DHGL_DROPS
ID DHGL_DROPS Reviewed; 625 AA.
AC P18172; Q294Q6; Q56RL3;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 4.
DT 03-AUG-2022, entry version 126.
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=GA11047;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
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=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 114-605.
RX PubMed=15545653; DOI=10.1534/genetics.104.033068;
RA Bartolome C., Maside X., Yi S., Grant A.L., Charlesworth B.;
RT "Patterns of selection on synonymous and nonsynonymous variants in
RT Drosophila miranda.";
RL Genetics 169:1495-1507(2005).
RN [4]
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 -!- 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=AAA28572.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=EAL28908.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; M29299; AAA28572.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000070; EAL28908.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY754494; AAX13069.1; -; Genomic_DNA.
DR PIR; B39019; B39019.
DR STRING; 7237.FBpp0281212; -.
DR eggNOG; KOG1238; Eukaryota.
DR InParanoid; P18172; -.
DR Proteomes; UP000001819; Genome assembly.
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 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 /evidence="ECO:0000250"
FT CHAIN 43..625
FT /note="Glucose dehydrogenase [FAD, quinone]"
FT /id="PRO_0000012336"
FT CHAIN 43..612
FT /note="Glucose dehydrogenase [FAD, quinone] short protein"
FT /id="PRO_0000012337"
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 168
FT /note="D -> E (in Ref. 1; AAA28572)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="H -> Q (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 68599 MW; 8243BDB400D9F522 CRC64;
MATSPSSCDC LVGVPTGPTL ASTCGGSAFM LFMGLLEVFI RSQCDLEDPC GRASTRFRSE
PDYEYDFIVI GGGSAGSVVA SRLSEVPQWK VLLIEAGGDE PVGAQIPSMF LNFIGSDIDY
RYNTEPERMA CLSSMEQRCY WPRGKVLGGT SVMNGMMYIR GNREDYDDWA AQGNPGWSYQ
DVLPFFKKSE DNLELDAVGT EYHAKGGLLP VGKFPYNPPL SYALLKAGEE MGFSVQDLNG
QNSTGFMIAQ MTARNGIRYS SARAFLRPAR MRNNLHILLN TTVTKVLIHP GTKNVVGVEV
SDQFGSMRKI LVKKEVIVSG GAVNSPQILL LSGVGPKEDL QKVNVRPVHH LPGVGKNLHN
HVAYFTNFFI DDADTAPLNW ATAMEYLLFR DGLMSGTGIS DVTAKMATRW ADRPNLPDLQ
LYFGGYLASC ARTGQVGELL SNNSRAIQIF PAVLNPKSRG YITLRSADPL DPPRIFANYL
TDERDVKTLV EGIKFAIRLS QTSPLKQYGM RLDKTVVKGC ESHAFASDAY WECAVRQNTG
PENHQAGSCK MGPSHDPMAV VNHELRVHGV RGLRVMDTSI MPKVTAGNTH APAVMIAEKG
AYLLKRAWGA KVURVDATWT LHRVI
