O02373 (UGDH_DROME) Reviewed, UniProtKB/Swiss-Prot

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

Alternative name(s):
Protein sugarless
Protein suppenkasper

Gene names

Name:	sgl
Synonyms:	kiwi, ska
ORF Names:	CG10072

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	476 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. 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 process	Wnt signaling pathway
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Traceable author statement. Source: FlyBase chondroitin sulfate biosynthetic process Inferred from mutant phenotype. Source: UniProtKB epithelial cell migration, open tracheal system Inferred from mutant phenotype. Source: UniProtKB fibroblast growth factor receptor signaling pathway Inferred from mutant phenotype. Source: UniProtKB heart development Non-traceable author statement. Source: FlyBase heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process Inferred from mutant phenotype. Source: UniProtKB inter-male aggressive behavior Inferred from mutant phenotype. Source: FlyBase mesoderm migration involved in gastrulation Inferred from mutant phenotype. Source: UniProtKB mushroom body development Inferred from mutant phenotype. Source: FlyBase olfactory behavior Inferred from mutant phenotype. Source: FlyBase primary branching, open tracheal system Traceable author statement. Source: FlyBase segment polarity determination Inferred from mutant phenotype. Source: FlyBase smoothened signaling pathway Traceable author statement. Source: FlyBase
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro UDP-glucose 6-dehydrogenase activity Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 476	476	UDP-glucose 6-dehydrogenase		PRO_0000074064
Regions
	Nucleotide binding	7 – 12	6	NAD By similarity
	Nucleotide binding	85 – 89	5	NAD By similarity
	Nucleotide binding	126 – 127	2	NAD By similarity
	Nucleotide binding	272 – 275	4	NAD By similarity
	Region	157 – 161	5	Substrate binding By similarity
	Region	216 – 223	8	Substrate binding By similarity
	Region	256 – 269	14	Substrate binding By similarity
	Region	334 – 335	2	Substrate binding By similarity
Sites
	Active site	272	1	Nucleophile By similarity
	Binding site	32	1	NAD By similarity
	Binding site	37	1	NAD By similarity
	Binding site	161	1	NAD By similarity
	Binding site	342	1	NAD By similarity
	Binding site	439	1	Substrate By similarity
Experimental info
	Sequence conflict	59	1	K → R in AAC97125. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O02373 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 1450B9A0C802BBE7	FASTA	476	52,875
	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

References

	« Hide 'large scale' referencesShow '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: 9217004] [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: 9342049] [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: 9272947] [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. , 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: 10731132] [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. , 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: 12537572] [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: 12537569] [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. AF001312, AF001311 Genomic DNA. Translation: AAC97126.1. AE014296 Genomic DNA. Translation: AAF50631.1. AY052137 mRNA. Translation: AAK93561.1.
RefSeq	NP_476980.1. NM_057632.3.
UniGene	Dm.4371.
3D structure databases
ProteinModelPortal	O02373.
SMR	O02373. Positions 2-460.
ModBase	Search...
Protein-protein interaction databases
STRING	O02373.
Proteomic databases
PRIDE	O02373.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0076938; FBpp0076647; FBgn0261445.
GeneID	38760.
KEGG	dme:Dmel_CG10072.
NMPDR	fig|7227.3.peg.8592.
Organism-specific databases
CTD	24054.
FlyBase	FBgn0261445. sgl.
Phylogenomic databases
eggNOG	inNOG04120.
InParanoid	O02373.
OMA	QMCPEIR.
OrthoDB	EOG4STQKV.
PhylomeDB	O02373.
Gene expression databases
ArrayExpress	O02373.
Bgee	O02373.
GermOnline	CG10072. Drosophila melanogaster.
Family and domain databases
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR021157. Cyt_c1_TM_anchor_C. 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]
Gene3D	G3DSA:1.20.5.100. Cyt_c1_TM_anchor_C. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
KO	K00012.
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	810251.

Entry information

Entry name

UGDH_DROME

Accession

Primary (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:	January 25, 2012
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project