ID   DHG3_PRIMG              Reviewed;         261 AA.
AC   P39484;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Glucose 1-dehydrogenase 3;
DE            EC=1.1.1.47;
DE   AltName: Full=GLCDH-III;
GN   Name=gdhIII;
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;
RX   PubMed=1629157; DOI=10.1128/jb.174.15.5013-5020.1992;
RA   Nagao T., Mitamura T., Wang X.H., Negoro S., Yomo T., Urabe I., Okada H.;
RT   "Cloning, nucleotide sequences, and enzymatic properties of glucose
RT   dehydrogenase isozymes from Bacillus megaterium IAM1030.";
RL   J. Bacteriol. 174:5013-5020(1992).
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 NAD to NADP; very unstable compared to the other
CC       isoenzymes and 2M NaCl enhances its pH and thermostability.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; D10625; BAA01475.1; -; Genomic_DNA.
DR   PIR; I40224; I40224.
DR   AlphaFoldDB; P39484; -.
DR   SMR; P39484; -.
DR   SABIO-RK; P39484; -.
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   NAD; Oxidoreductase.
FT   CHAIN           1..261
FT                   /note="Glucose 1-dehydrogenase 3"
FT                   /id="PRO_0000054611"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         11..35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   261 AA;  28202 MW;  7F50C7C5F53F5DB1 CRC64;
     MYTDLKDKVV VITGGSTGLG RAMAVRFGQE EAKVVINYYN NEEEALDAKK EVEEAGGQAI
     IVQGDVTKEE DVVNLVQTAI KEFGTLDVMI NNAGVENPVP SHELSLDNWN KVIDTNLTGA
     FLGSREAIKY FVENDIKGNV INMSSVHEMI PWPLFVHYAA SKGGMKQMTE TLALEYAPKG
     IRVNNIGPGA MNTPINAEKF ADPVQRADVE SMIPMGYIGK PEEVAAVAAF LASSQASYVT
     GITLFADGGM TKYPSFQTGR G