DHG_PRIMG
ID DHG_PRIMG Reviewed; 261 AA.
AC P40288;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glucose 1-dehydrogenase;
DE EC=1.1.1.47;
OS Priestia megaterium (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1404;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-29, AND
RP MUTAGENESIS.
RC STRAIN=IWG3;
RX PubMed=2495285; DOI=10.1016/s0021-9258(18)83360-9;
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; DOI=10.1093/oxfordjournals.jbchem.a002858;
RA Yamamoto K., Kurisu G., Kusunoki M., Tabata S., Urabe I., Osaki S.;
RT "Crystal structure of glucose dehydrogenase from Bacillus megaterium IWG3
RT at 1.7 A resolution.";
RL J. Biochem. 129:303-312(2001).
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. {ECO:0000269|PubMed:11173533}.
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 EMBL; J04805; AAA22475.1; -; Genomic_DNA.
DR PIR; A33528; A33528.
DR RefSeq; WP_033578120.1; NZ_VEEA01000001.1.
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 AlphaFoldDB; P40288; -.
DR SMR; P40288; -.
DR GeneID; 48011496; -.
DR BRENDA; 1.1.1.47; 656.
DR EvolutionaryTrace; P40288; -.
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 3D-structure; Direct protein sequencing; NADP; Oxidoreductase; Sporulation.
FT CHAIN 1..261
FT /note="Glucose 1-dehydrogenase"
FT /id="PRO_0000054615"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT BINDING 11..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11173533"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 96
FT /note="E->A,G,K: Heat stable."
FT /evidence="ECO:0000269|PubMed:2495285"
FT MUTAGEN 108
FT /note="D->N: Heat stable."
FT /evidence="ECO:0000269|PubMed:2495285"
FT MUTAGEN 112
FT /note="V->A: Heat stable."
FT /evidence="ECO:0000269|PubMed:2495285"
FT MUTAGEN 133
FT /note="E->K: Heat stable."
FT /evidence="ECO:0000269|PubMed:2495285"
FT MUTAGEN 183
FT /note="V->I: Heat stable."
FT /evidence="ECO:0000269|PubMed:2495285"
FT MUTAGEN 194
FT /note="P->Q: Heat stable."
FT /evidence="ECO:0000269|PubMed:2495285"
FT MUTAGEN 210
FT /note="E->K: Heat stable."
FT /evidence="ECO:0000269|PubMed:2495285"
FT MUTAGEN 217
FT /note="Y->H: Heat stable."
FT /evidence="ECO:0000269|PubMed:2495285"
FT MUTAGEN 252
FT /note="Q->L: Heat stable."
FT /evidence="ECO:0000269|PubMed:2495285"
FT MUTAGEN 253
FT /note="Y->C: Heat stable."
FT /evidence="ECO:0000269|PubMed:2495285"
FT MUTAGEN 258
FT /note="A->G: Heat stable."
FT /evidence="ECO:0000269|PubMed:2495285"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1GEE"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:1GEE"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:1GEE"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:1GEE"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 118..133
FT /evidence="ECO:0007829|PDB:1GEE"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 156..176
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1GEE"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1GEE"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:1GEE"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:1GEE"
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
