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P48826 (G6PD_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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:gsdA
Synonyms:g6pdh
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis By similarity. HAMAP-Rule MF_00966

Catalytic activity

D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH. HAMAP-Rule MF_00966

Pathway

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

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

glucose-6-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 510510Glucose-6-phosphate 1-dehydrogenase HAMAP-Rule MF_00966
PRO_0000068102

Regions

Nucleotide binding29 – 368NADP By similarity
Region194 – 1985Substrate binding By similarity

Sites

Active site2561Proton acceptor By similarity
Binding site631NADP By similarity
Binding site1641NADP; via carbonyl oxygen By similarity
Binding site1641Substrate By similarity
Binding site2321Substrate By similarity
Binding site2511Substrate By similarity
Binding site3501Substrate By similarity
Binding site3841Substrate By similarity

Experimental info

Sequence conflict1351L → F in CAA54840. Ref.2
Sequence conflict508 – 5103NRL → TVCK in CAA54840. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P48826 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: FDDF3F5025483AF6

FASTA51058,950
        10         20         30         40         50         60 
MASTIARTEE RQNAGTMELK DDTVIIVLGA SGDLAKKKTF PALFGLYRNK FLPKGIKIVG 

        70         80         90        100        110        120 
YARTNMDHEE YLRRVRSYIK TPTKEIEEQL DSFCQFCTYI SGQYDKDDSF INLNKHLEEI 

       130        140        150        160        170        180 
EKGQKEQNRI YYMALPPSVF TTVSDQLKRN CYPKNGVARI IVEKPFGKDL QSSRDLQKAL 

       190        200        210        220        230        240 
EPNWKEEEIF RIDHYLGKEM VKNILIMRFG NEFFNATWNR HHIDNVQITF KEPFGTEGRG 

       250        260        270        280        290        300 
GYFDEFGIIR DVMQNHLLQV LTLLAMERPI SFSAEDIRDE KVRVLRAMDA IEPKNVIIGQ 

       310        320        330        340        350        360 
YGKSLDGSKP AYKEDETVPQ DSRCPTFCAM VAYIKNERWD GVPFIMKAGK ALNEQKTEIR 

       370        380        390        400        410        420 
IQFRDVTSGI FKDIPRNELV IRVQPNESVY IKMNSKLPGL SMQTVVTELD LTYRRRFSDL 

       430        440        450        460        470        480 
KIPEAYESLI LDALKGDHSN FVRDDELDAS WRIFTPLLHY LDDNKEIIPM EYPYGSRGPA 

       490        500        510 
VLDDFTASFG YKFSDAAGYQ WPLTSTPNRL 

« Hide

References

[1]"G6PD-promoter activity in A. niger."
Thamm A.
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[2]"Isolation and characterization of the glucose-6-phosphate dehydrogenase encoding gene (gsdA) from Aspergillus niger."
van den Broek P., Goosen T., Wennekes B., van den Broek H.
Mol. Gen. Genet. 247:229-239(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X87942 mRNA. Translation: CAA61194.1.
X77829 Genomic DNA. Translation: CAA54840.1.
PIRS54720.

3D structure databases

ProteinModelPortalP48826.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP48826.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0364.

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_ASPNG
AccessionPrimary (citable) accession number: P48826
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways