ID   DHG_BACME               Reviewed;         261 AA.
AC   P40288;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-NOV-2008, entry version 52.
DE   RecName: Full=Glucose 1-dehydrogenase;
DE            EC=1.1.1.47;
OS   Bacillus megaterium.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-29, AND
RP   MUTAGENESIS.
RC   STRAIN=IWG3;
RX   MEDLINE=89197943; PubMed=2495285;
RA   Makino Y., Negoro S., Urabe I., Okada H.;
RT   "Stability-increasing mutants of glucose dehydrogenase from Bacillus
RT   megaterium IWG3.";
RL   J. Biol. Chem. 264:6381-6385(1989).
RN   [2]
RP   SEQUENCE REVISION.
RA   Urabe I.;
RL   Submitted (MAR-1989) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD.
RX   PubMed=11173533;
RA   Yamamoto K., Kurisu G., Kusunoki M., Tabata S., Urabe I., Osaki S.;
RT   "Crystal structure of glucose dehydrogenase from Bacillus megaterium
RT   IWG3 at 1.7 A resolution.";
RL   J. Biochem. 129:303-312(2001).
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   EMBL; J04805; AAA22475.1; -; Genomic_DNA.
DR   PIR; A33528; A33528.
DR   PDB; 1G6K; X-ray; 2.00 A; A/B/E/F=1-261.
DR   PDB; 1GCO; X-ray; 1.70 A; A/B/E/F=1-261.
DR   PDB; 1GEE; X-ray; 1.60 A; A/B/E/F=1-261.
DR   PDB; 1RWB; X-ray; 2.00 A; A/B/E/F=1-261.
DR   PDBsum; 1G6K; -.
DR   PDBsum; 1GCO; -.
DR   PDBsum; 1GEE; -.
DR   PDBsum; 1RWB; -.
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; DHase_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DHase.
DR   InterPro; IPR016040; NAD(P)-bd.
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   3D-structure; Direct protein sequencing; NADP; Oxidoreductase;
KW   Sporulation.
FT   CHAIN         1    261       Glucose 1-dehydrogenase.
FT                                /FTId=PRO_0000054615.
FT   NP_BIND      11     35       NADP.
FT   ACT_SITE    158    158       Proton acceptor.
FT   BINDING     145    145       Substrate (By similarity).
FT   MUTAGEN      96     96       E->A,G,K: Heat stable.
FT   MUTAGEN     108    108       D->N: Heat stable.
FT   MUTAGEN     112    112       V->A: Heat stable.
FT   MUTAGEN     133    133       E->K: Heat stable.
FT   MUTAGEN     183    183       V->I: Heat stable.
FT   MUTAGEN     194    194       P->Q: Heat stable.
FT   MUTAGEN     210    210       E->K: Heat stable.
FT   MUTAGEN     217    217       Y->H: Heat stable.
FT   MUTAGEN     252    252       Q->L: Heat stable.
FT   MUTAGEN     253    253       Y->C: Heat stable.
FT   MUTAGEN     258    258       A->G: Heat stable.
FT   HELIX         3      5
FT   STRAND        9     12
FT   HELIX        18     29
FT   STRAND       33     40
FT   HELIX        42     54
FT   STRAND       58     63
FT   HELIX        69     83
FT   STRAND       88     91
FT   HELIX       101    103
FT   HELIX       106    116
FT   HELIX       118    133
FT   STRAND      139    143
FT   HELIX       146    148
FT   HELIX       156    176
FT   HELIX       177    179
FT   STRAND      182    188
FT   HELIX       194    196
FT   TURN        197    201
FT   HELIX       203    210
FT   HELIX       221    232
FT   HELIX       234    236
FT   STRAND      243    247
FT   HELIX       250    252
FT   HELIX       254    259
SQ   SEQUENCE   261 AA;  28085 MW;  C23AC98D304EEB2F CRC64;
     MYKDLEGKVV VITGSSTGLG KSMAIRFATE KAKVVVNYRS KEDEANSVLE EIKKVGGEAI
     AVKGDVTVES DVINLVQSAI KEFGKLDVMI NNAGLENPVS SHEMSLSDWN KVIDTNLTGA
     FLGSREAIKY FVENDIKGTV INMSSVHEKI PWPLFVHYAA SKGGMKLMTE TLALEYAPKG
     IRVNNIGPGA INTPINAEKF ADPEQRADVE SMIPMGYIGE PEEIAAVAAW LASSEASYVT
     GITLFADGGM TQYPSFQAGR G
//