ID   6PGD_PIG                Reviewed;         250 AA.
AC   P14332;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2003, sequence version 3.
DT   24-JAN-2024, entry version 130.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE            EC=1.1.1.44;
DE   Flags: Fragment;
GN   Name=PGD;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=2361879; DOI=10.1111/j.1601-5223.1990.tb00141.x;
RA   Harbitz I., Chowdhary B., Chowdhary R., Kran S., Frengen E., Gustavsson I.,
RA   Davies W.;
RT   "Isolation, characterization and chromosomal assignment of a partial cDNA
RT   for porcine 6-phosphogluconate dehydrogenase.";
RL   Hereditas 112:83-88(1990).
RN   [2]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFTS.
RX   PubMed=1659648; DOI=10.1111/j.1365-2958.1991.tb01880.x;
RA   Reizer A., Deutscher J., Saier M.H. Jr., Reizer J.;
RT   "Analysis of the gluconate (gnt) operon of Bacillus subtilis.";
RL   Mol. Microbiol. 5:1081-1089(1991).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA34633.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X16638; CAA34633.1; ALT_FRAME; mRNA.
DR   PIR; A48325; A48325.
DR   AlphaFoldDB; P14332; -.
DR   SMR; P14332; -.
DR   STRING; 9823.ENSSSCP00000066512; -.
DR   PaxDb; 9823-ENSSSCP00000003687; -.
DR   PeptideAtlas; P14332; -.
DR   eggNOG; KOG2653; Eukaryota.
DR   InParanoid; P14332; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
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; ISS:UniProtKB.
DR   GO; GO:0046177; P:D-gluconate catabolic process; IBA:GO_Central.
DR   GO; GO:0006098; P:pentose-phosphate shunt; ISS:UniProtKB.
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   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006114; 6PGDH_C.
DR   InterPro; IPR006184; 6PGdom_BS.
DR   InterPro; IPR006183; Pgluconate_DH.
DR   PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11811:SF25; 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF00393; 6PGD; 1.
DR   PRINTS; PR00076; 6PGDHDRGNASE.
DR   SMART; SM01350; 6PGD; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   PROSITE; PS00461; 6PGD; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Gluconate utilization; NADP; Oxidoreductase;
KW   Pentose shunt; Reference proteome.
FT   CHAIN           <1..250
FT                   /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT                   /id="PRO_0000090065"
FT   BINDING         29
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         245..248
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         77
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P52209"
FT   NON_TER         1
SQ   SEQUENCE   250 AA;  27806 MW;  8BBB0655D9A40C36 CRC64;
     IEITANILKF QDADGKHLLP KIRDSAGQKG TGKWTAISAL EYGVPVTLIG EAVFARCLSS
     LKDERVQASK KLKGPQKIQF SGDKKSFLED IRKALYASKI ISYTQGFMLL RQAAAEFGWS
     STTEHRLMWR GGCIIRSVFL GKIKDAFDRN PGLQNLLLDD FFKSAVEDCQ DSWRRAVSTG
     VQTGIPMPCF TTALSFYDGY RHEMLPANLI QAQRDYFGAH TYELLAKPGH FVHTNWTGHG
     GSVSSSSYNA
//