ID A0A069DAE9_9BACL Unreviewed; 470 AA. AC A0A069DAE9; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 18-JAN-2017, entry version 17. 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, ECO:0000313|Proteomes:UP000028160}; RN [1] {ECO:0000313|EMBL:GAK39753.1, ECO:0000313|Proteomes:UP000028160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TCA20 {ECO:0000313|EMBL:GAK39753.1, RC ECO:0000313|Proteomes:UP000028160}; 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 RefSeq; WP_047910918.1; NZ_BBIW01000003.1. DR EnsemblBacteria; GAK39753; GAK39753; TCA2_2242. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000028160; Unassembled WGS sequence. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. 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; IPR013328; 6PGD_dom_2. DR InterPro; IPR012284; 6PGD_dom_3. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_Gnd/GntZ. DR InterPro; IPR006115; 6PGDH_NADP-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006183; Pgluconate_DH. DR Pfam; PF00393; 6PGD; 1. DR Pfam; PF03446; NAD_binding_2; 1. DR PIRSF; PIRSF000109; 6PGD; 1. DR PRINTS; PR00076; 6PGDHDRGNASE. DR SMART; SM01350; 6PGD; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00873; gnd; 1. DR PROSITE; PS00461; 6PGD; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028160}; KW Gluconate utilization {ECO:0000256|RuleBase:RU000485}; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000028160}. FT DOMAIN 178 468 6PGD. {ECO:0000259|SMART:SM01350}. FT NP_BIND 10 15 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT NP_BIND 33 35 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT NP_BIND 74 76 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT REGION 128 130 Substrate binding. {ECO:0000256|PIRSR: FT PIRSR000109-2}. FT REGION 185 186 Substrate binding. {ECO:0000256|PIRSR: FT PIRSR000109-2}. FT ACT_SITE 182 182 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR000109-1}. FT ACT_SITE 189 189 Proton donor. {ECO:0000256|PIRSR: FT PIRSR000109-1}. FT BINDING 102 102 NADP. {ECO:0000256|PIRSR:PIRSR000109-3}. FT BINDING 102 102 Substrate. {ECO:0000256|PIRSR: FT PIRSR000109-2}. FT BINDING 190 190 Substrate. {ECO:0000256|PIRSR: FT PIRSR000109-2}. FT BINDING 260 260 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 287 287 Substrate. {ECO:0000256|PIRSR: FT PIRSR000109-2}. FT BINDING 446 446 Substrate; shared with dimeric partner. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 452 452 Substrate; shared with dimeric partner. FT {ECO:0000256|PIRSR:PIRSR000109-2}. 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 //