DHGL_DROME
ID DHGL_DROME Reviewed; 625 AA.
AC P18173; Q9VI87;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Glucose dehydrogenase [FAD, quinone];
DE EC=1.1.5.9;
DE Contains:
DE RecName: Full=Glucose dehydrogenase [FAD, quinone] short protein;
DE Flags: Precursor;
GN Name=Gld; ORFNames=CG1152;
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 [GENOMIC DNA].
RX PubMed=2108306; DOI=10.1093/oxfordjournals.molbev.a040592;
RA Krasney P.A., Carr C.M., Cavener D.R.;
RT "Evolution of the glucose dehydrogenase gene in Drosophila.";
RL Mol. Biol. Evol. 7:155-177(1990).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
RX PubMed=3143620; DOI=10.1093/genetics/120.2.475;
RA Whetten R., Organ E., Krasney P., Cox-Foster D., Cavener D.R.;
RT "Molecular structure and transformation of the glucose dehydrogenase gene
RT in Drosophila melanogaster.";
RL Genetics 120:475-484(1988).
RN [5]
RP SIMILARITY TO YEAST ALCOHOL OXIDASE.
RX PubMed=2002763; DOI=10.1093/oxfordjournals.molbev.a040634;
RA Cavener D.R., Krasney P.;
RT "Drosophila glucose dehydrogenase and yeast alcohol oxidase are homologous
RT and share N-terminal homology with other flavoenzymes.";
RL Mol. Biol. Evol. 8:144-150(1991).
RN [6]
RP SELENOCYSTEINE AT SEC-613.
RA Perlaky S., Merritt K., Cavener D.;
RT "Incorporation of selenocysteine at a UGA codon of Gld.";
RL (In) Proceedings of the 39th annual Drosophila research conference,
RL pp.39:414C-414C, Washington D.C. (1998).
CC -!- FUNCTION: Essential for cuticular modification during development.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + D-glucose = a quinol + D-glucono-1,5-lactone;
CC Xref=Rhea:RHEA:47372, ChEBI:CHEBI:4167, ChEBI:CHEBI:16217,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.1.5.9;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted as part of the seminal
CC fluid transferred to females.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28571.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF54038.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; M29298; AAA28571.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014297; AAF54038.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X13582; CAA31918.1; -; Genomic_DNA.
DR PIR; A39019; A39019.
DR RefSeq; NP_477503.1; NM_058155.5.
DR BioGRID; 66070; 3.
DR IntAct; P18173; 1.
DR STRING; 7227.FBpp0081114; -.
DR PaxDb; P18173; -.
DR PRIDE; P18173; -.
DR GeneID; 40875; -.
DR KEGG; dme:Dmel_CG1152; -.
DR CTD; 40875; -.
DR FlyBase; FBgn0001112; Gld.
DR VEuPathDB; VectorBase:FBgn0001112; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_7_0_1; -.
DR InParanoid; P18173; -.
DR PhylomeDB; P18173; -.
DR BioGRID-ORCS; 40875; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40875; -.
DR PRO; PR:P18173; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR ExpressionAtlas; P18173; baseline and differential.
DR Genevisible; P18173; DM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0140762; F:glucose dehydrogenase (FAD, quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; TAS:FlyBase.
DR GO; GO:0008364; P:pupal chitin-based cuticle development; TAS:FlyBase.
DR GO; GO:0046693; P:sperm storage; IMP:FlyBase.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome; Secreted;
KW Selenocysteine; Signal.
FT SIGNAL 1..42
FT CHAIN 43..625
FT /note="Glucose dehydrogenase [FAD, quinone]"
FT /id="PRO_0000012334"
FT CHAIN 43..612
FT /note="Glucose dehydrogenase [FAD, quinone] short protein"
FT /id="PRO_0000012335"
FT ACT_SITE 544
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 66..95
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305"
FT NON_STD 613
FT /note="Selenocysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="Q -> R (in Ref. 1; AAA28571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 68434 MW; 02664FC3ABEEEDFC CRC64;
MSASASACDC LVGVPTGPTL ASTCGGSAFM LFMGLLEVFI RSQCDLEDPC GRASSRFRSE
PDYEYDFIVI GGGSAGSVVA SRLSEVPQWK VLLIEAGGDE PVGAQIPSMF LNFIGSDIDY
RYNTEPEPMA CLSSMEQRCY WPRGKVLGGT SVLNGMMYVR GNREDYDDWA ADGNPGWAYN
DVLPFFKKSE DNLDLDEVGT EYHAKGGLLP VGKFPYNPPL SYAILKAGEE LGFSVHDLNG
QNSTGFMIAQ MTARNGIRYS SARAFLRPAR MRNNLHILLN TTATKILIHP HTKNVLGVEV
SDQFGSTRKI LVKKEVVLSA GAVNSPHILL LSGVGPKDEL QQVNVRTVHN LPGVGKNLHN
HVTYFTNFFI DDADTAPLNW ATAMEYLLFR DGLMSGTGIS DVTAKLATRY ADSPERPDLQ
LYFGGYLASC ARTGQVGELL SNNSRSIQIF PAVLNPRSRG FIGLRSADPL EPPRIVANYL
THEQDVKTLV EGIKFVIRLS QTTPLKQYGM RLDKTVVKGC EAHAFGSDAY WECAVRQNTG
PENHQAGSCK MGPSHDPMAV VNHELRVHGI RGLRVMDTSI MPKVSSGNTH APAVMIAEKG
AYLLKRAWGA KVURVDATWT LHRVI
