ID G6PD2_MOUSE Reviewed; 513 AA. AC P97324; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 25-NOV-2008, entry version 76. DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase 2; DE Short=G6PD; DE EC=1.1.1.49; GN Name=G6pd2; Synonyms=G6pd-2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Swiss; RX MEDLINE=97312691; PubMed=9169132; DOI=10.1006/geno.1997.4673; RA Hendriksen P.J.M., Hoogerbrugge J.W., Baarends W.M., de Boer P., RA Vreeburg J.T.M., Vos E.A., van der Lende T., Grootegoed A.J.; RT "Testis-specific expression of a functional retroposon encoding RT glucose-6-phosphate dehydrogenase in the mouse."; RL Genomics 41:350-359(1997). CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = D-glucono- CC 1,5-lactone 6-phosphate + NADPH. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 1/3. CC -!- SUBUNIT: Homotetramer. CC -!- TISSUE SPECIFICITY: Testis. CC -!- MISCELLANEOUS: Has NADP both as cofactor (bound to the N-terminal CC domain) and as structural element bound to the C-terminal domain. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z84471; CAB06476.1; -; Genomic_DNA. DR RefSeq; NP_062341.1; -. DR UniGene; Mm.347430; -. DR HSSP; P11413; 1QKI. DR SMR; P97324; 28-513. DR PhosphoSite; P97324; -. DR Ensembl; ENSMUSG00000031400; Mus musculus. DR GeneID; 14380; -. DR KEGG; mmu:14380; -. DR MGI; MGI:105977; G6pd2. DR HOGENOM; P97324; -. DR HOVERGEN; P97324; -. DR NextBio; 285889; -. DR ArrayExpress; P97324; -. DR CleanEx; MM_G6PD2; -. DR GermOnline; ENSMUSG00000045120; Mus musculus. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001282; Glc-6-P_DHase. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR23429; G6PDH; 1. DR Pfam; PF02781; G6PD_C; 1. DR Pfam; PF00479; G6PD_N; 1. DR PIRSF; PIRSF000110; G6PD; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR ProDom; PD001129; G6PD; 1. DR TIGRFAMs; TIGR00871; zwf; 1. PE 2: Evidence at transcript level; KW Acetylation; Carbohydrate metabolism; Glucose metabolism; NADP; KW Oxidoreductase. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 513 Glucose-6-phosphate 1-dehydrogenase 2. FT /FTId=PRO_0000068086. FT ACT_SITE 263 263 Proton acceptor (By similarity). FT BINDING 40 40 NADP (By similarity). FT BINDING 72 72 NADP (By similarity). FT BINDING 201 201 Substrate (By similarity). FT BINDING 205 205 Substrate (By similarity). FT BINDING 238 238 NADP (By similarity). FT BINDING 357 357 NADP (By similarity). FT BINDING 487 487 NADP (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). SQ SEQUENCE 513 AA; 59126 MW; 655830EB767B6C53 CRC64; MAEQVTLSRT QVCGILREEL YQNDAFHQAD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL LPKETFIVGY ARSQLTVDDI QKQSEPFFKA TPEERPKLEE FFTRNSYVVG QYDDPASYKH LNSYINALHQ GMQANHLFYL ALPPTVYEAV TKNIQETCMS QTGFNRIIVE KPFGRDLQSS NQLSNHISSL FREDQIYRID HYLDKEMVQN LMVLRFANRI FGPIWNGDNI VCVILTFKEP FGTEGRGGYF DEFGIIRDVM QSHLLQMLCL VAMEKPATTD SDDVRNEKVK VLKCISEVET DNVILGQYVG NPNGEGEAAN GYLDDPTVPR GSTTATFAAA VLYVKNERWD GVPFILRCGK ALNERKAEVR LQFRDIPGDI FHQKCKRNEL VIRMQPNEAV YTTMMTKKPG MFFNPEESEL DLTYGNKYKN VKLPGAYERL ILDVFCGCQM HFVRTDELRE GWRIFTPLLH KIEREKPQPF PYVYGSRGPT EADELMRRVG FQYKGTYKGT HKH //