DHG_ECOLI
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 03-AUG-2022, entry version 199.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 = 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; 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_STEB01000010.1.
DR AlphaFoldDB; P15877; -.
DR SMR; P15877; -.
DR BioGRID; 4261958; 11.
DR DIP; DIP-9747N; -.
DR IntAct; P15877; 9.
DR STRING; 511145.b0124; -.
DR jPOST; P15877; -.
DR PaxDb; P15877; -.
DR PRIDE; P15877; -.
DR EnsemblBacteria; AAC73235; AAC73235; b0124.
DR EnsemblBacteria; BAB96699; BAB96699; BAB96699.
DR GeneID; 944830; -.
DR KEGG; ecj:JW0120; -.
DR KEGG; eco:b0124; -.
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; LVWNWDS; -.
DR PhylomeDB; P15877; -.
DR BioCyc; EcoCyc:GLUCDEHYDROG-MON; -.
DR BioCyc; MetaCyc:GLUCDEHYDROG-MON; -.
DR PRO; PR:P15877; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of 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 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; 6.
DR SMART; SM00564; PQQ; 6.
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 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
