ID G6PD_TAKRU Reviewed; 530 AA. AC P54996; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 04-NOV-2026, entry version 120. 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 Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7607684; DOI=10.1016/0888-7543(95)80179-p; RA Mason P.J., Stevens D.J., Luzzatto L., Brenner S., Aparicio S.; RT "Genomic structure and sequence of the Fugu rubripes glucose-6-phosphate RT dehydrogenase gene (G6PD)."; RL Genomics 26:587-591(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 + NADPH + H(+); 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol 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; X83611; CAA58590.2; -; Genomic_DNA. DR PIR; A56841; A56841. DR SMR; P54996; -. DR STRING; 31033.ENSTRUP00000055877; -. DR InParanoid; P54996; -. DR OMA; AACLQYM; -. DR UniPathway; UPA00115; UER00408. DR FunFam; 3.30.360.10:FF:000013; Glucose-6-phosphate 1-dehydrogenase; 1. DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1. 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 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 NCBIfam; TIGR00871; zwf; 1. DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. DR GO; GO:0005829; C:cytosol; 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:InterPro. DR GO; GO:0006739; P:NADP+ metabolic process; ISS:UniProtKB. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:TreeGrafter. DR Proteomes; UP000005226; Unplaced. DR AlphaFoldDB; P54996; -. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1..530 FT /note="Glucose-6-phosphate 1-dehydrogenase" FT /id="PRO_0000068088" FT ACT_SITE 278 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P11411" FT BINDING 53..60 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 87 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 162 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 186 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 186 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 216..220 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 254 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 273 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 372 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 375 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 380 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 381 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 385 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 408 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 410 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 416..418 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 436..438 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 502 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 518 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 524 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11413" SQ SEQUENCE 530 AA; 60469 MW; FC73FB53D834EF29 CRC64; MMIILFNCFF CASFREDGQH PTVSLGGVWG AAKELHEDKE FHQSDVHVFI IMGASGDLAK KKIYPTLWWL FRDGLLPEQT YFVGFARSAL TVDAIRTSCM PYLKVTETES DRLSAFFSRN SYISGNYTAG GSFSELNAHI MSLPGASDAN RLFYLALPPT IYHSVTENIK HFCMSAKGWN RVIVEKPFGH DLQSSEELST HLSSLFTEDQ IYRIDHYLGK EMVQNLMVLR FGNRIFGPIW NRDNVACVVL TFKEPFGTQG RGGYFDDFGI IRDVMQNHML QMLCLVAMEK PASTNSDDVR DEKVKVLKCI VPASMSDVVL GQYVGDPEGE GDAKLGYLDD PTVPKGSTQA TFATVVLYVH NERWDGVPFI LRCGKALNER KAEVRLQFTD VPGDIFRNQC YRNELVVRVQ PNEAIYAKMM SKKPGVYFTP EETELDLTYK SRYKDVKLPD AYERLILDVF CGSQMHFVAS DELREAWRIF TPLLHQIEKE KPKPIPYKYG SRGPAEADEL EKRVGFRYEG TYKWVNPHRL //