ID   A0A069DAE9_9BACL        Unreviewed;       470 AA.
AC   A0A069DAE9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   12-AUG-2020, entry version 30.
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; 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(+) = CO2 + D-ribulose 5-phosphate
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}.
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DR   EMBL; BBIW01000003; GAK39753.1; -; Genomic_DNA.
DR   RefSeq; WP_047910918.1; NZ_BBIW01000003.1.
DR   STRING; 1499968.TCA2_2242; -.
DR   EnsemblBacteria; GAK39753; GAK39753; TCA2_2242.
DR   eggNOG; COG0362; Bacteria.
DR   OrthoDB; 1245550at2; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000028160; Unassembled WGS sequence.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
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   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   PANTHER; PTHR11811; PTHR11811; 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; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00873; gnd; 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|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
FT                   /note="6PGD"
FT                   /evidence="ECO:0000259|SMART:SM01350"
FT   NP_BIND         10..15
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT   NP_BIND         33..35
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT   NP_BIND         74..76
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT   REGION          128..130
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   REGION          185..186
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
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         102
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT   BINDING         102
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         190
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         260
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         287
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         446
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         452
FT                   /note="Substrate; shared with dimeric partner"
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
//