[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=PP24[03,07,10]; DOI=10.1007/BF02464914; PubMed=2671663 [NCBI, ExPASy, EBI, Israel, Japan] Cleton-Jansen A.-M., Goosen N., Vink K., van de Putte P.; "Cloning, characterization and DNA sequencing of the gene encoding the Mr 50,000 quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus."; Mol. Gen. Genet. 217:430-436(1989).
[2]	X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, AND SUBUNIT. DOI=10.1006/jmbi.1999.2766; PubMed=10366508 [NCBI, ExPASy, EBI, Israel, Japan] Oubrie A., Rozeboom H.J., Kalk K.H., Duine J.A., Dijkstra B.W.; "The 1.7 A crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat."; J. Mol. Biol. 289:319-333(1999).
[3]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUCOSE; PQQ AND CALCIUM, AND SUBUNIT. DOI=10.1093/emboj/18.19.5187; PubMed=10508152 [NCBI, ExPASy, EBI, Israel, Japan] Oubrie A., Rozeboom H.J., Kalk K.H., Olsthoorn A.J.J., Duine J.A., Dijkstra B.W.; "Structure and mechanism of soluble quinoprotein glucose dehydrogenase."; EMBO J. 18:5187-5194(1999).

Comments

FUNCTION: Oxidizes glucose to gluconolactone.
CATALYTIC ACTIVITY: D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol.
COFACTOR: Binds 1 PQQ group per subunit.
COFACTOR: Binds 3 calcium ions per subunit.
SUBUNIT: Homodimer.
BIOTECHNOLOGY: Potent biocatalyst for the accurate in vivo monitoring of blood glucose in the management of diabetes.
MISCELLANEOUS: Acinetobacter calcoaceticus contains two different PQQ dependent enzymes with GDH activity. GDH-A prefers 2-deoxyglucose as substrate, the specific substrates for GDH-B are disaccharides.
SIMILARITY: Belongs to the PQQ oxidoreductase gdhB family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X15871; CAA33881.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S04784; S04784.

3D structure databases

PDB

1C9U; X-ray; 2.20 A; A/B=25-478.	[ExPASy / RCSB / EBI]
1CQ1; X-ray; 1.90 A; A/B=25-478.	[ExPASy / RCSB / EBI]
1CRU; X-ray; 1.50 A; A/B=25-478.	[ExPASy / RCSB / EBI]
1QBI; X-ray; 1.72 A; A/B=25-478.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1C9U; -.
1CQ1; -.
1CRU; -.
1QBI; -.

ModBase

P13650.

Ontologies

GO:0008876;	Molecular function: quinoprotein glucose dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR011042; 6-blade_b-propeller_TolB-like.
IPR012938; Glc_sorbosone_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.

Pfam

PF07995; GSDH; 1.
Pfam graphical view of domain structure.

Other

P13650; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Calcium; Metal-binding; Oxidoreductase; PQQ; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`
`CHAIN`	`25 478`	`454`	`Quinoprotein glucose dehydrogenase B.`	`PRO_0000025583`
`REGION`	`252 253`	`2`	`PQQ.`
`REGION`	`430 432`	`3`	`PQQ.`
`ACT_SITE`	`168 168`		`Proton acceptor.`
`METAL`	`271 271`		`Calcium 1 (via carbonyl oxygen).`
`METAL`	`272 272`		`Calcium 1 (via carbonyl oxygen).`
`METAL`	`277 277`		`Calcium 2.`
`METAL`	`287 287`		`Calcium 2 (via carbonyl oxygen).`
`METAL`	`293 293`		`Calcium 3 (via carbonyl oxygen).`
`METAL`	`295 295`		`Calcium 3 (via carbonyl oxygen).`
`METAL`	`297 297`		`Calcium 3.`
`METAL`	`333 333`		`Calcium 3.`
`BINDING`	`100 100`		`Glucose.`
`BINDING`	`167 167`		`Glucose.`
`BINDING`	`192 192`		`Glucose.`
`BINDING`	`252 252`		`Glucose.`
`BINDING`	`367 367`		`PQQ; via carbonyl oxygen.`
`BINDING`	`372 372`		`PQQ.`
`BINDING`	`401 401`		`PQQ.`
`HELIX`	`30 34`	`5`
`STRAND`	`43 47`	`5`
`STRAND`	`51 58`	`8`
`STRAND`	`64 68`	`5`
`TURN`	`69 71`	`3`
`STRAND`	`73 77`	`5`
`TURN`	`79 81`	`3`
`STRAND`	`84 89`	`6`
`STRAND`	`102 108`	`7`
`TURN`	`110 114`	`5`
`STRAND`	`117 125`	`9`
`STRAND`	`136 146`	`11`
`TURN`	`147 150`	`4`
`STRAND`	`151 162`	`12`
`STRAND`	`170 175`	`6`
`STRAND`	`181 185`	`5`
`TURN`	`188 191`	`4`
`HELIX`	`193 195`	`3`
`HELIX`	`208 212`	`5`
`STRAND`	`220 226`	`7`
`STRAND`	`238 241`	`4`
`STRAND`	`245 249`	`5`
`STRAND`	`252 259`	`8`
`STRAND`	`265 270`	`6`
`STRAND`	`272 274`	`3`
`STRAND`	`276 281`	`6`
`TURN`	`289 291`	`3`
`STRAND`	`293 297`	`5`
`HELIX`	`306 308`	`3`
`HELIX`	`333 335`	`3`
`STRAND`	`339 341`	`3`
`STRAND`	`345 348`	`4`
`HELIX`	`360 362`	`3`
`HELIX`	`366 369`	`4`
`STRAND`	`394 399`	`6`
`TURN`	`400 402`	`3`
`STRAND`	`405 410`	`6`
`STRAND`	`414 417`	`4`
`STRAND`	`422 425`	`4`
`STRAND`	`431 436`	`6`
`STRAND`	`438 441`	`4`
`STRAND`	`443 447`	`5`
`STRAND`	`456 458`	`3`
`STRAND`	`470 473`	`4`

Sequence information

Length: 478 AA [This is the length of the unprocessed precursor]

Molecular weight: 52773 Da [This is the MW of the unprocessed precursor]

CRC64: A32CF45F55078648 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNKHLLAKIA LLSAVQLVTL SAFADVPLTP SQFAKAKSEN FDKKVILSNL NKPHALLWGP 

        70         80         90        100        110        120 
DNQIWLTERA TGKILRVNPE SGSVKTVFQV PEIVNDADGQ NGLLGFAFHP DFKNNPYIYI 

       130        140        150        160        170        180 
SGTFKNPKST DKELPNQTII RRYTYNKSTD TLEKPVDLLA GLPSSKDHQS GRLVIGPDQK 

       190        200        210        220        230        240 
IYYTIGDQGR NQLAYLFLPN QAQHTPTQQE LNGKDYHTYM GKVLRLNLDG SIPKDNPSFN 

       250        260        270        280        290        300 
GVVSHIYTLG HRNPQGLAFT PNGKLLQSEQ GPNSDDEINL IVKGGNYGWP NVAGYKDDSG 

       310        320        330        340        350        360 
YAYANYSAAA NKSIKDLAQN GVKVAAGVPV TKESEWTGKN FVPPLKTLYT VQDTYNYNDP 

       370        380        390        400        410        420 
TCGEMTYICW PTVAPSSAYV YKGGKKAITG WENTLLVPSL KRGVIFRIKL DPTYSTTYDD 

       430        440        450        460        470 
AVPMFKSNNR YRDVIASPDG NVLYVLTDTA GNVQKDDGSV TNTLENPGSL IKFTYKAK

P13650 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools