ID A0A069DAE9_9BACL Unreviewed; 470 AA. AC A0A069DAE9; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 27-NOV-2024, entry version 44. 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; Bacillota; Bacilli; Bacillales; Paenibacillaceae; 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., Takahashi Y., RA Narumi I., Ito M.; RT "Draft Genome Sequence of Calcium-Dependent Paenibacillus sp. Strain TCA20, RT Isolated from a Hot Spring Containing a High Concentration of Calcium RT Ions."; RL Genome Announc. 2:e00866-14(2014). CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate CC to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP CC to NADPH. {ECO:0000256|PIRNR:PIRNR000109}. CC -!- CATALYTIC ACTIVITY: CC Reaction=6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO2 CC + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44; CC Evidence={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): step CC 3/3. {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, CC ECO:0000256|PIRNR:PIRNR000109}. CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|PIRNR:PIRNR000109, CC ECO:0000256|RuleBase:RU000485}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A069DAE9; -. DR eggNOG; COG0362; Bacteria. DR OrthoDB; 9804542at2; -. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000028160; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. DR GO; GO:0046177; P:D-gluconate catabolic process; IEA:TreeGrafter. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:TreeGrafter. DR FunFam; 1.10.1040.10:FF:000002; 6-phosphogluconate dehydrogenase, decarboxylating; 1. DR FunFam; 1.20.5.320:FF:000001; 6-phosphogluconate dehydrogenase, decarboxylating; 1. DR FunFam; 3.40.50.720:FF:000007; 6-phosphogluconate dehydrogenase, decarboxylating; 1. DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013328; 6PGD_dom2. DR InterPro; IPR006114; 6PGDH_C. DR InterPro; IPR006113; 6PGDH_Gnd/GntZ. DR InterPro; IPR006115; 6PGDH_NADP-bd. DR InterPro; IPR006184; 6PGdom_BS. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR006183; Pgluconate_DH. DR NCBIfam; TIGR00873; gnd; 1. DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1. DR PANTHER; PTHR11811:SF25; 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING; 1. 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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00461; 6PGD; 1. PE 3: Inferred from homology; KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064, KW ECO:0000256|RuleBase:RU000485}; KW NADP {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000109}; KW Pentose shunt {ECO:0000256|PIRNR:PIRNR000109, KW ECO:0000256|RuleBase:RU000485}; KW Reference proteome {ECO:0000313|Proteomes:UP000028160}. FT DOMAIN 178..468 FT /note="6-phosphogluconate dehydrogenase C-terminal" FT /evidence="ECO:0000259|SMART:SM01350" FT ACT_SITE 182 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1" FT ACT_SITE 189 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-1" FT BINDING 10..15 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3" FT BINDING 33..35 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3" FT BINDING 74..76 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3" FT BINDING 102 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-3" FT BINDING 102 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 128..130 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 185..186 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 190 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 260 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 287 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 446 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|PIRSR:PIRSR000109-2" FT BINDING 452 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="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 //