6PGD_DICDI
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 03-AUG-2022, entry version 119.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
GN Name=gnd; Synonyms=PGD; ORFNames=DDB_G0277885;
OS Dictyostelium discoideum (Slime mold).
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.DDB0215011; -.
DR PaxDb; Q8TA03; -.
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; 1.10.1040.10; -; 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 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
