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P11410 (G6PD_CYBJA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 93. 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
OrganismCyberlindnera jadinii (Torula yeast) (Pichia jadinii)
Taxonomic identifier4903 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeCyberlindnera

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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
   PTMAcetylation
   Technical termDirect protein sequencing
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 – 495495Glucose-6-phosphate 1-dehydrogenase HAMAP-Rule MF_00966
PRO_0000068105

Regions

Nucleotide binding15 – 228NADP By similarity
Region179 – 1835Substrate binding By similarity

Sites

Active site2411Proton acceptor By similarity
Binding site491NADP By similarity
Binding site1491NADP; via carbonyl oxygen By similarity
Binding site1491Substrate By similarity
Binding site2171Substrate By similarity
Binding site2361Substrate By similarity
Binding site3351Substrate By similarity
Binding site3691Substrate By similarity

Amino acid modifications

Modified residue11N-acetylserine HAMAP-Rule MF_00966

Natural variations

Natural variant1071H → G.
Natural variant1381P → M.
Natural variant4161I → T.

Sequences

Sequence LengthMass (Da)Tools
P11410 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: B6944216F4B4C8D8

FASTA49557,029
        10         20         30         40         50         60 
SYDSFGDRVT IIVFGASGDL ARKKTFPALF GLFREKQLPS TVQIIGYARS HLSDKDFKDY 

        70         80         90        100        110        120 
ISSHFKGGDD KTKEDFLNLC SYISDPYDTD EGYKKLEARC QEYESKHNVK VPERLFYLAL 

       130        140        150        160        170        180 
PPSVFHTVCE QVKKNVYPKN EKSRIIIEKP FGRDLETYRE LQKQISPLFT EDEVYRIDHY 

       190        200        210        220        230        240 
LGKEMVKNLL VLRFGNELFS GIWNNKHITS VQISFKEAFG TEGRGGYFDN IGIIRDVMQN 

       250        260        270        280        290        300 
HLLQVLTLLT MERPVSFDPE AVRDEKVKVL KAFDKIDVND VLLGQYGKSE DGTKPGYLDD 

       310        320        330        340        350        360 
STVKPNSKAV TYAAFRVNIH NERWDGVPIV LRAGKALDEG KAEIRIQFKP VAKGMFKEIQ 

       370        380        390        400        410        420 
RNELVIRIQP NEAIYLKINS KIPGISTETS LTDLDLTYST RYSKDFWIPE AYEALIRDCY 

       430        440        450        460        470        480 
LGNHSNFVRD DELEVSWKLF TPLLEAVEKE ENVKLESYPY GSKGPKELRK YLIDHGYVFN 

       490 
DPGTYQWPLT NTDVK 

« Hide

References

[1]"Glucose-6-phosphate dehydrogenase. Structure-function relationships and the Pichia jadinii enzyme structure."
Jeffery J., Persson B., Wood I., Bergman T., Jeffery R., Joernvall H.
Eur. J. Biochem. 212:41-49(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Glucose-6-phosphate dehydrogenase. Characterization of a reactive lysine residue in the Pichia jadinii enzyme reveals a limited structural variation in a functionally significant segment."
Jeffery J., Wood I., McLeod A., Jeffery R., Joernvall H.
Biochem. Biophys. Res. Commun. 160:1290-1295(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 177-187.
Strain: ATCC 9950 / CBS 5609 / DSM 2361 / NBRC 0998 / NRRL Y-900.
[3]"Alcoholytic deblocking of N-terminally acetylated peptides and proteins for sequence analysis."
Bergman T., Gheorghe M.T., Hjelmqvist L., Joernvall H.
FEBS Lett. 390:199-202(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10.

Cross-references

Sequence databases

PIRS11078.
S29381.

3D structure databases

ProteinModelPortalP11410.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_CYBJA
AccessionPrimary (citable) accession number: P11410
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: April 1, 1993
Last modified: February 19, 2014
This is version 93 of the entry and version 2 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