Quinoprotein glucose dehydrogenase - Escherichia coli (strain K12)

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P15877 (DHG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Quinoprotein glucose dehydrogenase
EC=1.1.5.2

Alternative name(s):
Glucose dehydrogenase [pyrroloquinoline-quinone]

Gene names

Name:	gcd
Ordered Locus Names:	b0124, JW0120

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	796 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	GDH is probably involved in energy conservation rather than in sugar metabolism.
Catalytic activity	D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol.
Cofactor	PQQ.
Subunit structure	Monomer.
Subcellular location	Cell inner membrane; Multi-pass membrane protein; Periplasmic side Ref.7 Ref.8.
Sequence similarities	Belongs to the bacterial PQQ dehydrogenase family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	PQQ
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	non-phosphorylated glucose catabolic process Inferred from genetic interaction Ref.1. Source: EcoCyc
Cellular component	integral to membrane Inferred from direct assay Ref.6. Source: EcoCyc outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from direct assay. Source: EcoCyc pyrroloquinoline quinone binding Inferred from direct assay. Source: EcoCyc quinoprotein glucose dehydrogenase activity Inferred from direct assay Ref.6. Source: EcoCyc ubiquinone binding Inferred from direct assay. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
csdA	Q46925	1	EBI-545666,EBI-545660
ycfH	P0AFQ7	1	EBI-545666,EBI-560527

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 796

796

Quinoprotein glucose dehydrogenase

PRO_0000205339

Regions

Topological domain

1 – 10

Cytoplasmic Probable

Transmembrane

11 – 37

Helical; Probable

Topological domain

38 – 40

Periplasmic Probable

Transmembrane

41 – 58

Helical; Probable

Topological domain

59 – 62

Cytoplasmic Probable

Transmembrane

63 – 81

Helical; Probable

Topological domain

82 – 95

Periplasmic Probable

Transmembrane

96 – 110

Helical; Probable

Topological domain

111 – 118

Cytoplasmic Probable

Transmembrane

119 – 141

Helical; Probable

Topological domain

142 – 796

655

Periplasmic Probable

Sites

Active site

466

Proton acceptor Probable

Experimental info

Sequence conflict

R → L in CAA35706. Ref.1

Sequence conflict

149 – 156

TLSADATP → HLKRRCHT Ref.1

Sequence conflict

149 – 156

TLSADATP → HLKRRCHT Ref.2

Sequence conflict

193

N → K Ref.1

Sequence conflict

193

N → K Ref.2

Sequence conflict

666

Q → H in BAA02174. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P15877 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: D9EDC705A12894E9
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FASTA

796

86,747

        10         20         30         40         50         60 
MAINNTGSRR LLVTLTALFA ALCGLYLLIG GGWLVAIGGS WYYPIAGLVM LGVAWMLWRS 

        70         80         90        100        110        120 
KRAALWLYAA LLLGTMIWGV WEVGFDFWAL TPRSDILVFF GIWLILPFVW RRLVIPASGA 

       130        140        150        160        170        180 
VAALVVALLI SGGILTWAGF NDPQEINGTL SADATPAEAI SPVADQDWPA YGRNQEGQRF 

       190        200        210        220        230        240 
SPLKQINADN VHNLKEAWVF RTGDVKQPND PGEITNEVTP IKVGDTLYLC TAHQRLFALD 

       250        260        270        280        290        300 
AASGKEKWHY DPELKTNESF QHVTCRGVSY HEAKAETASP EVMADCPRRI ILPVNDGRLI 

       310        320        330        340        350        360 
AINAENGKLC ETFANKGVLN LQSNMPDTKP GLYEPTSPPI ITDKTIVMAG SVTDNFSTRE 

       370        380        390        400        410        420 
TSGVIRGFDV NTGELLWAFD PGAKDPNAIP SDEHTFTFNS PNSWAPAAYD AKLDLVYLPM 

       430        440        450        460        470        480 
GVTTPDIWGG NRTPEQERYA SSILALNATT GKLAWSYQTV HHDLWDMDLP AQPTLADITV 

       490        500        510        520        530        540 
NGQKVPVIYA PAKTGNIFVL DRRNGELVVP APEKPVPQGA AKGDYVTPTQ PFSELSFRPT 

       550        560        570        580        590        600 
KDLSGADMWG ATMFDQLVCR VMFHQMRYEG IFTPPSEQGT LVFPGNLGMF EWGGISVDPN 

       610        620        630        640        650        660 
REVAIANPMA LPFVSKLIPR GPGNPMEQPK DAKGTGTESG IQPQYGVPYG VTLNPFLSPF 

       670        680        690        700        710        720 
GLPCKQPAWG YISALDLKTN EVVWKKRIGT PQDSMPFPMP VPVPFNMGMP MLGGPISTAG 

       730        740        750        760        770        780 
NVLFIAATAD NYLRAYNMSN GEKLWQGRLP AGGQATPMTY EVNGKQYVVI SAGGHGSFGT 

       790 
KMGDYIVAYA LPDDVK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, mapping, and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase." Cleton-Jansen A.-M., Goosen N., Fayet O., van de Putte P. J. Bacteriol. 172:6308-6315(1990) [PubMed: 2228962] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Characterization of the gcd gene from Escherichia coli K-12 W3110 and regulation of its expression." Yamada M., Asaoka S., Saier M.H. Jr., Yamada Y. J. Bacteriol. 175:568-571(1993) [PubMed: 8419307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed: 8202364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site." Yamada M., Sumi K., Matsushita K., Adachi O., Yamada Y. J. Biol. Chem. 268:12812-12817(1993) [PubMed: 8509415] [Abstract] Cited for: TOPOLOGY.
[7]	"Protein complexes of the Escherichia coli cell envelope." Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O. J. Biol. Chem. 280:34409-34419(2005) [PubMed: 16079137] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: BL21-DE3.
[8]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: K12 / MG1655 / ATCC 47076.
[9]	"Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens." Cozier G.E., Anthony C. Biochem. J. 312:679-685(1995) [PubMed: 8554505] [Abstract] Cited for: 3D-STRUCTURE MODELING.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X51323 Genomic DNA. Translation: CAA35706.1. D12651 Genomic DNA. Translation: BAA02174.1. U00096 Genomic DNA. Translation: AAC73235.1. AP009048 Genomic DNA. Translation: BAB96699.1.
PIR	JV0107. D64735.
RefSeq	NP_414666.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P15877.
SMR	P15877. Positions 218-250, 443-512, 720-750.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9747N.
IntAct	P15877. 9 interactions.
MINT	MINT-1267882.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000002761; EBESCP00000002761; EBESCG00000002252. EBESCT00000002762; EBESCP00000002762; EBESCG00000002252. EBESCT00000015725; EBESCP00000015016; EBESCG00000014785.
GeneID	944830.
GenomeReviews	Gene locus JW0120 in contig AP009048_GR. Gene locus b0124 in contig U00096_GR.
KEGG	ecj:JW0120. eco:b0124.
PATRIC	32115351. VBIEscCol129921_0127.
Organism-specific databases
EchoBASE	EB0364.
EcoGene	EG10369. gcd.
Phylogenomic databases
eggNOG	COG4993.
GeneTree	EBGT00050000009769.
HOGENOM	HBG586154.
OMA	TGADMWG.
PhylomeDB	P15877.
ProtClustDB	CLSK879560.
Enzyme and pathway databases
BioCyc	EcoCyc:GLUCDEHYDROG-MONOMER. MetaCyc:GLUCDEHYDROG-MONOMER.
BRENDA	1.1.5.2. 2026.
Gene expression databases
Genevestigator	P15877.
Family and domain databases
InterPro	IPR017511. PQQ-dep_membr-bd_DH. IPR019556. PQQ-dependent_C. IPR019551. PQQ-dependent_N. IPR018391. PQQ_beta_propeller_repeat. IPR002372. PQQ_repeat. IPR011047. Quinonprotein_ADH-like. IPR001479. Quinoprotein_DH_CS. [Graphical view]
Gene3D	G3DSA:2.140.10.10. Quinoprotein_alc_DH-like. 3 hits.
KO	K00117.
Pfam	PF01011. PQQ. 5 hits. PF10535. PQQ_C. 1 hit. PF10527. PQQ_N. 1 hit. [Graphical view]
SMART	SM00564. PQQ. 6 hits. [Graphical view]
SUPFAM	SSF50998. Quin_alc_DH_like. 1 hit.
TIGRFAMs	TIGR03074. PQQ_membr_DH. 1 hit.
PROSITE	PS00363. BACTERIAL_PQQ_1. 1 hit. PS00364. BACTERIAL_PQQ_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHG_ECOLI

Accession

Primary (citable) accession number: P15877

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 129 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents