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O70199 (UGDH_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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

Names and origin

Protein namesRecommended name:
UDP-glucose 6-dehydrogenase

Short name=UDP-Glc dehydrogenase
Short name=UDP-GlcDH
Short name=UDPGDH
EC=1.1.1.22
Gene names
Name:Ugdh
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate.

Catalytic activity

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

Enzyme regulation

UDP-alpha-D-xylose (UDX) acts as a feedback inhibitor by activating an allosteric switch By similarity.

Pathway

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

Subunit structure

Homohexamer By similarity.

Sequence similarities

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493UDP-glucose 6-dehydrogenase
PRO_0000074062

Regions

Nucleotide binding11 – 166NAD By similarity
Nucleotide binding89 – 935NAD By similarity
Nucleotide binding130 – 1312NAD By similarity
Nucleotide binding276 – 2794NAD By similarity
Region161 – 1655Substrate binding By similarity
Region220 – 2278Substrate binding By similarity
Region260 – 27314Substrate binding By similarity
Region338 – 3392Substrate binding By similarity

Sites

Active site2761Nucleophile By similarity
Binding site361NAD By similarity
Binding site411NAD By similarity
Binding site1651NAD By similarity
Binding site3461NAD By similarity
Binding site4421Substrate By similarity

Amino acid modifications

Modified residue1071N6-acetyllysine By similarity
Modified residue4741Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
O70199 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: F435D1F9AC8307EF

FASTA49354,892
        10         20         30         40         50         60 
MVEIKKICCI GAGYVGGPTC SVIARMCPEI RVTVVDVNEA RINAWNSPTL PIYEPGLKEV 

        70         80         90        100        110        120 
VESCRGKNLF FSTNIDDAIR EADLVFISVN TPTKTYGMGK GRAADLKYIE ACARRIVQNS 

       130        140        150        160        170        180 
NGYKIVTEKS TVPVRAAESI RRIFDANTKP NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI 

       190        200        210        220        230        240 
GGDETPEGQR AVQALCAVYE HWVPKEKILT TNTWSSELSK LAANAFLAQR ISSINSISAL 

       250        260        270        280        290        300 
CESTGADVEE VATAIGMDQR IGNKFLKASV GFGGGCFQKD VLNLVYLCEA LNLPEVARYW 

       310        320        330        340        350        360 
QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS IYISKYLMDE 

       370        380        390        400        410        420 
GAHLHIYDPK VPREQIVVDL SHPGVSADDQ VSRLVTISKD PYEACDGAHA LVICTEWDMF 

       430        440        450        460        470        480 
KELDYERIHK RMLKPAFIFD GRRVLDGLHN ELQTIGFQIE TIGKKVSSKR IPYTPGEIPK 

       490 
FSLQDPPNKK PKV 

« Hide

References

[1]"cDNA cloning of rat UDP-glucose dehydrogenase."
Kobayashi T., Yokota H., Yuasa A.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB013732 mRNA. Translation: BAA28215.1.
RefSeqNP_112615.1. NM_031325.1.
UniGeneRn.3967.

3D structure databases

ProteinModelPortalO70199.
SMRO70199. Positions 1-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4567212.
STRING10116.ENSRNOP00000003691.

PTM databases

PhosphoSiteO70199.

Proteomic databases

PaxDbO70199.
PRIDEO70199.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83472.
KEGGrno:83472.
UCSCRGD:621879. rat.

Organism-specific databases

CTD7358.
RGD621879. Ugdh.

Phylogenomic databases

eggNOGCOG1004.
HOGENOMHOG000153773.
HOVERGENHBG003512.
InParanoidO70199.
KOK00012.
PhylomeDBO70199.

Enzyme and pathway databases

UniPathwayUPA00038; UER00491.

Gene expression databases

GenevestigatorO70199.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR016040. NAD(P)-bd_dom.
IPR017476. UDP-Glc/GDP-Man.
IPR014027. UDP-Glc/GDP-Man_DH_C.
IPR014026. UDP-Glc/GDP-Man_DH_dimer.
IPR001732. UDP-Glc/GDP-Man_DH_N.
IPR028356. UDPglc_DH_euk.
[Graphical view]
PANTHERPTHR11374. PTHR11374. 1 hit.
PTHR11374:SF3. PTHR11374:SF3. 1 hit.
PfamPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF500133. UDPglc_DH_euk. 1 hit.
PIRSF000124. UDPglc_GDPman_dh. 1 hit.
SMARTSM00984. UDPG_MGDP_dh_C. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 1 hit.
SSF52413. SSF52413. 1 hit.
TIGRFAMsTIGR03026. NDP-sugDHase. 1 hit.
ProtoNetSearch...

Other

NextBio615885.
PROO70199.

Entry information

Entry nameUGDH_RAT
AccessionPrimary (citable) accession number: O70199
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways