DHG4_PRIMG
ID DHG4_PRIMG Reviewed; 261 AA.
AC P39485;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Glucose 1-dehydrogenase 4;
DE EC=1.1.1.47;
DE AltName: Full=GLCDH-IV;
GN Name=gdhIV;
OS Priestia megaterium (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1404;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IAM 1030 / JCM 20016;
RX PubMed=1629157; DOI=10.1128/jb.174.15.5013-5020.1992;
RA Nagao T., Mitamura T., Wang X.H., Negoro S., Yomo T., Urabe I., 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:
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 -!- INTERACTION:
CC P39485; P39485: gdhIV; NbExp=2; IntAct=EBI-7977646, EBI-7977646;
CC -!- MISCELLANEOUS: Prefers NAD to NADP; 2M NaCl enhances its pH and
CC thermostability.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; D10626; BAA01476.1; -; Genomic_DNA.
DR PIR; I40225; I40225.
DR RefSeq; WP_013055759.1; NZ_WIPB01000013.1.
DR PDB; 3AUS; X-ray; 2.00 A; A/B=1-261.
DR PDB; 3AUT; X-ray; 2.00 A; A/B=1-261.
DR PDB; 3AUU; X-ray; 2.00 A; A/B=1-261.
DR PDB; 3AY6; X-ray; 2.10 A; A/B/C/D=1-261.
DR PDB; 3AY7; X-ray; 1.90 A; A/B=1-261.
DR PDBsum; 3AUS; -.
DR PDBsum; 3AUT; -.
DR PDBsum; 3AUU; -.
DR PDBsum; 3AY6; -.
DR PDBsum; 3AY7; -.
DR AlphaFoldDB; P39485; -.
DR SMR; P39485; -.
DR MINT; P39485; -.
DR GeneID; 64144972; -.
DR OMA; VGQRAWP; -.
DR BRENDA; 1.1.1.47; 656.
DR SABIO-RK; P39485; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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; NAD; Oxidoreductase.
FT CHAIN 1..261
FT /note="Glucose 1-dehydrogenase 4"
FT /id="PRO_0000054612"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 11..35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:3AY7"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:3AY7"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:3AY7"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:3AY7"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:3AY7"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 118..133
FT /evidence="ECO:0007829|PDB:3AY7"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 156..176
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:3AY7"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:3AY7"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:3AY6"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:3AY7"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:3AY7"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:3AY7"
SQ SEQUENCE 261 AA; 28157 MW; 6FBEC9397BCF417C CRC64;
MYTDLKDKVV VITGGSTGLG RAMAVRFGQE EAKVVINYYN NEEEALDAKK EVEEAGGQAI
IVQGDVTKEE DVVNLVQTAI KEFGTLDVMI NNAGVENPVP SHELSLDNWN KVIDTNLTGA
FLGSREAIKY FVENDIKGNV INMSSVHEMI PWPLFVHYAA SKGGMKLMTE TLALEYAPKG
IRVNNIGPGA MNTPINAEKF ADPVQRADVE SMIPMGYIGK PEEVAAVAAF LASSQASYVT
GITLFADGGM TKYPSFQAGR G
