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Overview

Uniprot IDP11413
Protein NameGlucose-6-phosphate 1-dehydrogenase
Gene NameG6PD
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
171 WNRIIVEKPFGRDLQ
293 DEKVKVLKCISEVQA
386 DIFHQQCKRNELVIR
432 GNRYKNVKLPDAYER
476 LHQIELEKPKPIPYI
497 TEADELMKRVGFQYE
508 FQYEGTYKWVNPHKL
514 YKWVNPHKL******
82 LTVADIRKQSEPFFK
89 KQSEPFFKATPEEKL
95 FKATPEEKLKLEDFF
97 ATPEEKLKLEDFFAR

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. Also catalyzes the conversion of NAADPH, which is produced by enzymes such as DUOX1, DUOX2 and NOX5 from NAADP and promotes Ca(2+) signaling during T cell activation, back to NAADP (PubMed:34784249)

Protein Sequence

10 MAEQVALSRT 20 QVCGILREEL 30 FQGDAFHQSD 40 THIFIIMGAS 50 GDLAKKKIYP 60 TIWWLFRDGL 70 LPENTFIVGY 80 ARSRLTVADI 90 RKQSEPFFKA 100 TPEEKLKLED 110 FFARNSYVAG 120 QYDDAASYQR 130 LNSHMNALHL 140 GSQANRLFYL 150 ALPPTVYEAV 160 TKNIHESCMS 170 QIGWNRIIVE 180 KPFGRDLQSS 190 DRLSNHISSL 200 FREDQIYRID 210 HYLGKEMVQN 220 LMVLRFANRI 230 FGPIWNRDNI 240 ACVILTFKEP 250 FGTEGRGGYF 260 DEFGIIRDVM 270 QNHLLQMLCL 280 VAMEKPASTN 290 SDDVRDEKVK 300 VLKCISEVQA 310 NNVVLGQYVG 320 NPDGEGEATK 330 GYLDDPTVPR 340 GSTTATFAAV 350 VLYVENERWD 360 GVPFILRCGK 370 ALNERKAEVR 380 LQFHDVAGDI 390 FHQQCKRNEL 400 VIRVQPNEAV 410 YTKMMTKKPG 420 MFFNPEESEL 430 DLTYGNRYKN 440 VKLPDAYERL 450 ILDVFCGSQM 460 HFVRSDELRE 470 AWRIFTPLLH 480 QIELEKPKPI 490 PYIYGSRGPT 500 EADELMKRVG 510 FQYEGTYKWV NPHKL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0009898 cytoplasmic side of plasma membrane
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016020 membrane
Molecular Function GO:0005536 D-glucose binding
Molecular Function GO:0004345 glucose-6-phosphate dehydrogenase activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0050661 NADP binding
Molecular Function GO:0042803 protein homodimerization activity
Biological Process GO:0034599 cellular response to oxidative stress
Biological Process GO:0006695 cholesterol biosynthetic process
Biological Process GO:0043249 erythrocyte maturation
Biological Process GO:0051156 glucose 6-phosphate metabolic process
Biological Process GO:0006006 glucose metabolic process
Biological Process GO:0006749 glutathione metabolic process
Biological Process GO:0006629 lipid metabolic process
Biological Process GO:0006739 NADP+ metabolic process
Biological Process GO:0061052 negative regulation of cell growth involved in cardiac muscle cell development
Biological Process GO:2000378 negative regulation of reactive oxygen species metabolic process
Biological Process GO:0019322 pentose biosynthetic process
Biological Process GO:0006098 pentose-phosphate shunt
Biological Process GO:0009051 pentose-phosphate shunt, oxidative branch
Biological Process GO:1904879 positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel
Biological Process GO:0043523 regulation of neuron apoptotic process
Biological Process GO:0045471 response to ethanol
Biological Process GO:0032094 response to food
Biological Process GO:0010041 response to iron(III) ion
Biological Process GO:0046390 ribose phosphate biosynthetic process
Biological Process GO:0021762 substantia nigra development

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.