ID G6PD_BUCBP Reviewed; 490 AA. AC Q89AI7; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 02-SEP-2026, entry version 126. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966}; DE Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966}; DE EC=1.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00966}; GN Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966}; OrderedLocusNames=bbp_298; OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Erwiniaceae; Buchnera. OX NCBI_TaxID=224915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bp; RX PubMed=12522265; DOI=10.1073/pnas.0235981100; RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.; RT "Reductive genome evolution in Buchnera aphidicola."; RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003). CC -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6- CC phosphogluconolactone. {ECO:0000255|HAMAP-Rule:MF_00966}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00966}; CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 1/3. {ECO:0000255|HAMAP-Rule:MF_00966}. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_00966}. 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; AE016826; AAO27023.1; -; Genomic_DNA. DR RefSeq; WP_011091424.1; NC_004545.1. DR AlphaFoldDB; Q89AI7; -. DR SMR; Q89AI7; -. DR STRING; 224915.bbp_298; -. DR KEGG; bab:bbp_298; -. DR eggNOG; COG0364; Bacteria. DR HOGENOM; CLU_013524_5_0_6; -. DR OrthoDB; 9802739at2; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000000601; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:TreeGrafter. DR FunFam; 3.40.50.720:FF:000079; 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 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 3: Inferred from homology; KW Carbohydrate metabolism; Glucose metabolism; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1..490 FT /note="Glucose-6-phosphate 1-dehydrogenase" FT /id="PRO_0000068114" FT ACT_SITE 237 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 48 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 90..91 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 145 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 175 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 179 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 213 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 232 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 340 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" FT BINDING 345 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00966" SQ SEQUENCE 490 AA; 57318 MW; F5EE7D9055965AD9 CRC64; MKNKNSGYDL VIFGAKGDLS CRKLLPSLYQ LEKKNKLCTH TRIIGVGRAN WDKIIYTNVV YKSLIKFLNE TIIESIWKKF SSRLEFCNLD INCLHNFKKL KQIIQQNNNI IINYLAMPPH TFGNICLGLE SINLNLEPTR IIIEKPLGSS LKTSININNK IGKFFKEKQI FRIDHYLGKE TIQNLLAFRF SNSLFYYNWN NKFIDHVQIT VSETIGVEGR FNYFDTVGQI KDMVQNHLLQ ILTITTMSTP IDCHENSIRD EKVKILKSLR PFNINNIHKN VILGQYTSGI INQKKVKSYL DETNNQEYQM NKYTETFVSM KIYIDNDQWS GVPFYLRTGK RLPKKCSEIV IFFKTPPLNI FSKNYNTLSK NKLILSLQPN EAIKIYILNK KPKLTSQYKL DLITLDFNYS KFYKKIQLSD AYEKLLLESM KGIQSLFVRR DEVELAWKWI DSTLQCLHLK PRLPDLYPAG TWGPARSKTM INNDGYEWNE //