ID G6PD_CYBJA Reviewed; 495 AA. AC P11410; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 2. DT 13-SEP-2023, entry version 112. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase; DE Short=G6PD; DE EC=1.1.1.49 {ECO:0000250|UniProtKB:P11413}; OS Cyberlindnera jadinii (Torula yeast) (Pichia jadinii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera. OX NCBI_TaxID=4903; RN [1] RP PROTEIN SEQUENCE. RX PubMed=8444164; DOI=10.1111/j.1432-1033.1993.tb17630.x; RA Jeffery J., Persson B., Wood I., Bergman T., Jeffery R., Joernvall H.; RT "Glucose-6-phosphate dehydrogenase. Structure-function relationships and RT the Pichia jadinii enzyme structure."; RL Eur. J. Biochem. 212:41-49(1993). RN [2] RP PROTEIN SEQUENCE OF 177-187. RC STRAIN=ATCC 9950 / CBS 5609 / DSM 2361 / NBRC 0998 / NRRL Y-900; RX PubMed=2499329; DOI=10.1016/s0006-291x(89)80143-3; RA Jeffery J., Wood I., McLeod A., Jeffery R., Joernvall H.; RT "Glucose-6-phosphate dehydrogenase. Characterization of a reactive lysine RT residue in the Pichia jadinii enzyme reveals a limited structural variation RT in a functionally significant segment."; RL Biochem. Biophys. Res. Commun. 160:1290-1295(1989). RN [3] RP PROTEIN SEQUENCE OF 1-10, AND ACETYLATION AT SER-1. RX PubMed=8706859; DOI=10.1016/0014-5793(96)00657-6; RA Bergman T., Gheorghe M.T., Hjelmqvist L., Joernvall H.; RT "Alcoholytic deblocking of N-terminally acetylated peptides and proteins RT for sequence analysis."; RL FEBS Lett. 390:199-202(1996). 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: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 PIR; S11078; S11078. DR PIR; S29381; S29381. DR AlphaFoldDB; P11410; -. DR SMR; P11410; -. DR iPTMnet; P11410; -. 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 1: Evidence at protein level; KW Acetylation; Carbohydrate metabolism; Direct protein sequencing; KW Glucose metabolism; NADP; Oxidoreductase. FT CHAIN 1..495 FT /note="Glucose-6-phosphate 1-dehydrogenase" FT /id="PRO_0000068105" FT ACT_SITE 241 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P11411" FT BINDING 15..22 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 49 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 149 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 149 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 179..183 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 217 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 236 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 335 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT BINDING 369 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11413" FT MOD_RES 1 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:8706859" FT VARIANT 107 FT /note="H -> G" FT VARIANT 138 FT /note="P -> M" FT VARIANT 416 FT /note="I -> T" SQ SEQUENCE 495 AA; 57029 MW; B6944216F4B4C8D8 CRC64; SYDSFGDRVT IIVFGASGDL ARKKTFPALF GLFREKQLPS TVQIIGYARS HLSDKDFKDY ISSHFKGGDD KTKEDFLNLC SYISDPYDTD EGYKKLEARC QEYESKHNVK VPERLFYLAL PPSVFHTVCE QVKKNVYPKN EKSRIIIEKP FGRDLETYRE LQKQISPLFT EDEVYRIDHY LGKEMVKNLL VLRFGNELFS GIWNNKHITS VQISFKEAFG TEGRGGYFDN IGIIRDVMQN HLLQVLTLLT MERPVSFDPE AVRDEKVKVL KAFDKIDVND VLLGQYGKSE DGTKPGYLDD STVKPNSKAV TYAAFRVNIH NERWDGVPIV LRAGKALDEG KAEIRIQFKP VAKGMFKEIQ RNELVIRIQP NEAIYLKINS KIPGISTETS LTDLDLTYST RYSKDFWIPE AYEALIRDCY LGNHSNFVRD DELEVSWKLF TPLLEAVEKE ENVKLESYPY GSKGPKELRK YLIDHGYVFN DPGTYQWPLT NTDVK //