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O55044 (G6PD_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 89. 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:G6PD
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Subunit structure

Homotetramer; dimer of dimers By similarity. HAMAP-Rule MF_00966

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 515514Glucose-6-phosphate 1-dehydrogenase HAMAP-Rule MF_00966
PRO_0000068081

Regions

Nucleotide binding38 – 458NADP 1 By similarity
Nucleotide binding401 – 4033NADP 2 By similarity
Nucleotide binding421 – 4233NADP 2 By similarity
Region201 – 2055Substrate binding By similarity

Sites

Active site2631Proton acceptor By similarity
Binding site721NADP 1 By similarity
Binding site1471NADP 1 By similarity
Binding site1711NADP 1; via carbonyl oxygen By similarity
Binding site1711Substrate By similarity
Binding site2391Substrate By similarity
Binding site2581Substrate By similarity
Binding site3571NADP 2 By similarity
Binding site3601Substrate By similarity
Binding site3651Substrate By similarity
Binding site3661NADP 2 By similarity
Binding site3701NADP 2 By similarity
Binding site3931NADP 2 By similarity
Binding site3951Substrate By similarity
Binding site4871NADP 2 By similarity
Binding site5031NADP 2 By similarity
Binding site5091NADP 2 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue891N6-acetyllysine By similarity
Modified residue1711N6-acetyllysine By similarity
Modified residue4031N6-acetyllysine By similarity
Modified residue4321N6-acetyllysine By similarity
Modified residue4971N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O55044 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 892DD70C86C7438C

FASTA51559,326
        10         20         30         40         50         60 
MAEQVALSRT QVCGILREEL YQGDAFHQAD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL 

        70         80         90        100        110        120 
LPEDTFIVGY ARSRLTVDDI RKQSEPFFKA TPEERPKLEE FFARNSYVAG QYDDPASYKH 

       130        140        150        160        170        180 
LNSHMNALHQ GMQANRLFYL ALPPTVYEAV TKNIQETCMS QTGWNRIIVE KPFGRDLQSS 

       190        200        210        220        230        240 
NQLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP 

       250        260        270        280        290        300 
FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPASTD SDDVRDEKVK VLKCISEVET 

       310        320        330        340        350        360 
SNVVLGQYVG NPNGEGEATN GYLDDPTVPR GSTTATFAAA VLYVENERWD GVPFILRCGK 

       370        380        390        400        410        420 
ALNERKAEVR LQFRDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL 

       430        440        450        460        470        480 
DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH KIDQEKPQPI 

       490        500        510 
PYVYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL 

« Hide

References

[1]"cDNA sequence of Chinese hamster glucose-6-phosphate Dehydrogenase."
Perez M.L., Stamato T.D.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF044676 mRNA. Translation: AAC00204.1.
RefSeqNP_001233656.1. NM_001246727.1.

3D structure databases

ProteinModelPortalO55044.
SMRO55044. Positions 28-515.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689469.
KEGGcge:100689469.

Phylogenomic databases

HOVERGENHBG000856.
KOK00036.

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_CRIGR
AccessionPrimary (citable) accession number: O55044
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways