ID   6PGD_DICDI              Reviewed;         493 AA.
AC   Q8TA03; Q54YT0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE            EC=1.1.1.44;
GN   Name=gnd; Synonyms=PGD; ORFNames=DDB_G0277885;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11818061; DOI=10.1016/s0960-9822(01)00649-2;
RA   Andersson J.O., Roger A.J.;
RT   "A cyanobacterial gene in nonphotosynthetic protists -- an early
RT   chloroplast acquisition in eukaryotes?";
RL   Curr. Biol. 12:115-119(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 37-48; 305-320 AND 447-456, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RA   Bienvenut W.V., Veltman D.M., Insall R.H.;
RL   Submitted (JAN-2010) to UniProtKB.
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:0000250}.
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   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       3/3.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AF394516; AAL76326.1; -; Genomic_DNA.
DR   EMBL; AAFI02000023; EAL68115.1; -; Genomic_DNA.
DR   RefSeq; XP_642122.1; XM_637030.1.
DR   AlphaFoldDB; Q8TA03; -.
DR   SMR; Q8TA03; -.
DR   STRING; 44689.Q8TA03; -.
DR   PaxDb; 44689-DDB0215011; -.
DR   EnsemblProtists; EAL68115; EAL68115; DDB_G0277885.
DR   GeneID; 8621331; -.
DR   KEGG; ddi:DDB_G0277885; -.
DR   dictyBase; DDB_G0277885; gnd.
DR   eggNOG; KOG2653; Eukaryota.
DR   HOGENOM; CLU_024540_4_2_1; -.
DR   InParanoid; Q8TA03; -.
DR   OMA; QALYMGK; -.
DR   PhylomeDB; Q8TA03; -.
DR   Reactome; R-DDI-71336; Pentose phosphate pathway.
DR   UniPathway; UPA00115; UER00410.
DR   PRO; PR:Q8TA03; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR   GO; GO:0046177; P:D-gluconate catabolic process; IBA:GO_Central.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Gluconate utilization; NADP; Oxidoreductase;
KW   Pentose shunt; Reference proteome.
FT   CHAIN           1..493
FT                   /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT                   /id="PRO_0000327487"
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        194
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         12..17
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         35..37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         77..79
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         131..133
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         190..191
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         456
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         462
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   493 AA;  53891 MW;  C3FD8A0F07DFC688 CRC64;
     MTEAKGDIGL IGLAVMGENL VLNMESRGFT CSVYNRTTSK VDEFVQGRGK GKKFIGCHSL
     ETLVQSLKTP RRVMLMVKAG EVVDHFIQLL LPLLEKGDII IDGGNSLYTD SDRRTKDLDA
     KGILFIGTGV SGGEEGALLG PSIMPGGNPK AWEHVKPIFQ AISAKVQPGD QPCCDWVGDG
     GAGHYVKMVH NGIEYGDMQL ISEAYFILKH YLGLSNDELQ KTFAKWNTGD LDSYLIEITA
     DIFAKKCEKD PNTYVVDTIL DSAGQKGTGK WTAINALDVG IPLTLVAESV FARCVSSFKE
     ERVKASTILA GPNPNEANKK FTGDKEQVIE AVRQALFASK LVSYAQGFTM MKAAAKEYKW
     NLNYGNIALL WRGGCIIRST FLGEIKGAFD KNPQLDNLLT DCWFRDKLAA AQDGWRQVAS
     ISVLHGIPTP AFTSALSYYD SYRCAKLSAN LVQAQRDYFG AHTFQLLDDP KGAPVHVNWT
     GRGGSTHSTT YSI
//