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O68282 (G6PD_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-6-phosphate 1-dehydrogenase

Short name=G6PD
EC=1.1.1.49
Gene names
Name:zwf
Ordered Locus Names:PA3183
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone. Can utilize either NADP+ or NAD+. Ref.1

Catalytic activity

D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH. Ref.1

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. HAMAP-Rule MF_00966

Subunit structure

Homotetramer Probable. Ref.1

Induction

Transcription is maximal during early logarithmic phase when inducing substrates such as glycerol, glucose or gluconate are abundant. Transcription decreases during stationary phase. Ref.1

Disruption phenotype

Mutant is unable to grow on minimal medium supplemented with mannitol and shows increased sensitivity to the redox-active superoxide-generating agent methyl viologen (paraquat). Ref.1

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=530 µM for glucose 6-phosphate (with NADP) Ref.1

KM=57 µM for NADP

KM=333 µM for NAD

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glucose-6-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 489489Glucose-6-phosphate 1-dehydrogenase HAMAP-Rule MF_00966
PRO_0000068131

Regions

Nucleotide binding92 – 932NADP By similarity

Sites

Active site2371Proton acceptor By similarity
Binding site491NADP By similarity
Binding site1451NADP By similarity
Binding site1751Substrate By similarity
Binding site1791Substrate By similarity
Binding site2131Substrate By similarity
Binding site2321Substrate By similarity
Binding site3371Substrate By similarity
Binding site3421Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O68282 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 755849EB33BF9486

FASTA48955,620
        10         20         30         40         50         60 
MPDVRVLPCT LALFGALGDL ALRKLFPALY QLDRENLLHR DTRVLALARD EGAPAEHLAT 

        70         80         90        100        110        120 
LEQRLRLAVP AKEWDDVVWQ RFRERLDYLS MDFLDPQAYV GLREAVDDEL PLVAYFATPA 

       130        140        150        160        170        180 
SVFGGICENL AAAGLAERTR VVLEKPIGHD LESSREVNEA VARFFPESRI YRIDHYLGKE 

       190        200        210        220        230        240 
TVQNLIALRF ANSLFETQWN QNHISHVEIT VAEKVGIEGR WGYFDQAGQL RDMVQNHLLQ 

       250        260        270        280        290        300 
LLCLIAMDPP SDLSADSIRD EKVKVLRALE PIPAEQLASR VVRGQYTAGF SDGKAVPGYL 

       310        320        330        340        350        360 
EEEHANRDSD AETFVALRVD IRNWRWSGVP FYLRTGKRMP QKLSQIVIHF KEPPHYIFAP 

       370        380        390        400        410        420 
EQRSLISNRL IIRLQPDEGI SLQVMTKDQG LGKGMQLRTG PLQLSFSETY HAARIPDAYE 

       430        440        450        460        470        480 
RLLLEVTQGN QYLFVRKDEV EFAWKWCDQL IAGWERLSEA PKPYPAGSWG PVASVALVAR 


DGRSWYGDF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the Pseudomonas aeruginosa zwf gene encoding glucose-6-phosphate dehydrogenase, an enzyme important in resistance to methyl viologen (paraquat)."
Ma J.-F., Hager P.W., Howell M.L., Phibbs P.V. Jr., Hassett D.J.
J. Bacteriol. 180:1741-1749(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, DISRUPTION PHENOTYPE.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF029673 Genomic DNA. Translation: AAC38311.1.
AE004091 Genomic DNA. Translation: AAG06571.1.
PIRA83248.
RefSeqNP_251873.1. NC_002516.2.

3D structure databases

ProteinModelPortalO68282.
SMRO68282. Positions 11-478.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA3183.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG06571; AAG06571; PA3183.
GeneID882681.
KEGGpae:PA3183.
PATRIC19840933. VBIPseAer58763_3327.

Organism-specific databases

PseudoCAPPA3183.

Phylogenomic databases

eggNOGCOG0364.
HOGENOMHOG000046191.
KOK00036.
OMADSIMEAW.
OrthoDBEOG61308Z.
PhylomeDBO68282.

Enzyme and pathway databases

UniPathwayUPA00115; UER00408.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00966. G6PD.
InterProIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23429. PTHR23429. 1 hit.
PfamPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFPIRSF000110. G6PD. 1 hit.
PRINTSPR00079. G6PDHDRGNASE.
TIGRFAMsTIGR00871. zwf. 1 hit.
PROSITEPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG6PD_PSEAE
AccessionPrimary (citable) accession number: O68282
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways