Reviewed, UniProtKB/Swiss-Prot P15877 (DHG_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	796 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
Molecular function	Oxidoreductase
PTM	PQQ
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct quinone binding Inferred from electronic annotation. Source: InterPro quinoprotein glucose dehydrogenase activity Inferred from electronic annotation. Source: EC
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	10	Cytoplasmic Probable
	Transmembrane	11 – 37	27	Probable
	Topological domain	38 – 40	3	Periplasmic Probable
	Transmembrane	41 – 58	18	Probable
	Topological domain	59 – 62	4	Cytoplasmic Probable
	Transmembrane	63 – 81	19	Probable
	Topological domain	82 – 95	14	Periplasmic Probable
	Transmembrane	96 – 110	15	Probable
	Topological domain	111 – 118	8	Cytoplasmic Probable
	Transmembrane	119 – 141	23	Probable
	Topological domain	142 – 796	655	Periplasmic Probable
Sites
	Active site	466	1	Proton acceptor Probable
Experimental info
	Sequence conflict	59	1	R → L in CAA35706. Ref.1
	Sequence conflict	149 – 156	8	TLSADATP → HLKRRCHT Ref.1
	Sequence conflict	149 – 156	8	TLSADATP → HLKRRCHT Ref.2
	Sequence conflict	193	1	N → K Ref.1
	Sequence conflict	193	1	N → K Ref.2
	Sequence conflict	666	1	Q → H in BAA02174. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P15877-1 [UniParc]. Last modified November 1, 1997. Version 3. Checksum: D9EDC705A12894E9	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

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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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	AP_000785.1. NP_414666.1.
3D structure databases
HSSP	HSSP built from PDB template 1G72 based on UniProtKB P38539.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:9747N.
IntAct	P15877. 9 interactions.
Genome annotation databases
GeneID	944830.
GenomeReviews	Gene locus JW0120 in contig AP009048_GR. Gene locus b0124 in contig U00096_GR.
KEGG	ecj:JW0120. eco:b0124.
Organism-specific databases
EchoBASE	EB0364.
EcoGene	EG10369. gcd.
CMR	Search...
Phylogenomic databases
HOGENOM	P15877.
OMA	P15877. LTGADMW.
Enzyme and pathway databases
BioCyc	EcoCyc:GLUCDEHYDROG-MON. MetaCyc:GLUCDEHYDROG-MON.
BRENDA	1.1.5.2. 246.
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. Quino_AlcDH-like. IPR001479. Quinoprotein_DH_CS. [Graphical view]
Gene3D	G3DSA:2.140.10.10. Quinoprotein_alc_DH-like. 1 hit.
Pfam	PF01011. PQQ. 7 hits. PF10535. PQQ_C. 1 hit. PF10527. PQQ_N. 1 hit. [Graphical view]
SMART	SM00564. PQQ. 6 hits. [Graphical view]
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:	June 16, 2009
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)