ID G6PD_ASPNG Reviewed; 510 AA. AC P48826; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase; DE Short=G6PD; DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413}; GN Name=gsdA; Synonyms=g6pdh; OS Aspergillus niger. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=5061; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732; RA Thamm A.; RT "G6PD-promoter activity in A. niger."; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732; RX PubMed=7753033; DOI=10.1007/bf00705654; RA van den Broek P., Goosen T., Wennekes B., van den Broek H.; RT "Isolation and characterization of the glucose-6-phosphate dehydrogenase RT encoding gene (gsdA) from Aspergillus niger."; RL Mol. Gen. Genet. 247:229-239(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: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 -!- 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 -!- 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; X87942; CAA61194.1; -; mRNA. DR EMBL; X77829; CAA54840.1; -; Genomic_DNA. DR PIR; S54720; S54720. DR RefSeq; XP_001400342.1; XM_001400305.2. DR AlphaFoldDB; P48826; -. DR SMR; P48826; -. DR PaxDb; 5061-CADANGAP00002664; -. DR EnsemblFungi; CAK37895; CAK37895; An02g12140. DR GeneID; 4979751; -. DR VEuPathDB; FungiDB:An02g12140; -. DR VEuPathDB; FungiDB:ASPNIDRAFT2_1145051; -. DR VEuPathDB; FungiDB:ATCC64974_53050; -. DR VEuPathDB; FungiDB:M747DRAFT_293654; -. DR eggNOG; KOG0563; Eukaryota. DR OrthoDB; 989808at2759; -. DR UniPathway; UPA00115; UER00408. 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: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 Carbohydrate metabolism; Glucose metabolism; NADP; Oxidoreductase. FT CHAIN 1..510 FT /note="Glucose-6-phosphate 1-dehydrogenase" FT /id="PRO_0000068102" FT ACT_SITE 256 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P11411" FT BINDING 29..36 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 63 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 164 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 164 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 194..198 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 232 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 251 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 350 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 384 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT CONFLICT 135 FT /note="L -> F (in Ref. 2; CAA54840)" FT /evidence="ECO:0000305" FT CONFLICT 508..510 FT /note="NRL -> TVCK (in Ref. 2; CAA54840)" FT /evidence="ECO:0000305" SQ SEQUENCE 510 AA; 58950 MW; FDDF3F5025483AF6 CRC64; MASTIARTEE RQNAGTMELK DDTVIIVLGA SGDLAKKKTF PALFGLYRNK FLPKGIKIVG YARTNMDHEE YLRRVRSYIK TPTKEIEEQL DSFCQFCTYI SGQYDKDDSF INLNKHLEEI EKGQKEQNRI YYMALPPSVF TTVSDQLKRN CYPKNGVARI IVEKPFGKDL QSSRDLQKAL EPNWKEEEIF RIDHYLGKEM VKNILIMRFG NEFFNATWNR HHIDNVQITF KEPFGTEGRG GYFDEFGIIR DVMQNHLLQV LTLLAMERPI SFSAEDIRDE KVRVLRAMDA IEPKNVIIGQ YGKSLDGSKP AYKEDETVPQ DSRCPTFCAM VAYIKNERWD GVPFIMKAGK ALNEQKTEIR IQFRDVTSGI FKDIPRNELV IRVQPNESVY IKMNSKLPGL SMQTVVTELD LTYRRRFSDL KIPEAYESLI LDALKGDHSN FVRDDELDAS WRIFTPLLHY LDDNKEIIPM EYPYGSRGPA VLDDFTASFG YKFSDAAGYQ WPLTSTPNRL //