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 13-SEP-2023, entry version 112. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:MONOMER-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; TolB, C-terminal domain; 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 NCBIfam; TIGR03606; non_repeat_PQQ; 1. DR PANTHER; PTHR19328; HEDGEHOG-INTERACTING PROTEIN; 1. DR PANTHER; PTHR19328:SF13; HIPL1 PROTEIN; 1. DR Pfam; PF07995; GSDH; 2. DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 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 //