UGDH_DROME
ID UGDH_DROME Reviewed; 476 AA.
AC O02373; O02647; Q9VRZ9;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=UDP-glucose 6-dehydrogenase;
DE Short=UDP-Glc dehydrogenase;
DE Short=UDP-GlcDH;
DE Short=UDPGDH;
DE EC=1.1.1.22;
DE AltName: Full=Protein sugarless;
DE AltName: Full=Protein suppenkasper;
GN Name=sgl; Synonyms=kiwi, ska; ORFNames=CG10072;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=9217004; DOI=10.1242/dev.124.13.2623;
RA Binari R.C., Staveley B.E., Johnson W.A., Godavarti R., Sasisekharan R.,
RA Manoukian A.S.;
RT "Genetic evidence that heparin-like glycosaminoglycans are involved in
RT wingless signaling.";
RL Development 124:2623-2632(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9342049; DOI=10.1242/dev.124.18.3565;
RA Haecker U., Lin X., Perrimon N.;
RT "The Drosophila sugarless gene modulates Wingless signaling and encodes an
RT enzyme involved in polysaccharide biosynthesis.";
RL Development 124:3565-3573(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9272947; DOI=10.1242/dev.124.16.3055;
RA Haerry T.E., Heslip T.R., Marsh J.L., O'Connor M.B.;
RT "Defects in glucuronate biosynthesis disrupt Wingless signaling in
RT Drosophila.";
RL Development 124:3055-3064(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76.
RC STRAIN=Canton-S;
RA Benevolenskaya E.V., Frolov M.V., Birchler J.A.;
RT "Mutation in the Drosophila gene encoding UDP-glucose dehydrogenase affects
RT expression of unlinked genes.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Involved in the biosynthesis of glycosaminoglycans;
CC hyaluronan, chondroitin sulfate and heparan sulfate. Required for
CC wingless signaling in different tissues. {ECO:0000269|PubMed:9217004,
CC ECO:0000269|PubMed:9272947, ECO:0000269|PubMed:9342049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-
CC alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22;
CC Evidence={ECO:0000269|PubMed:9217004};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate
CC biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step
CC 1/1. {ECO:0000269|PubMed:9217004}.
CC -!- DISRUPTION PHENOTYPE: 'Wingless-like' cuticular phenotype; reduced
CC growth of imaginal disks and pattern defects.
CC {ECO:0000269|PubMed:9217004, ECO:0000269|PubMed:9272947}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AF007870; AAB63208.1; -; mRNA.
DR EMBL; AF000570; AAB58714.1; -; mRNA.
DR EMBL; AF009013; AAB63462.1; -; mRNA.
DR EMBL; AF001310; AAC97125.1; -; mRNA.
DR EMBL; AH007072; AAC97126.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50631.1; -; Genomic_DNA.
DR EMBL; AY052137; AAK93561.1; -; mRNA.
DR RefSeq; NP_476980.1; NM_057632.4.
DR AlphaFoldDB; O02373; -.
DR SMR; O02373; -.
DR BioGRID; 64209; 9.
DR IntAct; O02373; 1.
DR STRING; 7227.FBpp0076647; -.
DR PaxDb; O02373; -.
DR PRIDE; O02373; -.
DR DNASU; 38760; -.
DR EnsemblMetazoa; FBtr0076938; FBpp0076647; FBgn0261445.
DR GeneID; 38760; -.
DR KEGG; dme:Dmel_CG10072; -.
DR CTD; 24054; -.
DR FlyBase; FBgn0261445; sgl.
DR VEuPathDB; VectorBase:FBgn0261445; -.
DR eggNOG; KOG2666; Eukaryota.
DR HOGENOM; CLU_023810_7_0_1; -.
DR InParanoid; O02373; -.
DR OMA; CECLNLP; -.
DR OrthoDB; 915490at2759; -.
DR PhylomeDB; O02373; -.
DR Reactome; R-DME-173599; Formation of the active cofactor, UDP-glucuronate.
DR SignaLink; O02373; -.
DR UniPathway; UPA00038; UER00491.
DR BioGRID-ORCS; 38760; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38760; -.
DR PRO; PR:O02373; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0261445; Expressed in thoracico-abdominal ganglion (Drosophila) and 57 other tissues.
DR ExpressionAtlas; O02373; baseline and differential.
DR Genevisible; O02373; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IMP:UniProtKB.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IMP:UniProtKB.
DR GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IMP:UniProtKB.
DR GO; GO:0007509; P:mesoderm migration involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017476; UDP-Glc/GDP-Man.
DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR InterPro; IPR028356; UDPglc_DH_euk.
DR PANTHER; PTHR11374; PTHR11374; 1.
DR Pfam; PF00984; UDPG_MGDP_dh; 1.
DR Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR PIRSF; PIRSF500133; UDPglc_DH_euk; 1.
DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52413; SSF52413; 1.
DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome; Wnt signaling pathway.
FT CHAIN 1..476
FT /note="UDP-glucose 6-dehydrogenase"
FT /id="PRO_0000074064"
FT ACT_SITE 272
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 85..89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 126..127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 157..161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 216..220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 263..269
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 272..275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 334..335
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 342
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 439
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT CONFLICT 59
FT /note="K -> R (in Ref. 3; AAC97125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 52875 MW; 1450B9A0C802BBE7 CRC64;
MKVCCIGAGY VGGPTCAVMA LKCPDIVITL VDKSSERIAQ WNSDKLPIYE PGLDEVVKKC
RNVNLFFSTD IETAIKEADL IFISVNTPTK TCGNGKGRAA DLKYVESAAR MIAEIAQSNK
IVVEKSTVPV RAAESIMHIL RANQKPGIHY DILSNPEFLA EGTAINDLLN ADRVLIGGEE
TPEGHQAVEK LSWIYEHWIP KQNILTTNTW SSELSKLAAN AFLAQRISSI NSLSAVCEAT
GADVSEVARA VGLDSRIGSK FLQASVGFGG SCFQKDILNL IYICENLNLP EVAAYWQQVI
DMNEYQKRRF SQKIIESLFN TVSDKRIAIL GFAFKKNTGD TRETAAITVC QTLLEEGAAL
DIYDPKVEPE QIIDDLTHPS VTESPEKVKK AVQIHSDPYS AVRATHALVI CTEWDEFVDL
DFKRIYQSMM KPAYIFDGRK ILDHERLQQI GFHVQTIGKK YQRTGLLRSW GIVPQL
