ID   DHGB_PRIMG              Reviewed;         262 AA.
AC   P07999;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Glucose 1-dehydrogenase B;
DE            EC=1.1.1.47;
GN   Name=gdhB;
OS   Priestia megaterium (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1404;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6420184; DOI=10.1016/0014-5793(84)80003-4;
RA   Jany K.-D., Ulmer W., Froschle M., Pfleiderer G.;
RT   "Complete amino acid sequence of glucose dehydrogenase from Bacillus
RT   megaterium.";
RL   FEBS Lett. 165:6-10(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52, AND SEQUENCE REVISION TO 207 AND
RP   258.
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).
RN   [3]
RP   PROTEIN SEQUENCE OF 27-204.
RX   PubMed=6413208; DOI=10.1111/j.1432-1033.1983.tb07724.x;
RA   Ulmer W., Froschle M., Jany K.-D.;
RT   "Evidence for an essential histidine residue in glucose dehydrogenase from
RT   Bacillus megaterium and sequence analysis of the peptides labeled with
RT   bromoacetyl pyridine.";
RL   Eur. J. Biochem. 136:183-194(1983).
RN   [4]
RP   PROTEIN SEQUENCE OF 218-262.
RX   PubMed=6432532; DOI=10.1111/j.1432-1033.1984.tb08318.x;
RA   Froschle M., Ulmer W., Jany K.-D.;
RT   "Tyrosine modification of glucose dehydrogenase from Bacillus megaterium.
RT   Effect of tetranitromethane on the enzyme in the tetrameric and monomeric
RT   state.";
RL   Eur. J. Biochem. 142:533-540(1984).
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   -!- DEVELOPMENTAL STAGE: Expressed during sporulation.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   PIR; A23260; A23260.
DR   PIR; S01227; S01227.
DR   PIR; S02299; S02299.
DR   AlphaFoldDB; P07999; -.
DR   SMR; P07999; -.
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   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase; Sporulation.
FT   CHAIN           1..262
FT                   /note="Glucose 1-dehydrogenase B"
FT                   /id="PRO_0000054614"
FT   ACT_SITE        160
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         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   262 AA;  28347 MW;  C9281328D634E789 CRC64;
     MYKDLEGKVV VITGSSTGLG KSMAIRFATE KAKVVVNYRS KEDEANSVLE EEIKKVGGEA
     IAVKGDVTVE SDVINLVQSA IKEFGKLDVM INNAGMENPV SSHEMSLSDW NKVIDTNLTG
     AFLGSREAIK YFVENDIKGT VINMSSVHEW KIPWPLFVHY AASKGGMKLM TETLALEYAP
     KGIRVNNIGP GAINTPINAE KFADPEQRAD VESMIPMGYI GEPEEIAAVA WLASSEASYV
     TGITLFADGG MTQYPSFQAG RG