Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-01158
Entry Name
UniProt Accession
Theoretical PI
6.81
Molecular Weight
53247.2
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
6-phosphogluconate dehydrogenase, decarboxylating
Protein Synonyms/Alias
1.1.1.44;
Gene Name
Pgd
Gene Synonyms/Alias
Created Date
15-MAY-2002
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
422
Canonical
QAGIPMPCFTTALSF
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
Catalyzes the oxidative decarboxylation of 6- phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Sequence Annotation
Nucleotide-binding: 10 15 NADP.
Nucleotide-binding: 33 35 NADP.
Nucleotide-binding: 75 77 NADP.
Nucleotide-binding: 478 481 NADP; shared with dimeric partner.
Region: 129 131 Substrate binding.
Region: 187 188 Substrate binding.
Active site: 184 184 Proton acceptor.
Active site: 191 191 Proton donor.
Binding site: 103 103 NADP.
Binding site: 103 103 Substrate.
Binding site: 192 192 Substrate.
Binding site: 261 261 Substrate; via amide nitrogen.
Binding site: 288 288 Substrate.
Binding site: 447 447 Substrate; shared with dimeric partner.
Binding site: 453 453 Substrate; shared with dimeric partner.
Modified residue: 38 38 N6-acetyllysine.
Modified residue: 59 59 N6-acetyllysine.
Modified residue: 257 257 Phosphoserine.
Modified residue: 263 263 Phosphothreonine.
Modified residue: 267 267 Phosphothreonine.
Modified residue: 270 270 Phosphoserine.
Protein Length
483 AA.
Protein Sequence
(Canonical)
MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKD  60
MVSKLKKPRR VILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCRDLKAKG  120
ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKAIFQAI AAKVGTGEPC CDWVGDEGAG  180
HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MRHEEMAQAF EEWNKTELDS FLIEITANIL  240
KYRDTDGKEL LPKIRDSAGQ KGTGKWTAIS ALEYGMPVTL IGEAVFARCL SSLKEERVQA  300
SQKLKGPKVV QLEGSKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL  360
MWRGGCIIRS VFLGKIKDAF ERNPELQNLL LDDFFKSAVD NCQDSWRRVI STGVQAGIPM  420
PCFTTALSFY DGYRHEMLPA NLIQAQRDYF GAHTYELLTK PGEFIHTNWT GHGGSVSSSS  480
YNA                                                                483
FASTA
(Canonical)
>LipidDB-10090-01158|Q9DCD0
MAQADIALIGLAVMGQNLILNMNDHGFVVCAFNRTVSKVDDFLANEAKGTKVVGAQSLKD
MVSKLKKPRRVILLVKAGQAVDDFIEKLVPLLDTGDIIIDGGNSEYRDTTRRCRDLKAKG
ILFVGSGVSGGEEGARYGPSLMPGGNKEAWPHIKAIFQAIAAKVGTGEPCCDWVGDEGAG
HFVKMVHNGIEYGDMQLICEAYHLMKDVLGMRHEEMAQAFEEWNKTELDSFLIEITANIL
KYRDTDGKELLPKIRDSAGQKGTGKWTAISALEYGMPVTLIGEAVFARCLSSLKEERVQA
SQKLKGPKVVQLEGSKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIAL
MWRGGCIIRSVFLGKIKDAFERNPELQNLLLDDFFKSAVDNCQDSWRRVISTGVQAGIPM
PCFTTALSFYDGYRHEMLPANLIQAQRDYFGAHTYELLTKPGEFIHTNWTGHGGSVSSSS
YNA
Gene Ontology
GO:0005737; C:cytoplasm; IEA:UniProtKB-KW
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005634; C:nucleus; IEA:Ensembl
GO:0050661; F:NADP binding; IEA:InterPro
GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; ISS:UniProtKB
GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW
GO:0019322; P:pentose biosynthetic process; IDA:MGI
GO:0006098; P:pentose-phosphate shunt; ISS:UniProtKB
GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:Ensembl
Interpro
InterPro; IPR008927; 6-PGluconate_DH_C-like
InterPro; IPR006114; 6PGDH_C
InterPro; IPR006113; 6PGDH_decarbox
InterPro; IPR006115; 6PGDH_NADP-bd
InterPro; IPR006184; 6PGdom_BS
InterPro; IPR013328; DH_multihelical
InterPro; IPR012284; Fibritin/6PGD_C-extension
InterPro; IPR016040; NAD(P)-bd_dom
Pfam
Pfam; PF00393; 6PGD;
Pfam; PF03446; NAD_binding_2;
SMART
PROSITE
PROSITE; PS00461; 6PGD;
PRINTS