UDP-glucose 6-dehydrogenase - Mus musculus (Mouse)

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O70475 (UGDH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. 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
Short name=UDP-Glc dehydrogenase
Short name=UDP-GlcDH
Short name=UDPGDH
EC=1.1.1.22

Gene names

Name:

Ugdh

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate. Ref.1
Catalytic activity	UDP-glucose + 2 NAD⁺ + H₂O = UDP-glucuronate + 2 NADH. Ref.1
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

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-glucuronate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway gastrulation with mouth forming second Inferred from mutant phenotype PubMed 15755804. Source: MGI
Molecular_function	NAD 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 493

493

UDP-glucose 6-dehydrogenase

PRO_0000074061

Regions

Nucleotide binding

11 – 16

NAD By similarity

Nucleotide binding

89 – 93

NAD By similarity

Nucleotide binding

130 – 131

NAD By similarity

Nucleotide binding

276 – 279

NAD By similarity

Region

161 – 165

Substrate binding By similarity

Region

220 – 227

Substrate binding By similarity

Region

260 – 273

Substrate binding By similarity

Region

338 – 339

Substrate binding By similarity

Sites

Active site

276

Nucleophile By similarity

Binding site

NAD By similarity

Binding site

NAD By similarity

Binding site

165

NAD By similarity

Binding site

346

NAD By similarity

Binding site

442

Substrate By similarity

Amino acid modifications

Modified residue

107

N6-acetyllysine By similarity

Modified residue

473

Phosphotyrosine Ref.3

Modified residue

474

Phosphothreonine Ref.3 Ref.4 Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

O70475 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: C6234F3C1D7480C7
Show »

FASTA

493

54,832

        10         20         30         40         50         60 
MVEIKKICCI GAGYVGGPTC SVIAHMCPEI 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 
GGDETPEGQK AVRALCAVYE HWVPKEKILT TNTWSSELSK LAANAFLAQR ISSINSISAL 

       250        260        270        280        290        300 
CEATGADVEE VATAIGMDQR IGNKFLKASV GFGGSCFQKD 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 KMLKPAFIFD GRRVLDGLHS ELQTIGFQIE TIGKKVSSKR IPYTPGEIPK 

       490 
FSLQDPPNKK PKV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of the human and mouse UDP-glucose dehydrogenase genes." Spicer A.P., Kaback L.A., Smith T.J., Seldin M.F. J. Biol. Chem. 273:25117-25124(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
[3]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-473 AND THR-474, MASS SPECTROMETRY. Tissue: Liver.
[4]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-474, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-474, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF061017 mRNA. Translation: AAC36096.1. BC006749 mRNA. Translation: AAH06749.1.
IPI	IPI00118344.
RefSeq	NP_033492.1. NM_009466.2.
UniGene	Mm.344831.
3D structure databases
ProteinModelPortal	O70475.
SMR	O70475. Positions 1-466.
ModBase	Search...
PTM databases
PhosphoSite	O70475.
Proteomic databases
PaxDb	O70475.
PRIDE	O70475.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031103; ENSMUSP00000031103; ENSMUSG00000029201.
GeneID	22235.
KEGG	mmu:22235.
Organism-specific databases
CTD	7358.
MGI	MGI:1306785. Ugdh.
Phylogenomic databases
eggNOG	COG1004.
HOGENOM	HOG000153773.
HOVERGEN	HBG003512.
InParanoid	O70475.
KO	K00012.
OMA	QMCPEIR.
OrthoDB	EOG4N30NS.
Enzyme and pathway databases
UniPathway	UPA00038; UER00491.
Gene expression databases
ArrayExpress	O70475.
Bgee	O70475.
CleanEx	MM_UGDH.
Genevestigator	O70475.
GermOnline	ENSMUSG00000029201. Mus musculus.
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...
Other
NextBio	302285.
SOURCE	Search...

Entry information

Entry name

UGDH_MOUSE

Accession

Primary (citable) accession number: O70475

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 1, 1998
Last modified:	April 3, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM 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

Other

Entry information

Relevant documents