ID A0A069DAE9_9BACL Unreviewed; 470 AA. AC A0A069DAE9; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 07-JAN-2015, entry version 3. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}; DE EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}; GN ORFNames=TCA2_2242 {ECO:0000313|EMBL:GAK39753.1}; OS Paenibacillus sp. TCA20. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Paenibacillus. OX NCBI_TaxID=1499968 {ECO:0000313|EMBL:GAK39753.1}; RN [1] {ECO:0000313|EMBL:GAK39753.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TCA20 {ECO:0000313|EMBL:GAK39753.1}; RA Fujinami S., Takeda-Yano K., Onodera T., Satoh K., Sano M., RA Takahashi Y., Narumi I., Ito M.; RT "Draft Genome Sequence of Calcium-Dependent Paenibacillus sp. Strain RT TCA20, Isolated from a Hot Spring Containing a High Concentration of RT Calcium Ions."; RL Genome Announc. 2:e00866-14(2014). CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6- CC phosphogluconate to ribulose 5-phosphate and CO(2), with CC concomitant reduction of NADP to NADPH. CC {ECO:0000256|PIRNR:PIRNR000109}. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose CC 5-phosphate + CO(2) + NADPH. {ECO:0000256|PIRNR:PIRNR000109, CC ECO:0000256|RuleBase:RU000485}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 3/3. {ECO:0000256|PIRNR:PIRNR000109, CC ECO:0000256|RuleBase:RU000485}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000109}. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase CC family. {ECO:0000256|PIRNR:PIRNR000109, CC ECO:0000256|RuleBase:RU000485}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GAK39753.1}. 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; BBIW01000003; GAK39753.1; -; Genomic_DNA. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro. DR Gene3D; 1.10.1040.10; -; 1. DR Gene3D; 1.20.5.320; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_decarbox. DR InterPro; IPR006115; 6PGDH_NADP-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR012284; Fibritin/6PGD_C-extension. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000109; 6PGD; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. PE 3: Inferred from homology; KW Gluconate utilization {ECO:0000256|RuleBase:RU000486}; KW NADP {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000109, KW ECO:0000256|RuleBase:RU000485}; KW Pentose shunt {ECO:0000256|PIRNR:PIRNR000109, KW ECO:0000256|RuleBase:RU000485}. SQ SEQUENCE 470 AA; 51766 MW; ABD2E82E29EC1136 CRC64; MAKQQIGVIG LAVMGKNLAL NIESKGFSVS VFNRSPEKTQ DLLKEADGKN LVGTFSIEEF VQSLESPRKI LIMVQAGPAT DATIEQLVPH LDQGDIIIDG GNAYFPDTQR RSKELEEKGF RFIGAGVSGG EEGALKGPSI MPGGQESAYE LVKPILTSIA AQVNGEPCTT YIGPDGAGHY VKMVHNGIEY GDMQLIGEAY HLLKDVLGLN AEQFHEIFSE WNKGELDSYL IEITADIFSK YDEETGKPMV DVILDAAGQK GTGKWTSQSA LDLGVPLSMI TESVFSRFLS AMKEERIAAS KVLSGPKTEA FTGDKAEFIE NVRKALFASK IVSYAQGFAQ MRAASDEYGW NLKYGNIAMI FRGGCIIRSQ FLQNIKDAYD KDAELKNLLL DPYFKNVVES YQDAWRKVIS VAVANGIPVP GFASALSYYD SYRTERLPAN LLQAQRDYFG AHTFKRVDKE GTFHYNWMGN //