 
EWDEFKNLDF QKIFDNMQKP AFVFDGRNIM NLQKLREIGF IVYSIGKPLD DWLKDMPAVA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones." Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S. DNA Res. 7:217-221(2000) [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. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Arabidopsis ORF clones." Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Arabidopsis ORF Clone." Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[7]	"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].
[8]	"Matrix polysaccharide precursors in Arabidopsis cell walls are synthesized by alternate pathways with organ-specific expression patterns." Seitz B., Klos C., Wurm M., Tenhaken R. Plant J. 21:537-546(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[9]	"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.
[10]	"Nucleotide sugar interconversions and cell wall biosynthesis: how to bring the inside to the outside." Seifert G.J. Curr. Opin. Plant Biol. 7:277-284(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[11]	"Genome-wide analysis of the UDP-glucose dehydrogenase gene family in Arabidopsis, a key enzyme for matrix polysaccharides in cell walls." Klinghammer M., Tenhaken R. J. Exp. Bot. 58:3609-3621(2007) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE, DEVELOPMENTAL STAGE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[12]	"Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis." Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H. Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, MASS SPECTROMETRY. Strain: cv. Columbia.
[13]	"Down-regulation of UDP-glucuronic acid biosynthesis leads to swollen plant cell walls and severe developmental defects associated with changes in pectic polysaccharides." Reboul R., Geserick C., Pabst M., Frey B., Wittmann D., Luetz-Meindl U., Leonard R., Tenhaken R. J. Biol. Chem. 286:39982-39992(2011) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[14]	"Cell wall ingrowths in nematode induced syncytia require UGD2 and UGD3." Siddique S., Sobczak M., Tenhaken R., Grundler F.M., Bohlmann H. PLoS ONE 7:E41515-E41515(2012) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP001309 Genomic DNA. Translation: BAB02581.1. CP002686 Genomic DNA. Translation: AEE77573.1. CP002686 Genomic DNA. Translation: AEE77574.1. AF424576 mRNA. Translation: AAL11570.1. BT021126 mRNA. Translation: AAX22261.1. AK226539 mRNA. Translation: BAE98678.1. BT029164 mRNA. Translation: ABJ17099.1. AY088902 mRNA. Translation: AAM67208.1.
IPI	IPI00545262.
RefSeq	NP_001030792.1. NM_001035715.1. NP_189582.1. NM_113861.3.
UniGene	At.22975.
3D structure databases
ProteinModelPortal	Q9LIA8.
SMR	Q9LIA8. Positions 3-467.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9LIA8. 1 interaction.
Proteomic databases
PaxDb	Q9LIA8.
PRIDE	Q9LIA8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G29360.1; AT3G29360.1; AT3G29360. AT3G29360.2; AT3G29360.2; AT3G29360.
GeneID	822594.
KEGG	ath:AT3G29360.
Organism-specific databases
TAIR	At3g29360.
Phylogenomic databases
eggNOG	COG1004.
HOGENOM	HOG000153773.
InParanoid	Q9LIA8.
KO	K00012.
OMA	FAESGND.
PhylomeDB	Q9LIA8.
ProtClustDB	PLN02353.
Enzyme and pathway databases
UniPathway	UPA00038; UER00491.
Gene expression databases
Genevestigator	Q9LIA8.
Family and domain databases
Gene3D	3.40.50.720. 2 hits.
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR016040. NAD(P)-bd_dom. IPR017476. Nucleotide_sugar_DH. IPR014027. UDP-Glc/GDP-Man_DH_C. IPR014026. UDP-Glc/GDP-Man_DH_dimer. IPR001732. UDP-Glc/GDP-Man_DH_N. [Graphical view]
Pfam	PF00984. UDPG_MGDP_dh. 1 hit. PF03720. UDPG_MGDP_dh_C. 1 hit. PF03721. UDPG_MGDP_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMART	SM00984. UDPG_MGDP_dh_C. 1 hit. [Graphical view]
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit. SSF52413. UDP-Glc/GDP-Man_DH_C. 1 hit.
TIGRFAMs	TIGR03026. NDP-sugDHase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

UGDH2_ARATH

Accession

Primary (citable) accession number: Q9LIA8
Secondary accession number(s): Q8L8N1, Q944R8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	October 1, 2000
Last modified:	May 29, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents