DHG_GLUOX
ID DHG_GLUOX Reviewed; 808 AA.
AC P27175; Q5FU98;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Quinoprotein glucose dehydrogenase;
DE EC=1.1.5.2;
DE AltName: Full=Glucose dehydrogenase [pyrroloquinoline-quinone];
DE Flags: Precursor;
GN Name=gdh; OrderedLocusNames=GOX0265;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1833618; DOI=10.1007/bf00272157;
RA Cleton-Jansen A.-M., Dekker S., van de Putte P., Goosen N.;
RT "A single amino acid substitution changes the substrate specificity of
RT quinoprotein glucose dehydrogenase in Gluconobacter oxydans.";
RL Mol. Gen. Genet. 229:206-212(1991).
RN [2]
RP SEQUENCE REVISION TO 213.
RA Goosen N.;
RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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 -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein;
CC Periplasmic side.
CC -!- MISCELLANEOUS: The P1 form can oxidize only D-glucose, while the P2
CC form can also oxidize maltose. The sequence of P1 form is shown here.
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase 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; X62710; CAA44594.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP000009; AAW60048.1; -; Genomic_DNA.
DR PIR; S17716; QPKEX.
DR RefSeq; WP_011251851.1; NZ_LT900338.1.
DR AlphaFoldDB; P27175; -.
DR SMR; P27175; -.
DR STRING; 290633.GOX0265; -.
DR EnsemblBacteria; AAW60048; AAW60048; GOX0265.
DR KEGG; gox:GOX0265; -.
DR eggNOG; COG4993; Bacteria.
DR HOGENOM; CLU_018478_1_0_5; -.
DR OMA; YQHMTCR; -.
DR Proteomes; UP000006375; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0008876; F:quinoprotein glucose dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd10280; PQQ_mGDH; 1.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR017511; PQQ_mDH.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR001479; Quinoprotein_DH_CS.
DR PANTHER; PTHR32303:SF4; PTHR32303:SF4; 1.
DR Pfam; PF01011; PQQ; 5.
DR SMART; SM00564; PQQ; 3.
DR SUPFAM; SSF50998; SSF50998; 1.
DR TIGRFAMs; TIGR03074; PQQ_membr_DH; 1.
DR PROSITE; PS00363; BACTERIAL_PQQ_1; 1.
DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Oxidoreductase; PQQ;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..808
FT /note="Quinoprotein glucose dehydrogenase"
FT /id="PRO_0000025558"
FT TRANSMEM 35..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 514..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 470
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT VARIANT 788
FT /note="H -> N (in P2 form)"
FT CONFLICT 4
FT /note="T -> I (in Ref. 1; CAA44594)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="G -> R (in Ref. 1; CAA44594)"
FT /evidence="ECO:0000305"
FT CONFLICT 110..123
FT /note="QIGGTRTTVLPLAG -> ARSVARGRPSCRSP (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="D -> E (in Ref. 1; CAA44594)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="S -> T (in Ref. 1; CAA44594)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="A -> Q (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="T -> M (in Ref. 1; CAA44594)"
FT /evidence="ECO:0000305"
FT CONFLICT 291..292
FT /note="RI -> DS (in Ref. 1; CAA44594)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="D -> E (in Ref. 1; CAA44594)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="R -> A (in Ref. 1; CAA44594)"
FT /evidence="ECO:0000305"
FT CONFLICT 472..473
FT /note="DV -> EL (in Ref. 1; CAA44594)"
FT /evidence="ECO:0000305"
FT CONFLICT 635..636
FT /note="KD -> EN (in Ref. 1; CAA44594)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 808 AA; 87335 MW; 6FFF304215A63D29 CRC64;
MSTTSRPGLW ALITAAVFAL CGAILTVGGA WVAAIGGPLY YVILGLALLA TAFLSFRRNP
AALYLFAVVV FGTVIWELTV VGLDIWALIP RSDIVIILGI WLLLPFVSRQ IGGTRTTVLP
LAGAVGVAVL ALFASLFTDP HDISGDLPTQ IANASPADPD NVPASEWHAY GRTQAGDRWS
PLNQINASNV SNLKVAWHIH TKDMMNSNDP GEATNEATPI EFNNTLYMCS LHQKLFAVDG
ATGNVKWVYD PKLQINPGFQ HLTCRGVSFH ETPANATDSD GNPAPTDCAK RIILPVNDGR
LVEVDADTGK TCSGFGNNGE IDLRVPNQPY TTPGQYEPTS PPVITDKLII ANSAITDNGS
VKQASGATQA FDVYTGKRVW VFDASNPDPN QLPDDSHPVF HPNSPNSWIV SSYDRNLNLV
YIPMGVGTPD QWGGDRTKDS ERFAPGIVAL NADTGKLAWF YQTVHHDLWD MDVPSQPSLV
DVTQKDGTLV PAIYAPTKTG DIFVLDRRTG KEIVPAPETP VPQGAAPGDH TSPTQPMSQL
TLRPKNPLND SDIWGGTIFD QMFCSIYFHT LRYEGPFTPP SLKGSLIFPG DLGMFEWGGL
AVDPQRQVAF ANPISLPFVS QLVPRGPGNP LWPEKDAKGT GGETGLQHNY GIPYAVNLHP
FLDPVLLPFG IKMPCRTPPW GYVAGIDLKT NKVVWQHRNG TLRDSMYGSS LPIPLPPIKI
GVPSLGGPLS TAGNLGFLTA SMDYYIRAYN LTTGKVLWQD RLPAGAQATP ITYAINGKQY
IVTYAGGHNS FPTRMGDDII AYALPDQK
