ID   6PGD_CERCA              Reviewed;         481 AA.
AC   P41570;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE            EC=1.1.1.44;
GN   Name=Pgd;
OS   Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Ceratitis; Ceratitis.
OX   NCBI_TaxID=7213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8269100; DOI=10.1111/j.1365-2583.1993.tb00094.x;
RA   Scott M.J., Kriticou D., Robinson A.S.;
RT   "Isolation of cDNAs encoding 6-phosphogluconate dehydrogenase and glucose-
RT   6-phosphate dehydrogenase from the mediterranean fruit fly Ceratitis
RT   capitata: correlating genetic and physical maps of chromosome 5.";
RL   Insect Mol. Biol. 1:213-222(1993).
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}.
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; S67873; AAB29396.1; -; mRNA.
DR   RefSeq; NP_001266319.1; NM_001279390.1.
DR   AlphaFoldDB; P41570; -.
DR   SMR; P41570; -.
DR   PRIDE; P41570; -.
DR   GeneID; 101451876; -.
DR   KEGG; ccat:101451876; -.
DR   OrthoDB; 847823at2759; -.
DR   UniPathway; UPA00115; UER00410.
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   2: Evidence at transcript level;
KW   Gluconate utilization; NADP; Oxidoreductase; Pentose shunt.
FT   CHAIN           1..481
FT                   /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT                   /id="PRO_0000090068"
FT   ACT_SITE        184
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        191
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         11..16
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         34..36
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         76..78
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..132
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         187..188
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         445
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         451
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   481 AA;  52964 MW;  F0ABB506AD1B86D0 CRC64;
     MSAKADIALI GLAVMGQNLV LNMNDKGFVV CAYNRTVEKV NQFLKNEAKG TNVIGATSLQ
     DMVNKLKLPR KIMLLVKAGS AVDDFIQQLV PLLSPGDVII DGGNSEYQDT ARRCDELRAK
     KILYVGSGVS GGEEGARHGP SLMPGGHPEA WPLIQPIFQS ICAKADKEPC CEWVGEGGAG
     HFVKMVHNGI EYGDMQLICE AYQIMKALGL SQAEMATEFE KWNSEELDSF LIEITRDILN
     YQDDRGYLLE RIRDTAGQKG TGKWTAISAL QYGVPVTLIG EAVFSRCLSA LKDERVAASK
     QLKGPNVNAK VEDLPKFLNH IKHALYCSKI VSYAQGFMLM REAAKENNWN LNYGGIALMW
     RGGCIIRSVF LGNIKDAYTR NPQLSNLLLD DFFKKAIEVG QNSWRQVVAN AFLWGIPVPA
     LSTALSFYDG YRTEKLPANL LQAQRDYFGA HTYELLGAEG KFVHTNWTGT GGNVSASTYQ
     A