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Reviewed, UniProtKB/Swiss-Prot P11410 (G6PD_PICJA)

Last modified November 25, 2008. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glucose-6-phosphate 1-dehydrogenase
      Short name=G6PD
    EC=1.1.1.49
OrganismPichia jadinii (Yeast) (Candida utilis)
Taxonomic identifier4903 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaePichia

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

D-glucose 6-phosphate + NADP(+) = D-glucono-1,5-lactone 6-phosphate + NADPH.

Pathway

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

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 processglucose metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

glucose-6-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495Glucose-6-phosphate 1-dehydrogenase
PRO_0000068105

Sites

Active site2411Proton acceptor By similarity
Binding site171NADP By similarity
Binding site491NADP By similarity
Binding site1791Substrate By similarity
Binding site1831Substrate By similarity

Amino acid modifications

Modified residue11N-acetylserine

Natural variations

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

Sequences

Sequence LengthMass (Da)Tools
P11410-1 [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: 8444164] [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: 2499329] [Abstract]
Cited for: PROTEIN SEQUENCE OF 177-187.
Strain: ATCC 9950 / CBS 5609 / DSM 2361 / IFO 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: 8706859] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10.

Cross-references

Sequence databases

PIRS11078.
S29381.

3D structure databases

HSSPHSSP built from PDB template 1QKI based on UniProtKB P11413.
ModBaseSearch...

Family and domain databases

InterProIPR001282. Glc-6-P_DHase.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR23429. G6PDH. 1 hit.
PfamPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFPIRSF000110. G6PD. 1 hit.
PRINTSPR00079. G6PDHDRGNASE.
ProDomPD001129. G6PD. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00871. zwf. 1 hit.
PROSITEPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG6PD_PICJA
AccessionPrimary (citable) accession number: P11410
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: April 1, 1993
Last modified: November 25, 2008
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents