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Protein

Glucose-6-phosphate 1-dehydrogenase 2

Gene

G6pd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Miscellaneous

Has NADP both as cofactor (bound to the N-terminal domain) and as structural element bound to the C-terminal domain.

Catalytic activityi

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

Pathwayi: pentose phosphate pathway

This protein is involved in step 1 of the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glucose-6-phosphate 1-dehydrogenase (G6pd2), Glucose-6-phosphate 1-dehydrogenase X (G6pdx), Glucose-6-phosphate 1-dehydrogenase (G6pdx), Glucose-6-phosphate 1-dehydrogenase 2 (G6pd2), Glucose-6-phosphate 1-dehydrogenase (G6pdx), Glucose-6-phosphate 1-dehydrogenase (G6pd2), Glucose-6-phosphate 1-dehydrogenase (G6pdx)
  2. 6-phosphogluconolactonase (Pgls)
  3. 6-phosphogluconate dehydrogenase, decarboxylating (Pgd), 6-phosphogluconate dehydrogenase, decarboxylating (Pgd), 6-phosphogluconate dehydrogenase, decarboxylating (Pgd), 6-phosphogluconate dehydrogenase, decarboxylating (Pgd)
This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei72NADP 1By similarity1
Binding sitei147NADP 1By similarity1
Binding sitei171NADP 1; via carbonyl oxygenBy similarity1
Binding sitei171SubstrateBy similarity1
Binding sitei239SubstrateBy similarity1
Binding sitei258SubstrateBy similarity1
Active sitei263Proton acceptorBy similarity1
Binding sitei357NADP 2By similarity1
Binding sitei360SubstrateBy similarity1
Binding sitei365SubstrateBy similarity1
Binding sitei366NADP 2By similarity1
Binding sitei370NADP 2By similarity1
Binding sitei393NADP 2By similarity1
Binding sitei395SubstrateBy similarity1
Binding sitei487NADP 2By similarity1
Binding sitei503NADP 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi38 – 45NADP 1By similarity8
Nucleotide bindingi401 – 403NADP 2By similarity3
Nucleotide bindingi421 – 423NADP 2By similarity3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processCarbohydrate metabolism, Glucose metabolism
LigandNADP

Enzyme and pathway databases

UniPathwayiUPA00115; UER00408.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphate 1-dehydrogenase 2 (EC:1.1.1.49)
Short name:
G6PD
Gene namesi
Name:G6pd2
Synonyms:G6pd-2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:105977. G6pd2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000680861 – 513Glucose-6-phosphate 1-dehydrogenase 2Add BLAST513

Post-translational modificationi

Acetylated by ELP3; acetylation inhibits its homodimerization and enzyme activity. Deacetylated by SIRT2; deacetylation stimulates its enzyme activity (By similarity).By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP97324.
PaxDbiP97324.
PeptideAtlasiP97324.
PRIDEiP97324.

PTM databases

iPTMnetiP97324.
PhosphoSitePlusiP97324.

Expressioni

Tissue specificityi

Testis.1 Publication

Gene expression databases

CleanExiMM_G6PD2.

Interactioni

Subunit structurei

Interacts with SIRT2; the interaction is enhanced by H2O2 treatment (By similarity). Homotetramer; dimer of dimers.By similarity1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000131163.

Structurei

3D structure databases

ProteinModelPortaliP97324.
SMRiP97324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni201 – 205Substrate bindingBy similarity5

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0563. Eukaryota.
COG0364. LUCA.
HOGENOMiHOG000046192.
HOVERGENiHBG000856.
InParanoidiP97324.
KOiK00036.

Family and domain databases

HAMAPiMF_00966. G6PD. 1 hit.
InterProiView protein in InterPro
IPR001282. G6P_DH.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR036291. NAD(P)-bd_dom_sf.
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiView protein in Pfam
PF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
PIRSFiPIRSF000110. G6PD. 1 hit.
PRINTSiPR00079. G6PDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00871. zwf. 1 hit.

Sequencei

Sequence statusi: Complete.

P97324-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEQVTLSRT QVCGILREEL YQNDAFHQAD THIFIIMGAS GDLAKKKIYP
60 70 80 90 100
TIWWLFRDGL LPKETFIVGY ARSQLTVDDI QKQSEPFFKA TPEERPKLEE
110 120 130 140 150
FFTRNSYVVG QYDDPASYKH LNSYINALHQ GMQANHLFYL ALPPTVYEAV
160 170 180 190 200
TKNIQETCMS QTGFNRIIVE KPFGRDLQSS NQLSNHISSL FREDQIYRID
210 220 230 240 250
HYLDKEMVQN LMVLRFANRI FGPIWNGDNI VCVILTFKEP FGTEGRGGYF
260 270 280 290 300
DEFGIIRDVM QSHLLQMLCL VAMEKPATTD SDDVRNEKVK VLKCISEVET
310 320 330 340 350
DNVILGQYVG NPNGEGEAAN GYLDDPTVPR GSTTATFAAA VLYVKNERWD
360 370 380 390 400
GVPFILRCGK ALNERKAEVR LQFRDIPGDI FHQKCKRNEL VIRMQPNEAV
410 420 430 440 450
YTTMMTKKPG MFFNPEESEL DLTYGNKYKN VKLPGAYERL ILDVFCGCQM
460 470 480 490 500
HFVRTDELRE GWRIFTPLLH KIEREKPQPF PYVYGSRGPT EADELMRRVG
510
FQYKGTYKGT HKH
Length:513
Mass (Da):59,126
Last modified:January 23, 2007 - v3
Checksum:i655830EB767B6C53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z84471 Genomic DNA. Translation: CAB06476.1.
BC120827 mRNA. Translation: AAI20828.1.
BC137684 mRNA. Translation: AAI37685.1.
CCDSiCCDS19297.1.
RefSeqiNP_062341.2. NM_019468.2.
UniGeneiMm.347430.

Genome annotation databases

GeneIDi14380.
KEGGimmu:14380.

Similar proteinsi

Entry informationi

Entry nameiG6PD2_MOUSE
AccessioniPrimary (citable) accession number: P97324
Secondary accession number(s): Q0VB18
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 142 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families