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O02373 (UGDH_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Alternative name(s):
Protein sugarless
Protein suppenkasper
Gene names
Name:sgl
Synonyms:kiwi, ska
ORF Names:CG10072
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate and heparan sulfate. Required for wingless signaling in different tissues. Ref.1 Ref.2 Ref.3

Catalytic activity

UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH. Ref.1

Pathway

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

Disruption phenotype

'Wingless-like' cuticular phenotype; reduced growth of imaginal disks and pattern defects. Ref.1 Ref.3

Sequence similarities

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

Ontologies

Keywords
   Biological processWnt signaling pathway
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processUDP-glucuronate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

Wnt signaling pathway

Traceable author statement PubMed 12417410. Source: FlyBase

cell surface receptor signaling pathway

Non-traceable author statement PubMed 12027431. Source: FlyBase

chondroitin sulfate biosynthetic process

Inferred from mutant phenotype PubMed 10806213. Source: UniProtKB

epithelial cell migration, open tracheal system

Inferred from mutant phenotype PubMed 10433902. Source: UniProtKB

fibroblast growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 10433902. Source: UniProtKB

glycosaminoglycan biosynthetic process

Inferred from mutant phenotype PubMed 10806213. Source: UniProtKB

heart development

Non-traceable author statement PubMed 12417410. Source: FlyBase

heparan sulfate proteoglycan biosynthetic process

Traceable author statement PubMed 10931855PubMed 14570584. Source: FlyBase

heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process

Inferred from mutant phenotype PubMed 10806213. Source: UniProtKB

imaginal disc-derived wing morphogenesis

Inferred from mutant phenotype PubMed 21635778. Source: FlyBase

inter-male aggressive behavior

Inferred from mutant phenotype PubMed 19519879. Source: FlyBase

mesoderm migration involved in gastrulation

Inferred from mutant phenotype PubMed 10433902. Source: UniProtKB

mushroom body development

Inferred from mutant phenotype PubMed 19519879. Source: FlyBase

olfactory behavior

Inferred from mutant phenotype PubMed 17028343. Source: FlyBase

primary branching, open tracheal system

Traceable author statement PubMed 14570584. Source: FlyBase

segment polarity determination

Inferred from mutant phenotype PubMed 16049108PubMed 8978055. Source: FlyBase

smoothened signaling pathway

Traceable author statement PubMed 12417410. Source: FlyBase

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

UDP-glucose 6-dehydrogenase activity

Inferred from mutant phenotype PubMed 10806213. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476UDP-glucose 6-dehydrogenase
PRO_0000074064

Regions

Nucleotide binding7 – 126NAD By similarity
Nucleotide binding85 – 895NAD By similarity
Nucleotide binding126 – 1272NAD By similarity
Nucleotide binding272 – 2754NAD By similarity
Region157 – 1615Substrate binding By similarity
Region216 – 2238Substrate binding By similarity
Region256 – 26914Substrate binding By similarity
Region334 – 3352Substrate binding By similarity

Sites

Active site2721Nucleophile By similarity
Binding site321NAD By similarity
Binding site371NAD By similarity
Binding site1611NAD By similarity
Binding site3421NAD By similarity
Binding site4391Substrate By similarity

Experimental info

Sequence conflict591K → R in AAC97125. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O02373 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 1450B9A0C802BBE7

FASTA47652,875
        10         20         30         40         50         60 
MKVCCIGAGY VGGPTCAVMA LKCPDIVITL VDKSSERIAQ WNSDKLPIYE PGLDEVVKKC 

        70         80         90        100        110        120 
RNVNLFFSTD IETAIKEADL IFISVNTPTK TCGNGKGRAA DLKYVESAAR MIAEIAQSNK 

       130        140        150        160        170        180 
IVVEKSTVPV RAAESIMHIL RANQKPGIHY DILSNPEFLA EGTAINDLLN ADRVLIGGEE 

       190        200        210        220        230        240 
TPEGHQAVEK LSWIYEHWIP KQNILTTNTW SSELSKLAAN AFLAQRISSI NSLSAVCEAT 

       250        260        270        280        290        300 
GADVSEVARA VGLDSRIGSK FLQASVGFGG SCFQKDILNL IYICENLNLP EVAAYWQQVI 

       310        320        330        340        350        360 
DMNEYQKRRF SQKIIESLFN TVSDKRIAIL GFAFKKNTGD TRETAAITVC QTLLEEGAAL 

       370        380        390        400        410        420 
DIYDPKVEPE QIIDDLTHPS VTESPEKVKK AVQIHSDPYS AVRATHALVI CTEWDEFVDL 

       430        440        450        460        470 
DFKRIYQSMM KPAYIFDGRK ILDHERLQQI GFHVQTIGKK YQRTGLLRSW GIVPQL 

« Hide

References

« Hide 'large scale' references
[1]"Genetic evidence that heparin-like glycosaminoglycans are involved in wingless signaling."
Binari R.C., Staveley B.E., Johnson W.A., Godavarti R., Sasisekharan R., Manoukian A.S.
Development 124:2623-2632(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE.
[2]"The Drosophila sugarless gene modulates Wingless signaling and encodes an enzyme involved in polysaccharide biosynthesis."
Haecker U., Lin X., Perrimon N.
Development 124:3565-3573(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[3]"Defects in glucuronate biosynthesis disrupt Wingless signaling in Drosophila."
Haerry T.E., Heslip T.R., Marsh J.L., O'Connor M.B.
Development 124:3055-3064(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE.
[4]"Mutation in the Drosophila gene encoding UDP-glucose dehydrogenase affects expression of unlinked genes."
Benevolenskaya E.V., Frolov M.V., Birchler J.A.
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76.
Strain: Canton-S.
[5]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[6]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[7]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF007870 mRNA. Translation: AAB63208.1.
AF000570 mRNA. Translation: AAB58714.1.
AF009013 mRNA. Translation: AAB63462.1.
AF001310 mRNA. Translation: AAC97125.1.
AH007072 Genomic DNA. Translation: AAC97126.1.
AE014296 Genomic DNA. Translation: AAF50631.1.
AY052137 mRNA. Translation: AAK93561.1.
RefSeqNP_476980.1. NM_057632.4.
UniGeneDm.4371.

3D structure databases

ProteinModelPortalO02373.
SMRO02373. Positions 2-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid64209. 9 interactions.

Proteomic databases

PaxDbO02373.
PRIDEO02373.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0076938; FBpp0076647; FBgn0261445.
GeneID38760.
KEGGdme:Dmel_CG10072.

Organism-specific databases

CTD24054.
FlyBaseFBgn0261445. sgl.

Phylogenomic databases

eggNOGCOG1004.
GeneTreeENSGT00390000015355.
InParanoidO02373.
KOK00012.
OMAVELNTWQ.
OrthoDBEOG7034GP.
PhylomeDBO02373.

Enzyme and pathway databases

UniPathwayUPA00038; UER00491.

Gene expression databases

BgeeO02373.

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

GenomeRNAi38760.
NextBio810251.
PROO02373.

Entry information

Entry nameUGDH_DROME
AccessionPrimary (citable) accession number: O02373
Secondary accession number(s): O02647, Q9VRZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase