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Reviewed, UniProtKB/Swiss-Prot Q5R7B3 (UGDH_PONAB)

Last modified February 9, 2010. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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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
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

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

Subunit structure

Homohexamer By similarity.

Sequence similarities

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

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Ontologies

Keywords
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494UDP-glucose 6-dehydrogenase
PRO_0000317477

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 residue1731N6-acetyllysine By similarity
Modified residue4341N6-acetyllysine By similarity
Modified residue4731Phosphotyrosine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5R7B3-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 9584347DAD728943

FASTA49455,077
        10         20         30         40         50         60 
MFEIKKICCI GAGYVGGPTC SVIAHMRPEI RVTVVDVNES RINAWNSPTL PIYEPGLKEV 

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

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

       190        200        210        220        230        240 
GGDETPEGQR AVQALCAVYE HWVPREKILT 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 SHPGVSEDDQ VSRLVTISKD PYEACDGAHA VVICTEWDMF 

       430        440        450        460        470        480 
KELDYERIHK KMLKPAFIFD GRRVLDGLHN ELQTIGFQIE TIGKKVSSKR IPYAPSGEIP 

       490 
KFSLQDPPNK KPKV

« Hide

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR860205 mRNA. Translation: CAH92347.1.
RefSeqNP_001127543.1.
UniGenePab.18800

3D structure databases

SMRQ5R7B3. Positions 1-466.
ModBaseSearch...

Genome annotation databases

GeneID100174620.

Organism-specific databases

CTD100174620.

Phylogenomic databases

HOVERGENQ5R7B3.
InParanoidQ5R7B3.

Enzyme and pathway databases

BRENDA1.1.1.22. 269192.

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...

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Entry information

Entry nameUGDH_PONAB
AccessionPrimary (citable) accession number: Q5R7B3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 21, 2004
Last modified: February 9, 2010
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

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