ID G6PD_OSPRO Reviewed; 515 AA. AC Q29492; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 13-SEP-2023, entry version 108. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase; DE Short=G6PD; DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413}; GN Name=G6PD; OS Osphranter robustus (Wallaroo) (Macropus robustus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Metatheria; Diprotodontia; Macropodidae; Osphranter. OX NCBI_TaxID=9319; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=7749228; DOI=10.1007/bf00293013; RA Loebel D.A., Longhurst T.J., Johnston P.G.; RT "Full-length cDNA sequence of X-linked G6PD of an Australian marsupial, the RT wallaroo."; RL Mamm. Genome 6:198-201(1995). CC -!- FUNCTION: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes CC the first and rate-limiting step of the oxidative branch within the CC pentose phosphate pathway/shunt, an alternative route to glycolysis for CC the dissimilation of carbohydrates and a major source of reducing power CC and metabolic intermediates for fatty acid and nucleic acid CC biosynthetic processes. {ECO:0000250|UniProtKB:P11413}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5- CC lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:61548; EC=1.1.1.49; CC Evidence={ECO:0000250|UniProtKB:P11413}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842; CC Evidence={ECO:0000250|UniProtKB:P11413}; CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 1/3. {ECO:0000250|UniProtKB:P11413}. CC -!- SUBUNIT: Homotetramer; dimer of dimers. Interacts with SIRT2; the CC interaction is enhanced by H(2)O(2) treatment (By similarity). Forms a CC ternary complex with ALDOB and TP53; this interaction is direct. ALDOB CC stabilizes the complex inhibiting G6PD activity and keeping oxidative CC pentose phosphate metabolism in check. {ECO:0000250|UniProtKB:P11413}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P11413}. Membrane CC {ECO:0000250|UniProtKB:P11413}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P11413}. CC -!- PTM: Acetylated by ELP3 at Lys-403; acetylation inhibits its CC homodimerization and enzyme activity. Deacetylated by SIRT2 at Lys-403; CC deacetylation stimulates its enzyme activity (By similarity). CC {ECO:0000250|UniProtKB:P11413}. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U13899; AAA76599.1; -; mRNA. DR AlphaFoldDB; Q29492; -. DR SMR; Q29492; -. DR UniPathway; UPA00115; UER00408. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00966; G6PD; 1. DR InterPro; IPR001282; G6P_DH. DR InterPro; IPR019796; G6P_DH_AS. DR InterPro; IPR022675; G6P_DH_C. DR InterPro; IPR022674; G6P_DH_NAD-bd. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR00871; zwf; 1. DR PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1. DR PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1. DR Pfam; PF02781; G6PD_C; 1. DR Pfam; PF00479; G6PD_N; 1. DR PIRSF; PIRSF000110; G6PD; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. PE 2: Evidence at transcript level; KW Acetylation; Carbohydrate metabolism; Cytoplasm; Glucose metabolism; KW Hydroxylation; Membrane; NADP; Oxidoreductase; Phosphoprotein. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P11413" FT CHAIN 2..515 FT /note="Glucose-6-phosphate 1-dehydrogenase" FT /id="PRO_0000068084" FT ACT_SITE 263 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 38..45 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 72 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 147 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 171 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 171 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 201..205 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 239 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 258 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 357 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 360 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 365 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 366 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 370 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 393 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 395 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 401..403 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 421..423 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 487 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 503 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 509 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 8 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 10 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 89 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 171 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 171 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 403 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 432 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 497 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 503 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P11413" SQ SEQUENCE 515 AA; 59315 MW; D49BA95185A78952 CRC64; MAEQVALSRT QVCGILREEL YQGDAFHQSD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL LPEDTFIVGY ARSNLTVDDI RKQSEPYFKA TPEENLKLEE FFSRNSYVAG QYDEPASFQR LNAHMNSLHH GSQANRLFYL ALPPTVYEAV TKNIKETCMS QIGWNRVIVE KPFGKDLQSS DKLSNHISSL FHEDQIYRID HYLGKEMVQN LMVLRFGNRI FGPIWNRDNI ACVIFTFKEP FGTLGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPASTN SDDVRDEKVK VLKCISEVRA TDVVLGQYVG NPDGEGEATK GYLDDPTVPR GSTTATFAAV VLYVENERWD GVPFILRCGK ALNERKAEVR LQFRDVAGDI FQRQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL DLTYGNRYKD VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH HIEKEKTQPI AYVYGSRGPP EADELMKRVG FQYEGTYKWV NPHKL //