ID   DHGB_BACME              Reviewed;         262 AA.
AC   P07999;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 2.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=Glucose 1-dehydrogenase B;
DE            EC=1.1.1.47;
GN   Name=gdhB;
OS   Bacillus megaterium.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1404;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=84108870; 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
RP   207 AND 258.
RC   STRAIN=M1286;
RX   MEDLINE=88271315; PubMed=3134196;
RX   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
RT   Bacillus 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   MEDLINE=84004396; PubMed=6413208;
RX   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
RT   from Bacillus megaterium and sequence analysis of the peptides labeled
RT   with bromoacetyl pyridine.";
RL   Eur. J. Biochem. 136:183-194(1983).
RN   [4]
RP   PROTEIN SEQUENCE OF 218-262.
RX   MEDLINE=84285362; PubMed=6432532;
RX   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
RT   megaterium. Effect of tetranitromethane on the enzyme in the
RT   tetrameric and monomeric state.";
RL   Eur. J. Biochem. 142:533-540(1984).
CC   -!- CATALYTIC ACTIVITY: Beta-D-glucose + NAD(P)(+) = D-glucono-1,5-
CC       lactone + NAD(P)H.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- DEVELOPMENTAL STAGE: Expressed during sporulation.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   PIR; A23260; A23260.
DR   PIR; S01227; S01227.
DR   PIR; S02299; S02299.
DR   HSSP; P40288; 1GCO.
DR   SMR; P07999; 1-262.
DR   BRENDA; 1.1.1.47; 325.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0047936; F:glucose 1-dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cel...; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase; Sporulation.
FT   CHAIN         1    262       Glucose 1-dehydrogenase B.
FT                                /FTId=PRO_0000054614.
FT   NP_BIND      11     35       NADP (By similarity).
FT   ACT_SITE    160    160       Proton acceptor (By similarity).
FT   BINDING     146    146       Substrate (By similarity).
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
//