UDP-glucose 6-dehydrogenase - Homo sapiens (Human)

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

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate.
Catalytic activity	UDP-glucose + 2 NAD(+) + H(2)O = UDP-glucuronate + 2 NADH.
Pathway	Nucleotide-sugar biosynthesis; UDP-glucuronate biosynthesis; UDP-glucuronate from UDP-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
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	UDP-glucose metabolic process Ref.1 Traceable author statement. Source: ProtInc UDP-glucuronate biosynthetic process Ref.1 Traceable author statement. Source: ProtInc glycosaminoglycan biosynthetic process Ref.1 Traceable author statement. Source: ProtInc oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro UDP-glucose 6-dehydrogenase activity Ref.1 Traceable author statement. Source: ProtInc electron carrier activity Ref.1 Traceable author statement. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 494

494

UDP-glucose 6-dehydrogenase

PRO_0000074060

Regions

Nucleotide binding

6 – 23

18

NAD By similarity

Region

162 – 165

4

Substrate binding By similarity

Sites

Active site

276

1

Nucleophile By similarity

Binding site

36

1

NAD By similarity

Binding site

41

1

NAD By similarity

Binding site

93

1

NAD By similarity

Binding site

131

1

NAD; via amide nitrogen By similarity

Binding site

165

1

NAD By similarity

Binding site

220

1

Substrate By similarity

Binding site

273

1

Substrate; via amide nitrogen By similarity

Binding site

279

1

NAD By similarity

Binding site

339

1

Substrate By similarity

Binding site

346

1

NAD By similarity

Amino acid modifications

Modified residue

473

1

Phosphotyrosine By similarity

Experimental info

Sequence conflict

338

1

F → V in AAC05135. Ref.5

Sequence conflict

377

1

V → A in AAC05135. Ref.5

Secondary structure

1

.

494

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

O60701-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 9C9DA5E1227D65CC
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FASTA

494

55,024

        10         20         30         40         50         60 
MFEIKKICCI GAGYVGGPTC SVIAHMCPEI 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

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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: 9737970] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"cDNA cloning and expression analysis of the human UDPglucose dehydrogenase." Peng H.L., Lou M.D., Chang M.L., Chang H.Y. Proc. Natl. Sci. Counc. Repub. China, B, Life Sci. 22:166-172(1998) [PubMed: 9850599] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Tissue: Liver.
[3]	"Characterization of human gene encoding UDP-glucose dehydrogenase." Chang M.L., Chang H.Y., Peng H.L. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[5]	Raghuram V., Foskett J.K. Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 214-388.
+	Additional computationally mapped references.