6PGD2_SPIOL
ID 6PGD2_SPIOL Reviewed; 537 AA.
AC Q94KU2;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating 2, chloroplastic {ECO:0000305};
DE EC=1.1.1.44 {ECO:0000269|PubMed:11322889};
DE Flags: Precursor;
GN Name=pgdP {ECO:0000305};
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], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PROTEIN SEQUENCE OF 71-83; 288-300;
RP 350-357 AND 358-369.
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:0000269|PubMed:11322889}.
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 Evidence={ECO:0000269|PubMed:11322889};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10117;
CC Evidence={ECO:0000269|PubMed:11322889};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for 6-phosphoglutanate {ECO:0000269|PubMed:11322889};
CC KM=6 uM for NADP {ECO:0000269|PubMed:11322889};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11322889}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF295670; AAK49897.1; -; mRNA.
DR AlphaFoldDB; Q94KU2; -.
DR SMR; Q94KU2; -.
DR SABIO-RK; Q94KU2; -.
DR UniPathway; UPA00115; UER00410.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IDA:UniProtKB.
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 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 Chloroplast; Direct protein sequencing; Gluconate utilization; NADP;
KW Oxidoreductase; Pentose shunt; Plastid; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..537
FT /note="6-phosphogluconate dehydrogenase, decarboxylating 2,
FT chloroplastic"
FT /id="PRO_0000421104"
FT ACT_SITE 230
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT ACT_SITE 237
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 55..60
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 78..80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 122..124
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 150
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 150
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 176..178
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 233..234
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 238
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 308
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 335
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 500
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P96789"
FT BINDING 506
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P96789"
SQ SEQUENCE 537 AA; 58293 MW; 8AB4D8F926B1DA71 CRC64;
MRSEVPSSTS PSFLSPPFIH LPLLSLSSPT PLPHSSSSTF SLFSTMAASQ IGLVGLAVMG
QNLALNIAEK GFPISVYNRT ASKVDETLDR AKSEGDLPLS GHYTPRDFVL SIERPRSIVI
LVKAGSPVDQ TIASLASFME PGDTIIDGGN EWYQNTERRL SDAHSNGLLY LGMGVSGGEE
GARFGPSLMP GGDFQAYDNI QHILKKVAAQ VDDGPCVTYI GEGGSGNFVK MVHNGIEYGD
MQLISEAYDV LKNVGGLSNE ELGQIFDEWN KSELESFLVE ITADIFKVKD DLADGGLVDK
ILDKTGMKGT GKWTVQQAAE LSVAAPTIAA SLDCRYLSGL KEERENAAKI LEAAGMKEEV
NAIRGGVDKK RLIDDVRQAL YASKICSYAQ GMNLLRAKSA EMGWDLNLGE LARIWKGGCI
IRAVFLDSIK QAYQRNPNLA SLVVDPEFAK EMVQRQAAWR RVVGLAVSAG ISTPGMCASL
AYFDTYRRAR LPANLVQAQR DYFGAHTYER VDLPGSYHTE WSKLARKSDP NVAAALH
