6PGD1_SPIOL
ID 6PGD1_SPIOL Reviewed; 483 AA.
AC Q94KU1;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating 1;
DE EC=1.1.1.44;
GN Name=pgdC;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RX PubMed=11322889; DOI=10.1046/j.1432-1327.2001.02154.x;
RA Krepinsky K., Plaumann M., Martin W., Schnarrenberger C.;
RT "Purification and cloning of chloroplast 6-phosphogluconate dehydrogenase
RT from spinach. Cyanobacterial genes for chloroplast and cytosolic isoenzymes
RT encoded in eukaryotic chromosomes.";
RL Eur. J. Biochem. 268:2678-2686(2001).
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:0000269|PubMed:11322889}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF307144; AAK51690.1; -; mRNA.
DR AlphaFoldDB; Q94KU1; -.
DR SMR; Q94KU1; -.
DR PRIDE; Q94KU1; -.
DR UniPathway; UPA00115; UER00410.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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.
PE 1: Evidence at protein level;
KW Cytoplasm; Gluconate utilization; NADP; Oxidoreductase; Pentose shunt.
FT CHAIN 1..483
FT /note="6-phosphogluconate dehydrogenase, decarboxylating 1"
FT /id="PRO_0000421103"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 193
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 78..80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 132..134
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 189..190
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
SQ SEQUENCE 483 AA; 53245 MW; A2E5CBB1C442D45F CRC64;
MAPPTRIGLA GLAVMGQNLA LNIAEKGFPI SVYNRTTSKV DETVERAKQE GNLPLYGFHD
PESFVNSIQK PRVIIMLVKA GAPVDATIKT LSAYLEKGDC IIDGGNEWYE NTERREKAME
EKGLLYLGMG VSGGEEGARN GPSMMPGGSF DAYKNIEDIL TKVAAQVDSG PCVTYIGKGG
SGNFVKMIHN GIEYGDMQLI AEAYDVLKSV GKLSNEELKE VFAEWNRGEL LSFLIEITAD
IFGIKDDKGE GYLVDKVLDK TGMKGTGKWT VQQAAELSVA APTIASSLDS RFLSGLKDER
VEAAKVFKAG GVEDTLSDQV VDKKKLIDDV RQALYAAKIC SYAQGMNLIR AKSVEKEWDL
KLGELARIWK GGCIIRAMFL DRIKKAYDRN PNLSNLLIDP EFSKEMIERQ SAWRRVVCLA
IGAGISTPGM SSSLAYFDSY RRERLPANLV QAQRDYFGAH TYERIDIPGA FHTEWFKLAK
SKI
