ID   A0A1X0WI15_9GAMM        Unreviewed;       469 AA.
AC   A0A1X0WI15;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   22-NOV-2017, entry version 5.
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=BS640_06090 {ECO:0000313|EMBL:ORJ26409.1};
OS   Rouxiella badensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Rouxiella.
OX   NCBI_TaxID=1646377 {ECO:0000313|EMBL:ORJ26409.1, ECO:0000313|Proteomes:UP000192536};
RN   [1] {ECO:0000313|EMBL:ORJ26409.1, ECO:0000313|Proteomes:UP000192536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100043 {ECO:0000313|EMBL:ORJ26409.1,
RC   ECO:0000313|Proteomes:UP000192536};
RX   PubMed=28100296;
RA   LE Fleche-Mateos A., Kugler J.H., Hansen S.H., Syldatk C.,
RA   Hausmann R., Lomprez F., Vandenbogaert M., Manuguerra J.C.,
RA   Grimont P.A.;
RT   "Rouxiella badensis sp. nov. and Rouxiella silvae sp. nov. isolated
RT   from peat bog soil in Germany and emendation of the genus
RT   description.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2017).
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:ORJ26409.1}.
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; MRWE01000007; ORJ26409.1; -; Genomic_DNA.
DR   RefSeq; WP_017490007.1; NZ_MRWE01000007.1.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000192536; 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   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   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:UP000192536};
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}.
FT   DOMAIN      179    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      186    187       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   ACT_SITE    183    183       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   ACT_SITE    190    190       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     191    191       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   469 AA;  51569 MW;  FD3875317566772B CRC64;
     MSKQQIGVVG MAVMGRNLAL NIESRGYSVA IFNRSGDKTD EVVAENPGKN LVPYYTVEEF
     VESLEKPRRI LLMVKAGEAT DKTIASLTPH LDKGDILIDG GNTFYKDTIR RNKELSDQGF
     NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILEQIA ARADDGDACV AYIGADGAGH
     YVKMVHNGIE YGDMQLIAEA YSLLKQSLNL SNEELATTFA EWNKGELSSY LIDITKDIFT
     KKDEAGNYLV DVILDEAANK GTGKWTSQSS LDLGEPLTLI TESVFARYLS SLKDQRVAAS
     KVLTGPAVKA FAGDKAEFIE KIRRALYLGK IVSYAQGFSQ LKAASDENNW NLHYGEIAKI
     FRAGCIIRAQ FLQKITDAYE ENASIANLLL APYFKNIADE YQQALRDVVS YAVQNGIPTP
     TFSAAINYYD SYRSAVLPAN LIQAQRDYFG AHTYKRTDKE GVFHTEWLD
//