ID   DHGA_ACICA              Reviewed;         801 AA.
AC   P05465;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Quinoprotein glucose dehydrogenase A;
DE            EC=1.1.99.35;
DE   AltName: Full=GDH-A;
DE   AltName: Full=Glucose dehydrogenase A [pyrroloquinoline-quinone];
DE   AltName: Full=Quinoprotein glucose DH;
DE   Flags: Precursor;
GN   Name=gdhA;
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=LMD 79.41;
RX   PubMed=3399393; DOI=10.1093/nar/16.13.6228;
RA   Cleton-Jansen A.-M., Goosen N., Odle G., van de Putte P.;
RT   "Nucleotide sequence of the gene coding for quinoprotein glucose
RT   dehydrogenase from Acinetobacter calcoaceticus.";
RL   Nucleic Acids Res. 16:6228-6228(1988).
CC   -!- FUNCTION: Catalyzes an exceptionally high rate of oxidation of a wide
CC       range of aldose sugars, including D-glucose, galactose, arabinose and
CC       xylose, and also the disaccharides lactose, cellobiose and maltose.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + D-glucose = AH2 + D-glucono-1,5-lactone;
CC         Xref=Rhea:RHEA:24540, ChEBI:CHEBI:4167, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:16217, ChEBI:CHEBI:17499; EC=1.1.99.35;
CC   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein;
CC       Periplasmic side.
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 bacterial PQQ dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X07235; CAA30222.1; -; Genomic_DNA.
DR   PIR; S00943; S00943.
DR   AlphaFoldDB; P05465; -.
DR   SMR; P05465; -.
DR   STRING; 471.BUM88_16395; -.
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:0004344; F:glucose dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
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; 4.
DR   SMART; SM00564; PQQ; 5.
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; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..801
FT                   /note="Quinoprotein glucose dehydrogenase A"
FT                   /id="PRO_0000025557"
FT   TRANSMEM        39..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        471
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   801 AA;  86957 MW;  2F4EA222EB5450D8 CRC64;
     MNQPTSRSGL TTFTVIIIGL LALFLLIGGI WLATLGGSIY YIIAGVLLLI VAWQLYKRAS
     TALWFYAALM LGTIIWSVWE VGTDFWALAP RLDILGILGL WLLVPAVTRG INNLGSSKVA
     LSSTLAIAIV LMVYSIFNDP QEINGEIKTP QPETAQAVPG VAESDWPAYG RTQAGVRYSP
     LKQINDQNVK DLKVAWTLRT GDLKTDNDSG ETTNQVTPIK IGNNMFICTA HQQLIAIDPA
     TGKEKWRFDP KLKTDKSFQH LTCRGVMYYD ANNTTEFATS LQSKKSSSTQ CPRKVFVPVN
     DGRLVAVNAD TGKACTDFGQ NGQVNLQEFM PYAYPGGYNP TSPGIVTGST VVIAGSVTDN
     YSNKEPSGVI RGYDVNTGKL LWVFDTGAAD PNAMPGEGTT FVHNSPNAWA PLAYDAKLDI
     VYVPTGVGTP DIWGGDRTEL KERYANSMLA INASTGKLVW NFQTTHHDLW DMDVPSQPSL
     ADIKNKAGQT VPAIYVLTKT GNAFVLDRRN GQPIVPVTEK PVPQTVKRGP QTKGEFYSKT
     QPFSDLNLAP QDKLTDKDMW GATMLDQLMC RVSFKRLNYD GIYTPPSENG TLVFPGNLGV
     FEWGGMSVNP DRQVAVMNPI GLPFVSRLIP ADPNRAQTAK GAGTEQGVQP MYGVPYGVEI
     SAFLSPLGLP CKQPAWGYVA GVDLKTHEVV WKKRIGTIRD SLPNLFQLPA VKIGVPGLGG
     SISTAGNVMF VGATQDNYLR AFNVTNGKKL WEARLPAGGQ ATPMTYEING KQYVVIMAGG
     HGSFGTKMGD YLVAYALPDN K