ID   DHG_ECOLI               Reviewed;         796 AA.
AC   P15877;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   04-NOV-2026, entry version 216.
DE   RecName: Full=Quinoprotein glucose dehydrogenase;
DE            EC=1.1.5.2 {ECO:0000269|PubMed:8509415};
DE   AltName: Full=Glucose dehydrogenase [pyrroloquinoline-quinone];
GN   Name=gcd; OrderedLocusNames=b0124, JW0120;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2228962; DOI=10.1128/jb.172.11.6308-6315.1990;
RA   Cleton-Jansen A.-M., Goosen N., Fayet O., van de Putte P.;
RT   "Cloning, mapping, and sequencing of the gene encoding Escherichia coli
RT   quinoprotein glucose dehydrogenase.";
RL   J. Bacteriol. 172:6308-6315(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8419307; DOI=10.1128/jb.175.2.568-571.1993;
RA   Yamada M., Asaoka S., Saier M.H. Jr., Yamada Y.;
RT   "Characterization of the gcd gene from Escherichia coli K-12 W3110 and
RT   regulation of its expression.";
RL   J. Bacteriol. 175:568-571(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA   Fujita N., Mori H., Yura T., Ishihama A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT   4.1 min (110,917-193,643 bp) region.";
RL   Nucleic Acids Res. 22:1637-1639(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND TOPOLOGY.
RX   PubMed=8509415; DOI=10.1016/s0021-9258(18)31460-1;
RA   Yamada M., Sumi K., Matsushita K., Adachi O., Yamada Y.;
RT   "Topological analysis of quinoprotein glucose dehydrogenase in Escherichia
RT   coli and its ubiquinone-binding site.";
RL   J. Biol. Chem. 268:12812-12817(1993).
RN   [7]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=BL21-DE3;
RX   PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA   Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA   von Heijne G., Daley D.O.;
RT   "Protein complexes of the Escherichia coli cell envelope.";
RL   J. Biol. Chem. 280:34409-34419(2005).
RN   [8]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
RN   [9]
RP   3D-STRUCTURE MODELING.
RX   PubMed=8554505; DOI=10.1042/bj3120679;
RA   Cozier G.E., Anthony C.;
RT   "Structure of the quinoprotein glucose dehydrogenase of Escherichia coli
RT   modelled on that of methanol dehydrogenase from Methylobacterium
RT   extorquens.";
RL   Biochem. J. 312:679-685(1995).
CC   -!- FUNCTION: GDH is probably involved in energy conservation rather than
CC       in sugar metabolism. {ECO:0000305|PubMed:8509415}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + D-glucose = D-glucono-1,5-lactone + a
CC         ubiquinol; 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; Evidence={ECO:0000269|PubMed:8509415};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22153;
CC         Evidence={ECO:0000305|PubMed:8509415};
CC   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC   -!- SUBUNIT: Monomer.
CC   -!- INTERACTION:
CC       P15877; Q46925: csdA; NbExp=2; IntAct=EBI-545666, EBI-545660;
CC       P15877; P0AFQ7: ycfH; NbExp=2; IntAct=EBI-545666, EBI-560527;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC       ECO:0000269|PubMed:16079137}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16079137}; Periplasmic
CC       side {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16079137}.
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X51323; CAA35706.1; -; Genomic_DNA.
DR   EMBL; D12651; BAA02174.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73235.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAB96699.1; -; Genomic_DNA.
DR   PIR; D64735; JV0107.
DR   RefSeq; NP_414666.1; NC_000913.3.
DR   RefSeq; WP_001306211.1; NZ_CP009789.1.
DR   AlphaFoldDB; P15877; -.
DR   SMR; P15877; -.
DR   BioGRID; 4261958; 17.
DR   DIP; DIP-9747N; -.
DR   FunCoup; P15877; 80.
DR   IntAct; P15877; 9.
DR   STRING; 511145.b0124; -.
DR   jPOST; P15877; -.
DR   PaxDb; 511145-b0124; -.
DR   EnsemblBacteria; AAC73235; AAC73235; b0124.
DR   GeneID; 944830; -.
DR   KEGG; ecj:JW0120; -.
DR   KEGG; eco:b0124; -.
DR   KEGG; ecoc:C3026_00525; -.
DR   PATRIC; fig|1411691.4.peg.2158; -.
DR   EchoBASE; EB0364; -.
DR   eggNOG; COG4993; Bacteria.
DR   HOGENOM; CLU_018478_1_0_6; -.
DR   InParanoid; P15877; -.
DR   OMA; AAEWTYG; -.
DR   OrthoDB; 9794322at2; -.
DR   PhylomeDB; P15877; -.
DR   BioCyc; EcoCyc:GLUCDEHYDROG-MONOMER; -.
DR   BioCyc; MetaCyc:GLUCDEHYDROG-MONOMER; -.
DR   BRENDA; 1.1.5.2; 2026.
DR   PRO; PR:P15877; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P15877; -.
DR   GO; GO:0016020; C:membrane; IDA:EcoCyc.
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:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR   GO; GO:0070968; F:pyrroloquinoline quinone binding; IDA:EcoCyc.
DR   GO; GO:0008876; F:quinoprotein glucose dehydrogenase activity; IDA:EcoCyc.
DR   GO; GO:0048039; F:ubiquinone binding; IDA:EcoCyc.
DR   GO; GO:0019595; P:non-phosphorylated glucose catabolic process; EXP:EcoCyc.
DR   CDD; cd10280; PQQ_mGDH; 1.
DR   FunFam; 2.140.10.10:FF:000001; Quinoprotein glucose dehydrogenase; 1.
DR   Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 1.
DR   InterPro; IPR018391; PQQ_b-propeller_rpt.
DR   InterPro; IPR017511; PQQ_mDH.
DR   InterPro; IPR002372; PQQ_rpt_dom.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_sf.
DR   InterPro; IPR001479; Quinoprotein_DH_CS.
DR   NCBIfam; TIGR03074; PQQ_membr_DH; 1.
DR   PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR   PANTHER; PTHR32303:SF4; QUINOPROTEIN GLUCOSE DEHYDROGENASE; 1.
DR   Pfam; PF01011; PQQ; 1.
DR   SMART; SM00564; PQQ; 6.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS00363; BACTERIAL_PQQ_1; 1.
DR   PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Oxidoreductase; PQQ;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..796
FT                   /note="Quinoprotein glucose dehydrogenase"
FT                   /id="PRO_0000205339"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:8509415"
FT   TRANSMEM        11..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        38..40
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:8509415"
FT   TRANSMEM        41..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        59..62
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:8509415"
FT   TRANSMEM        63..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        82..95
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:8509415"
FT   TRANSMEM        96..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        111..118
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:8509415"
FT   TRANSMEM        119..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        142..796
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:8509415"
FT   ACT_SITE        466
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        59
FT                   /note="R -> L (in Ref. 1; CAA35706)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149..156
FT                   /note="TLSADATP -> HLKRRCHT (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        193
FT                   /note="N -> K (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        666
FT                   /note="Q -> H (in Ref. 2; BAA02174)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   796 AA;  86747 MW;  D9EDC705A12894E9 CRC64;
     MAINNTGSRR LLVTLTALFA ALCGLYLLIG GGWLVAIGGS WYYPIAGLVM LGVAWMLWRS
     KRAALWLYAA LLLGTMIWGV WEVGFDFWAL TPRSDILVFF GIWLILPFVW RRLVIPASGA
     VAALVVALLI SGGILTWAGF NDPQEINGTL SADATPAEAI SPVADQDWPA YGRNQEGQRF
     SPLKQINADN VHNLKEAWVF RTGDVKQPND PGEITNEVTP IKVGDTLYLC TAHQRLFALD
     AASGKEKWHY DPELKTNESF QHVTCRGVSY HEAKAETASP EVMADCPRRI ILPVNDGRLI
     AINAENGKLC ETFANKGVLN LQSNMPDTKP GLYEPTSPPI ITDKTIVMAG SVTDNFSTRE
     TSGVIRGFDV NTGELLWAFD PGAKDPNAIP SDEHTFTFNS PNSWAPAAYD AKLDLVYLPM
     GVTTPDIWGG NRTPEQERYA SSILALNATT GKLAWSYQTV HHDLWDMDLP AQPTLADITV
     NGQKVPVIYA PAKTGNIFVL DRRNGELVVP APEKPVPQGA AKGDYVTPTQ PFSELSFRPT
     KDLSGADMWG ATMFDQLVCR VMFHQMRYEG IFTPPSEQGT LVFPGNLGMF EWGGISVDPN
     REVAIANPMA LPFVSKLIPR GPGNPMEQPK DAKGTGTESG IQPQYGVPYG VTLNPFLSPF
     GLPCKQPAWG YISALDLKTN EVVWKKRIGT PQDSMPFPMP VPVPFNMGMP MLGGPISTAG
     NVLFIAATAD NYLRAYNMSN GEKLWQGRLP AGGQATPMTY EVNGKQYVVI SAGGHGSFGT
     KMGDYIVAYA LPDDVK
//