ID DHGA_PRIMG Reviewed; 261 AA. AC P10528; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 04-NOV-2026, entry version 119. DE RecName: Full=Glucose 1-dehydrogenase A; DE EC=1.1.1.47 {ECO:0000250|UniProtKB:P07999}; GN Name=gdhA; OS Priestia megaterium (Bacillus megaterium). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Priestia. OX NCBI_TaxID=1404; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=M1286; RX PubMed=3134196; DOI=10.1111/j.1432-1033.1988.tb14124.x; RA Heilmann H.J., Maegert H.-J., Gassen H.G.; RT "Identification and isolation of glucose dehydrogenase genes of Bacillus RT megaterium M1286 and their expression in Escherichia coli."; RL Eur. J. Biochem. 174:485-490(1988). CC -!- FUNCTION: Catalyzes the NAD(P)+-dependent oxidation of D-glucose to D- CC gluconate via gluconolactone (By similarity). Can utilize both NAD(+) CC and NADP(+) as electron acceptor (By similarity). CC {ECO:0000250|UniProtKB:P07999, ECO:0000250|UniProtKB:P40288}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucose + NAD(+) = D-glucono-1,5-lactone + NADH + H(+); CC Xref=Rhea:RHEA:14293, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16217, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.47; CC Evidence={ECO:0000250|UniProtKB:P07999}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucose + NADP(+) = D-glucono-1,5-lactone + NADPH + H(+); CC Xref=Rhea:RHEA:14405, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16217, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.47; CC Evidence={ECO:0000250|UniProtKB:P40288}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P07999}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X12370; CAA30931.1; -; Genomic_DNA. DR PIR; S00812; S00812. DR RefSeq; WP_025749618.1; NZ_AZUJ01000001.1. DR AlphaFoldDB; P10528; -. DR SMR; P10528; -. DR OMA; AAFIACD; -. DR GO; GO:0047934; F:glucose 1-dehydrogenase (NAD+) activity; IEA:UniProtKB-ARBA. DR GO; GO:0047935; F:glucose 1-dehydrogenase (NADP+) activity; IEA:RHEA. DR CDD; cd05358; GlcDH_SDR_c; 1. DR FunFam; 3.40.50.720:FF:000248; Glucose 1-dehydrogenase; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR NCBIfam; NF005559; PRK07231.1; 1. DR NCBIfam; NF006493; PRK08936.1; 1. DR PANTHER; PTHR43639; OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870); 1. DR PANTHER; PTHR43639:SF1; SHORT-CHAIN DEHYDROGENASE_REDUCTASE FAMILY PROTEIN; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 3: Inferred from homology; KW NAD; NADP; Nucleotide-binding; Oxidoreductase. FT CHAIN 1..261 FT /note="Glucose 1-dehydrogenase A" FT /id="PRO_0000054613" FT ACT_SITE 158 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001" FT BINDING 17 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 19 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 65 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 66 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 92 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 94 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 96 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 145 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 147 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 158 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 158 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 162 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 191 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 193 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 195 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 196 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 196 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 199 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:P39485" FT BINDING 261 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000250|UniProtKB:P39485" SQ SEQUENCE 261 AA; 28187 MW; 6FADDA3968DC417C CRC64; MYTDLKDKVV VITGGSTGLG RAMAVRFGQE EAKVVINYYN NEEEALDAKK EVEEAGGQAI IVQGDVTKEE DVVNLVQTAI KEFGTLDVMI NNAGVENPVP SHELSLDNWN KVIDTNLTGA FLGSREAIKY FVENDIKGNV INMSSVHEMI PWPLFVHYAA SKGGMKLMTE TLALEYAPKG IRVNNIGPGA MNTPINAEKF ADPEQRADVE SMIPMGYIGK PEEVAAVAAF LASSQASYVT GITLFADGGM TKYPSFQAGR G //