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Protein

Quinoprotein glucose dehydrogenase B

Gene

gdhB

Organism
Acinetobacter calcoaceticus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Oxidizes glucose to gluconolactone.

Catalytic activityi

D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei100Glucose1 Publication1
Binding sitei167Glucose1 Publication1
Active sitei168Proton acceptor1
Binding sitei192Glucose1 Publication1
Binding sitei252Glucose1 Publication1
Metal bindingi271Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi272Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi277Calcium 21 Publication1
Metal bindingi287Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi293Calcium 3; via carbonyl oxygen1 Publication1
Metal bindingi295Calcium 3; via carbonyl oxygen1 Publication1
Metal bindingi297Calcium 31 Publication1
Metal bindingi333Calcium 31 Publication1
Binding sitei367PQQ; via carbonyl oxygen1 Publication1
Binding sitei372PQQ1 Publication1
Binding sitei401PQQ1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Metal-binding, PQQ

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15518.
BRENDAi1.1.5.2. 99.
1.1.99.35. 99.

Names & Taxonomyi

Protein namesi
Recommended name:
Quinoprotein glucose dehydrogenase B (EC:1.1.5.2)
Alternative name(s):
Glucose dehydrogenase B [pyrroloquinoline-quinone]
Soluble glucose dehydrogenase
Short name:
s-GDH
Gene namesi
Name:gdhB
OrganismiAcinetobacter calcoaceticus
Taxonomic identifieri471 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Pathology & Biotechi

Biotechnological usei

Potent biocatalyst for the accurate in vivo monitoring of blood glucose in the management of diabetes.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Add BLAST24
ChainiPRO_000002558325 – 478Quinoprotein glucose dehydrogenase BAdd BLAST454

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi871585.BDGL_001432.

Structurei

Secondary structure

1478
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 34Combined sources5
Beta strandi41 – 47Combined sources7
Beta strandi51 – 58Combined sources8
Beta strandi64 – 68Combined sources5
Turni69 – 71Combined sources3
Beta strandi73 – 77Combined sources5
Turni79 – 81Combined sources3
Beta strandi84 – 89Combined sources6
Beta strandi102 – 108Combined sources7
Turni110 – 114Combined sources5
Beta strandi117 – 125Combined sources9
Beta strandi131 – 133Combined sources3
Beta strandi136 – 146Combined sources11
Turni147 – 150Combined sources4
Beta strandi151 – 162Combined sources12
Beta strandi170 – 175Combined sources6
Beta strandi181 – 185Combined sources5
Turni188 – 191Combined sources4
Helixi193 – 195Combined sources3
Helixi208 – 212Combined sources5
Beta strandi220 – 226Combined sources7
Beta strandi238 – 241Combined sources4
Beta strandi245 – 249Combined sources5
Beta strandi252 – 259Combined sources8
Beta strandi265 – 270Combined sources6
Beta strandi272 – 274Combined sources3
Beta strandi276 – 280Combined sources5
Turni289 – 291Combined sources3
Beta strandi293 – 297Combined sources5
Helixi306 – 308Combined sources3
Helixi333 – 335Combined sources3
Beta strandi339 – 341Combined sources3
Beta strandi345 – 348Combined sources4
Helixi360 – 362Combined sources3
Helixi366 – 369Combined sources4
Beta strandi394 – 402Combined sources9
Beta strandi405 – 410Combined sources6
Beta strandi414 – 425Combined sources12
Beta strandi431 – 436Combined sources6
Beta strandi438 – 441Combined sources4
Beta strandi443 – 447Combined sources5
Beta strandi456 – 458Combined sources3
Beta strandi470 – 475Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C9UX-ray2.20A/B25-478[»]
1CQ1X-ray1.90A/B25-478[»]
1CRUX-ray1.50A/B25-478[»]
1QBIX-ray1.72A/B25-478[»]
ProteinModelPortaliP13650.
SMRiP13650.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13650.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni252 – 253PQQ2
Regioni430 – 432PQQ3

Sequence similaritiesi

Belongs to the PQQ oxidoreductase GdhB family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105D8V. Bacteria.
COG2133. LUCA.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR012938. Glc/Sorbosone_DH.
IPR019893. PQQ-dependent_DH_s-GDH.
IPR011041. Quinoprot_gluc/sorb_DH.
[Graphical view]
PfamiPF07995. GSDH. 2 hits.
[Graphical view]
SUPFAMiSSF50952. SSF50952. 1 hit.
TIGRFAMsiTIGR03606. non_repeat_PQQ. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13650-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKHLLAKIA LLSAVQLVTL SAFADVPLTP SQFAKAKSEN FDKKVILSNL
60 70 80 90 100
NKPHALLWGP DNQIWLTERA TGKILRVNPE SGSVKTVFQV PEIVNDADGQ
110 120 130 140 150
NGLLGFAFHP DFKNNPYIYI SGTFKNPKST DKELPNQTII RRYTYNKSTD
160 170 180 190 200
TLEKPVDLLA GLPSSKDHQS GRLVIGPDQK IYYTIGDQGR NQLAYLFLPN
210 220 230 240 250
QAQHTPTQQE LNGKDYHTYM GKVLRLNLDG SIPKDNPSFN GVVSHIYTLG
260 270 280 290 300
HRNPQGLAFT PNGKLLQSEQ GPNSDDEINL IVKGGNYGWP NVAGYKDDSG
310 320 330 340 350
YAYANYSAAA NKSIKDLAQN GVKVAAGVPV TKESEWTGKN FVPPLKTLYT
360 370 380 390 400
VQDTYNYNDP TCGEMTYICW PTVAPSSAYV YKGGKKAITG WENTLLVPSL
410 420 430 440 450
KRGVIFRIKL DPTYSTTYDD AVPMFKSNNR YRDVIASPDG NVLYVLTDTA
460 470
GNVQKDDGSV TNTLENPGSL IKFTYKAK
Length:478
Mass (Da):52,773
Last modified:January 1, 1990 - v1
Checksum:iA32CF45F55078648
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15871 Genomic DNA. Translation: CAA33881.1.
PIRiS04784.
RefSeqiWP_002121021.1. NZ_JQLC01000017.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15871 Genomic DNA. Translation: CAA33881.1.
PIRiS04784.
RefSeqiWP_002121021.1. NZ_JQLC01000017.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C9UX-ray2.20A/B25-478[»]
1CQ1X-ray1.90A/B25-478[»]
1CRUX-ray1.50A/B25-478[»]
1QBIX-ray1.72A/B25-478[»]
ProteinModelPortaliP13650.
SMRiP13650.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi871585.BDGL_001432.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105D8V. Bacteria.
COG2133. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15518.
BRENDAi1.1.5.2. 99.
1.1.99.35. 99.

Miscellaneous databases

EvolutionaryTraceiP13650.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR012938. Glc/Sorbosone_DH.
IPR019893. PQQ-dependent_DH_s-GDH.
IPR011041. Quinoprot_gluc/sorb_DH.
[Graphical view]
PfamiPF07995. GSDH. 2 hits.
[Graphical view]
SUPFAMiSSF50952. SSF50952. 1 hit.
TIGRFAMsiTIGR03606. non_repeat_PQQ. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDHGB_ACICA
AccessioniPrimary (citable) accession number: P13650
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 2, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.