Reviewed, UniProtKB/Swiss-Prot O60701 (UGDH_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

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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.
Pathway	Nucleotide-sugar biosynthesis; UDP-glucuronic acid biosynthesis; UDP-glucuronic acid from UDP-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	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 or NADH 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...

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

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494

Helix Strand Turn

Details...

Beta strand

6 – 10

5

Helix

16 – 26

11

Beta strand

30 – 35

6

Helix

39 – 45

7

Beta strand

47 – 49

3

Helix

57 – 64

8

Turn

66 – 68

3

Beta strand

69 – 73

5

Helix

75 – 81

7

Beta strand

83 – 87

5

Turn

98 – 102

5

Helix

107 – 118

12

Beta strand

122 – 128

7

Helix

136 – 146

11

Beta strand

153 – 158

6

Helix

168 – 173

6

Beta strand

178 – 181

4

Helix

186 – 199

14

Turn

200 – 202

3

Helix

205 – 207

3

Beta strand

208 – 211

4

Helix

213 – 244

32

Helix

248 – 256

9

Turn

259 – 261

3

Beta strand

263 – 265

3

Beta strand

274 – 276

3

Helix

277 – 290

14

Helix

294 – 321

28

Turn

322 – 324

3

Beta strand

330 – 334

5

Beta strand

337 – 339

3

Helix

349 – 359

11

Beta strand

363 – 367

5

Beta strand

369 – 371

3

Helix

373 – 380

8

Helix

390 – 394

5

Beta strand

395 – 397

3

Helix

401 – 405

5

Beta strand

409 – 413

5

Helix

418 – 422

5

Helix

425 – 431

7

Beta strand

437 – 442

6

Turn

444 – 447

4

Helix

449 – 455

7

Beta strand

458 – 461

4

Sequences

	Sequence		Length	Mass (Da)
	O60701-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 9C9DA5E1227D65CC	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

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 [MRNA]. 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 [GENOMIC DNA].
[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.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF061016 mRNA. Translation: AAC36095.1.
AJ007702 mRNA. Translation: CAA07609.1.
AJ272274 , AJ272275, AJ272276, AJ272277, AJ272278, AJ272279, AJ272280, AJ272281 Genomic DNA. Translation: CAB75891.1.
BC022781 mRNA. Translation: AAH22781.1.
AF049126 mRNA. Translation: AAC05135.1.

IPI

IPI00031420.

PIR

JE0353.

RefSeq

NP_003350.1.

UniGene

Hs.572518

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Q3E	X-ray	2.00	A/B/C/D/E/F/G/H/I/J/K/L	1-466	[»]
2QG4	X-ray	2.10	A/B/C/D/E/F/G/H	1-466	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O60701. 2 interactions.

PTM databases

PhosphoSite

O60701.

2-D gel databases

REPRODUCTION-2DPAGE

O60701.

Proteomic databases

PeptideAtlas

O60701.

PRIDE

O60701.

Genome annotation databases

Ensembl

ENSG00000109814. Homo sapiens. [Contig view]

GeneID

7358.

KEGG

hsa:7358.

NMPDR

fig|9606.3.peg.24043.

Organism-specific databases

GeneCards

GC04M039176.

H-InvDB

HIX0004163.

HGNC

HGNC:12525. UGDH.

MIM

603370. gene.

PharmGKB

PA37170.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O60701.

HOVERGEN

O60701.

OMA

O60701. QMCPEIR.

Enzyme and pathway databases

BRENDA

1.1.1.22. 247.

Reactome

REACT_13433. Biological oxidations.

Gene expression databases

ArrayExpress

O60701.

Bgee

O60701.

CleanEx

HS_UGDH.

GermOnline

ENSG00000109814. Homo sapiens.

Family and domain databases

InterPro

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]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:3.40.50.1870. UDP-Glc/GDP-Man_DH_C. 1 hit.

PANTHER

PTHR11374. UDPG_MGDP_DH_Creg. 1 hit.

Pfam

PF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03026. NDP-sugDHase. 1 hit.

ProtoNet

Search...

Other Resources

DrugBank

DB00157. NADH.

NextBio

28812.

SOURCE

Search...

Entry information

Entry name

UGDH_HUMAN

Accession

Primary (citable) accession number: O60701
Secondary accession number(s): O60589

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 1, 1998
Last modified:	June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)