ID G6PD_MEDSA Reviewed; 515 AA. AC Q42919; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-SEP-2023, entry version 105. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform; DE Short=G6PD; DE EC=1.1.1.49 {ECO:0000250|UniProtKB:Q9LK23}; OS Medicago sativa (Alfalfa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago. OX NCBI_TaxID=3879; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Apollo; RX PubMed=7640360; DOI=10.1007/bf00042073; RA Fahrendorf T., Ni W., Shorrosh B.S., Dixon R.A.; RT "Stress responses in alfalfa (Medicago sativa L.) XIX. Transcriptional RT activation of oxidative pentose phosphate pathway genes at the onset of the RT isoflavonoid phytoalexin response."; RL Plant Mol. Biol. 28:885-900(1995). CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose- CC phosphate pathway, which represents a route for the dissimilation of CC carbohydrates besides glycolysis. The main function of this enzyme is CC to provide reducing power (NADPH) and pentose phosphates for fatty acid CC and nucleic acid synthesis (By similarity). CC {ECO:0000250|UniProtKB:Q9LK23}. 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:Q9LK23}; CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 1/3. {ECO:0000305}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11411}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q9LK23}. 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; U18238; AAB41552.1; -; mRNA. DR PIR; S57785; S57785. DR AlphaFoldDB; Q42919; -. DR SMR; Q42919; -. DR UniPathway; UPA00115; UER00408. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:UniProt. 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 Carbohydrate metabolism; Cytoplasm; Glucose metabolism; NADP; KW Oxidoreductase. FT CHAIN 1..515 FT /note="Glucose-6-phosphate 1-dehydrogenase, cytoplasmic FT isoform" FT /id="PRO_0000068100" FT ACT_SITE 274 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P11411" FT BINDING 36..43 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 71 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 155 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 182 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 182 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 212..216 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 250 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 269 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 360 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 365 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 396 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" SQ SEQUENCE 515 AA; 58923 MW; 836C1B96F2709FC7 CRC64; MGTNEWHVER RDSIGTESPV AREVLETGTL SIVVLGASGD LAKKKTFPAL FHLYKQELLP PDEVHIFGYA RSKISDDELR NKLRSYLVPE KGASPKQLDD VSKFLQLVKY VSGPYDSEDG FRLLDKEISE HEYLKNSKEG SSRRLFYLAL PPSVYPSVCK MIKTCCMNKS DLGGWTRVVV EKPFGRDLES AEELSTQIGE LFEEPQIYRI DHYLGKELVQ NMLVLRFANR FFLPLWNHNH IDNVQIVFRE DFGTDGRGGY FDQYGIIRDI IPNHLLQVLC LIAMEKPVSL KPEHIRDEKV KVLESVLPIR DDEVVLGQYE GYTDDPTVPD DSNTPTFATT ILRIHNERWE GVPFIVKAGK ALNSRKAEIR VQFKDVPGDI FRSKKQGRNE FVIRLQPSEA IYMKLTVKQP GLEMSAVQSE LDLSYGQRYQ GITIPEAYER LILDTIRGDQ QHFVRRDELK ASWQIFTPLL HKIDRGELKP VPYNPGSRGP AEADELLEKA GYVQTPGYIW IPPTL //