ID   DHG3_BACME              Reviewed;         261 AA.
AC   P39484;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-NOV-2008, entry version 45.
DE   RecName: Full=Glucose 1-dehydrogenase 3;
DE            EC=1.1.1.47;
DE   AltName: Full=GLCDH-III;
GN   Name=gdhIII;
OS   Bacillus megaterium.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IAM 1030;
RX   MEDLINE=92332436; PubMed=1629157;
RA   Nagao T., Mitamura T., Wang X.H., Negoro S., Yomo T., Urabe I.,
RA   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: Beta-D-glucose + NAD(P)(+) = D-glucono-1,5-
CC       lactone + NAD(P)H.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- MISCELLANEOUS: Prefers NAD to NADP; very unstable compared to the
CC       other isoenzymes and 2M NaCl enhances its pH and thermostability.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; D10625; BAA01475.1; -; Genomic_DNA.
DR   PIR; I40224; I40224.
DR   HSSP; P40288; 1GEE.
DR   SMR; P39484; 1-261.
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   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   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN         1    261       Glucose 1-dehydrogenase 3.
FT                                /FTId=PRO_0000054611.
FT   NP_BIND      11     35       NAD (By similarity).
FT   ACT_SITE    158    158       Proton acceptor (By similarity).
FT   BINDING     145    145       Substrate (By similarity).
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
//