DHGB_ACICA
ID DHGB_ACICA Reviewed; 478 AA.
AC P13650;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Quinoprotein glucose dehydrogenase B;
DE EC=1.1.5.2;
DE AltName: Full=Glucose dehydrogenase B [pyrroloquinoline-quinone];
DE AltName: Full=Soluble glucose dehydrogenase;
DE Short=s-GDH;
DE Flags: Precursor;
GN Name=gdhB;
OS Acinetobacter calcoaceticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=471;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PP2403, PP2407, and PP2410;
RX PubMed=2671663; DOI=10.1007/bf02464914;
RA Cleton-Jansen A.-M., Goosen N., Vink K., van de Putte P.;
RT "Cloning, characterization and DNA sequencing of the gene encoding the Mr
RT 50,000 quinoprotein glucose dehydrogenase from Acinetobacter
RT calcoaceticus.";
RL Mol. Gen. Genet. 217:430-436(1989).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, AND
RP SUBUNIT.
RX PubMed=10366508; DOI=10.1006/jmbi.1999.2766;
RA Oubrie A., Rozeboom H.J., Kalk K.H., Duine J.A., Dijkstra B.W.;
RT "The 1.7 A crystal structure of the apo form of the soluble quinoprotein
RT glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel
RT internal conserved sequence repeat.";
RL J. Mol. Biol. 289:319-333(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUCOSE; PQQ AND
RP CALCIUM, AND SUBUNIT.
RX PubMed=10508152; DOI=10.1093/emboj/18.19.5187;
RA Oubrie A., Rozeboom H.J., Kalk K.H., Olsthoorn A.J.J., Duine J.A.,
RA Dijkstra B.W.;
RT "Structure and mechanism of soluble quinoprotein glucose dehydrogenase.";
RL EMBO J. 18:5187-5194(1999).
CC -!- FUNCTION: Oxidizes glucose to gluconolactone.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + D-glucose = a ubiquinol + D-glucono-1,5-
CC lactone; Xref=Rhea:RHEA:22152, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:4167, ChEBI:CHEBI:16217, ChEBI:CHEBI:16389,
CC ChEBI:CHEBI:17976; EC=1.1.5.2;
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Note=Binds 1 PQQ group per subunit.;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 3 Ca(2+) ions per subunit.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10366508,
CC ECO:0000269|PubMed:10508152}.
CC -!- BIOTECHNOLOGY: Potent biocatalyst for the accurate in vivo monitoring
CC of blood glucose in the management of diabetes.
CC -!- MISCELLANEOUS: Acinetobacter calcoaceticus contains two different PQQ
CC dependent enzymes with GDH activity. GDH-A prefers 2-deoxyglucose as
CC substrate, the specific substrates for GDH-B are disaccharides.
CC -!- SIMILARITY: Belongs to the PQQ oxidoreductase GdhB family.
CC {ECO:0000305}.
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DR EMBL; X15871; CAA33881.1; -; Genomic_DNA.
DR PIR; S04784; S04784.
DR PDB; 1C9U; X-ray; 2.20 A; A/B=25-478.
DR PDB; 1CQ1; X-ray; 1.90 A; A/B=25-478.
DR PDB; 1CRU; X-ray; 1.50 A; A/B=25-478.
DR PDB; 1QBI; X-ray; 1.72 A; A/B=25-478.
DR PDB; 5MIN; X-ray; 1.76 A; A/B=25-477.
DR PDBsum; 1C9U; -.
DR PDBsum; 1CQ1; -.
DR PDBsum; 1CRU; -.
DR PDBsum; 1QBI; -.
DR PDBsum; 5MIN; -.
DR AlphaFoldDB; P13650; -.
DR SMR; P13650; -.
DR STRING; 471.BUM88_11175; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB04361; Methyldiazene.
DR DrugBank; DB03205; Pyrroloquinoline Quinone.
DR BioCyc; MetaCyc:MON-15518; -.
DR BRENDA; 1.1.5.2; 99.
DR BRENDA; 1.1.99.35; 99.
DR EvolutionaryTrace; P13650; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008876; F:quinoprotein glucose dehydrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR012938; Glc/Sorbosone_DH.
DR InterPro; IPR019893; PQQ-dependent_DH_s-GDH.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR Pfam; PF07995; GSDH; 2.
DR SUPFAM; SSF50952; SSF50952; 1.
DR TIGRFAMs; TIGR03606; non_repeat_PQQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Metal-binding; Oxidoreductase; PQQ; Signal.
FT SIGNAL 1..24
FT CHAIN 25..478
FT /note="Quinoprotein glucose dehydrogenase B"
FT /id="PRO_0000025583"
FT REGION 252..253
FT /note="PQQ"
FT REGION 430..432
FT /note="PQQ"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT BINDING 100
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 167
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 192
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 252
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 367
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 372
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:10508152"
FT BINDING 401
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:10508152"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1CRU"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1CRU"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1CRU"
FT TURN 110..114
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1C9U"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:1CRU"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 151..162
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1CRU"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:1CRU"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1CRU"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1C9U"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:1CRU"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:1CRU"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1CRU"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:1CRU"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:1CRU"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 394..402
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 414..425
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:1C9U"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:1CRU"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:1C9U"
FT STRAND 470..475
FT /evidence="ECO:0007829|PDB:1CRU"
SQ SEQUENCE 478 AA; 52773 MW; A32CF45F55078648 CRC64;
MNKHLLAKIA LLSAVQLVTL SAFADVPLTP SQFAKAKSEN FDKKVILSNL NKPHALLWGP
DNQIWLTERA TGKILRVNPE SGSVKTVFQV PEIVNDADGQ NGLLGFAFHP DFKNNPYIYI
SGTFKNPKST DKELPNQTII RRYTYNKSTD TLEKPVDLLA GLPSSKDHQS GRLVIGPDQK
IYYTIGDQGR NQLAYLFLPN QAQHTPTQQE LNGKDYHTYM GKVLRLNLDG SIPKDNPSFN
GVVSHIYTLG HRNPQGLAFT PNGKLLQSEQ GPNSDDEINL IVKGGNYGWP NVAGYKDDSG
YAYANYSAAA NKSIKDLAQN GVKVAAGVPV TKESEWTGKN FVPPLKTLYT VQDTYNYNDP
TCGEMTYICW PTVAPSSAYV YKGGKKAITG WENTLLVPSL KRGVIFRIKL DPTYSTTYDD
AVPMFKSNNR YRDVIASPDG NVLYVLTDTA GNVQKDDGSV TNTLENPGSL IKFTYKAK
