ID 6PGD_BUCBP Reviewed; 468 AA. AC Q89AX5; DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2003, sequence version 1. DT 25-NOV-2008, entry version 44. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating; DE EC=1.1.1.44; GN Name=gnd; OrderedLocusNames=bbp_101; OS Buchnera aphidicola subsp. Baizongia pistaciae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=135842; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22426901; 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 -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose CC 5-phosphate + CO(2) + NADPH. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 3/3. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate 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; AE016826; AAO26836.1; -; Genomic_DNA. DR RefSeq; NP_777731.1; -. DR HSSP; P00349; 2PGD. DR GeneID; 1058155; -. DR GenomeReviews; AE016826_GR; bbp_101. DR KEGG; bab:bbp101; -. DR HOGENOM; Q89AX5; -. DR BioCyc; BAPH224915:BBP_101-MON; -. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxyla...; IEA:InterPro. DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro. DR InterPro; IPR006183; 6-phosphogluconate_DHase. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_decarbox. DR InterPro; IPR006115; 6PGDH_NAD-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR013328; DHase_multihelical. DR InterPro; IPR012284; Fibritin/6PGD_C-extension. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:1.20.5.320; Fibritin/6PGD_C-extension; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. PE 3: Inferred from homology; KW Complete proteome; Gluconate utilization; NADP; Oxidoreductase; KW Pentose shunt. FT CHAIN 1 468 6-phosphogluconate dehydrogenase, FT decarboxylating. FT /FTId=PRO_0000090030. SQ SEQUENCE 468 AA; 52646 MW; C28B8C09CCB64E11 CRC64; MAKQQIGVIG MAVMGRNLAL NMERNQYTVS IFNRSLDITE KIILNNPNKN LFPFFSIKDF VLSLIVPRCI VLMIKSGVAT DDTIKSLIPY LSKGDIIIDG GNTFYKDTIQ RGYELLKIGV NLIGAGFSGG EKGALYGPSI MPGGRQEAYN YVSPILKKIA SNSEGIPCVT YIGPDGSGHY VKMVHNGIEY GDMQLIAESY FILKTLLRLD NQSISKIFDI WNQGELNSYL IDITKDILIK KDDQNNYLID CILDEGSSKG TGTWTTKSAL DLNEPLTLIT ESVFFRYLSS LKSQRLLASK ILCGPKDFFI VLNRDDFIEK IRQALYLGKI ISYAQGFSQL NSASQKYNWN LKLGEISRIF QSGCIIRAKL LKNITQEYSS NNNFVNLLLT PYFREIANTY HSSLREIVSI SVKYGIPIPA LSSAISYFDS YRSAFLPSNL IQAQRDFFGA HTYKRIDKSG IFHTNWYS //