Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9LIA8 (UGDH1_ARATH)

Last modified February 9, 2010. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable UDP-glucose 6-dehydrogenase 1
      Short name=UDP-Glc dehydrogenase 1
      Short name=UDP-GlcDH 1
      Short name=UDPGDH 1
    EC=1.1.1.22
Gene names
Name: UGD1
Ordered Locus Names: At3g29360
ORF Names: MUO10_6, MUO10.18
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Provides UDP-glucuronic acid for hemicellulose precursors By similarity.

Catalytic activity

UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH.

Pathway

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

Post-translational modification

Phosphorylation level varies significantly during early response to general elicitors.

Sequence similarities

Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.

Ontologies

Keywords
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from direct assay. Source: TAIR

nucleus

Inferred from direct assay. Source: TAIR

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

UDP-glucose 6-dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Probable UDP-glucose 6-dehydrogenase 1
PRO_0000312027

Regions

Nucleotide binding8 – 136NAD By similarity
Nucleotide binding86 – 905NAD By similarity
Nucleotide binding127 – 1282NAD By similarity
Nucleotide binding272 – 2754NAD By similarity
Region157 – 1615Substrate binding By similarity
Region216 – 2238Substrate binding By similarity
Region256 – 26914Substrate binding By similarity
Region334 – 3352Substrate binding By similarity

Sites

Active site2721Nucleophile By similarity
Binding site331NAD By similarity
Binding site381NAD By similarity
Binding site1611NAD By similarity
Binding site3421NAD By similarity
Binding site4471Substrate By similarity

Amino acid modifications

Modified residue3931Phosphoserine Ref.7

Experimental info

Sequence conflict121V → I in AAL11570. Ref.2
Sequence conflict1781G → R in AAL11570. Ref.2
Sequence conflict1931N → D in AAM67208. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9LIA8-1 [UniParc].

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

FASTA48053,173
        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

[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: 10907853] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"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].
[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. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., 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]"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: 17317660] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP001309 Genomic DNA. Translation: BAB02581.1.
AF424576 mRNA. Translation: AAL11570.1.
AY088902 mRNA. Translation: AAM67208.1.
BT021126 mRNA. Translation: AAX22261.1.
AK226539 mRNA. Translation: BAE98678.1.
BT029164 mRNA. Translation: ABJ17099.1.
IPIIPI00545262.
RefSeqNP_001030792.1.
NP_189582.1.
UniGeneAt.22975

3D structure databases

SMRQ9LIA8. Positions 3-467.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9LIA8.

Proteomic databases

PRIDEQ9LIA8.

Genome annotation databases

GeneID822594.
GenomeReviewsGene locus AT3G29360 in contig BA000014_GR.
KEGGath:AT3G29360.
NMPDRfig|3702.1.peg.15250.

Organism-specific databases

TAIRAt3g29360.

Phylogenomic databases

eggNOGKOG2666.
HOGENOMHBG400967.
InParanoidQ9LIA8.
OMAVELNTWQ.
PhylomeDBQ9LIA8.

Enzyme and pathway databases

BRENDA1.1.1.22. 302.

Gene expression databases

GenevestigatorQ9LIA8.

Family and domain databases

InterProIPR008927. 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.
IPR014028. UDP-Glc/GDP-Man_DH_dimer-bd.
IPR001732. UDP-Glc/GDP-Man_DH_N.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:3.40.50.1870. UDP-Glc/GDP-Man_DH_C. 1 hit.
PANTHERPTHR11374. UDPG_MGDP_DH_Creg. 1 hit.
PfamPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR03026. NDP-sugDHase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameUGDH1_ARATH
AccessionPrimary (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: February 9, 2010
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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 and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents