UniProt Accession

 6PGD_HUMAN; P52209; A8K2Y9; Q9BWD8 

Genbank Protein ID

 U30255; AK290404; AL139424; CH471130; BC000368 

Genbank Nucleotide ID

 AAA75302.1; BAF83093.1; CAI95751.1; EAW71648.1; AAH00368.1 

Protein Name

 6-phosphogluconate dehydrogenase, decarboxylating 

Protein Synonyms/Alias

  

Gene Name

 PGD 

Gene Synonyms/Alias

 PGDH 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
38	AFNRTVSKVDDFLAN	acetylation	[1]
38	AFNRTVSKVDDFLAN	ubiquitination	[2, 3, 4, 5, 6, 7]
48	DFLANEAKGTKVVGA	ubiquitination	[3, 5, 6, 8]
51	ANEAKGTKVVGAQSL	ubiquitination	[5]
59	VVGAQSLKEMVSKLK	acetylation	[1]
59	VVGAQSLKEMVSKLK	ubiquitination	[2, 3, 4, 5, 6, 7, 8, 9, 10]
76	RRIILLVKAGQAVDD	acetylation	[1]
119	RCRDLKAKGILFVGS	ubiquitination	[2, 3, 5, 7]
147	SLMPGGNKEAWPHIK	ubiquitination	[5]
154	KEAWPHIKTIFQGIA	acetylation	[1]
154	KEAWPHIKTIFQGIA	ubiquitination	[2, 5, 7]
163	IFQGIAAKVGTGEPC	ubiquitination	[5]
248	KFQDTDGKHLLPKIR	ubiquitination	[4, 5]
265	AGQKGTGKWTAISAL	ubiquitination	[5]
294	ARCLSSLKDERIQAS	ubiquitination	[5, 8]
309	KKLKGPQKFQFDGDK	acetylation	[1]
309	KKLKGPQKFQFDGDK	ubiquitination	[4]
316	KFQFDGDKKSFLEDI	ubiquitination	[5]
317	FQFDGDKKSFLEDIR	ubiquitination	[5]
377	SVFLGKIKDAFDRNP	ubiquitination	[3, 4, 5, 6]
460	HTYELLAKPGQFIHT	ubiquitination	[5]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [9] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [10] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048] 

Functional Description

 Catalyzes the oxidative decarboxylation of 6- phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH (By similarity). 

Sequence Annotation

 NP_BIND 10 15 NADP.
 NP_BIND 33 35 NADP.
 NP_BIND 75 77 NADP.
 NP_BIND 478 481 NADP; shared with dimeric partner.
 REGION 129 131 Substrate binding (By similarity).
 REGION 187 188 Substrate binding (By similarity).
 ACT_SITE 184 184 Proton acceptor (By similarity).
 ACT_SITE 191 191 Proton donor (By similarity).
 BINDING 103 103 NADP.
 BINDING 103 103 Substrate (By similarity).
 BINDING 192 192 Substrate (By similarity).
 BINDING 261 261 Substrate; via amide nitrogen (By
 BINDING 288 288 Substrate (By similarity).
 BINDING 447 447 Substrate; shared with dimeric partner
 BINDING 453 453 Substrate; shared with dimeric partner
 MOD_RES 59 59 N6-acetyllysine.
 MOD_RES 257 257 Phosphoserine (By similarity).
 MOD_RES 263 263 Phosphothreonine (By similarity).
 MOD_RES 267 267 Phosphothreonine (By similarity).
 MOD_RES 270 270 Phosphoserine (By similarity).
 MOD_RES 309 309 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Gluconate utilization; NADP; Oxidoreductase; Pentose shunt; Phosphoprotein; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 483 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 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; IEA:Compara.
 GO:0009051; P:pentose-phosphate shunt, oxidative branch; IDA:UniProtKB. 

Interpro

 IPR008927; 6-PGluconate_DH_C-like.
 IPR006114; 6PGDH_C.
 IPR006113; 6PGDH_decarbox.
 IPR006115; 6PGDH_NADP-bd.
 IPR006184; 6PGdom_BS.
 IPR013328; DH_multihelical.
 IPR012284; Fibritin/6PGD_C-extension.
 IPR016040; NAD(P)-bd_dom. 

Pfam

 PF00393; 6PGD
 PF03446; NAD_binding_2 

SMART

  

PROSITE

 PS00461; 6PGD 

PRINTS