ID   DHG2_PRIMG              Reviewed;         261 AA.
AC   P39483;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Glucose 1-dehydrogenase 2;
DE            EC=1.1.1.47;
DE   AltName: Full=GLCDH-II;
GN   Name=gdhII;
OS   Priestia megaterium (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IAM 1030 / JCM 20016;
RA   Mitamura T., Ebora R.V., Nakai T., Makino Y., Negoro S., Urabe I.,
RA   Okada H.;
RT   "Structure of isozyme genes of glucose dehydrogenase from Bacillus
RT   megaterium IAM1030.";
RL   J. Ferment. Bioeng. 70:363-369(1990).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH;
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   -!- SUBUNIT: Homotetramer.
CC   -!- MISCELLANEOUS: Prefers NADP to NAD.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; D90044; BAA14100.1; -; Genomic_DNA.
DR   PIR; I39853; I39853.
DR   AlphaFoldDB; P39483; -.
DR   SMR; P39483; -.
DR   SABIO-RK; P39483; -.
DR   GO; GO:0047934; F:glucose 1-dehydrogenase (NAD+) activity; IEA:RHEA.
DR   GO; GO:0047935; F:glucose 1-dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0047936; F:glucose 1-dehydrogenase [NAD(P)] activity; IEA:UniProtKB-EC.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..261
FT                   /note="Glucose 1-dehydrogenase 2"
FT                   /id="PRO_0000054610"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         11..35
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   261 AA;  28251 MW;  CEF9AA1425D2999C CRC64;
     MYTDLKDKVV VVTGGSKGLG RAMAVRFGQE QSKVVVNYRS NEEEALEVKK EIEEAGGQAI
     IVRGDVTKEE DVVNLVETAV KEFGSLDVMI NNAGVENPVP SHELSLENWN QVIDTNLTGA
     FLGSREAIKY FVENDIKGNV INMSSVHEMI PWPLFVHYAA SKGGMKLMTE TLALEYAPKG
     IRVNNIGPGA IDTPINAEKF ADPEQRADVE SMIPMGYIGK PEEIASVAAF LASSQASYVT
     GITLFADGGM TKYPSFQAGR G