UniProt Accession

 B4DQJ8_HUMAN; B4DQJ8 

Genbank Protein ID

 AL139424; AK298830 

Genbank Nucleotide ID

 BAG60960.1 

Protein Name

 6-phosphogluconate dehydrogenase, decarboxylating 

Protein Synonyms/Alias

  

Gene Name

 PGD 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
25	AFNRTVSKVDDFLAN	acetylation	[1, 2]
25	AFNRTVSKVDDFLAN	ubiquitination	[2, 3, 4, 5, 6]
35	DFLANEAKGTKVVGA	ubiquitination	[2, 4, 5, 6, 7, 8]
38	ANEAKGTKVVGAQSL	ubiquitination	[2, 5]
46	VVGAQSLKEMVSKLK	acetylation	[1, 2, 9]
46	VVGAQSLKEMVSKLK	ubiquitination	[2, 3, 4, 5, 6, 8, 10]
74	AVDDFIEKLVPLLDT	acetylation	[11]
106	RCRDLKAKGILFVGS	ubiquitination	[2, 3, 4, 5]
134	SLMPGGNKEAWPHIK	ubiquitination	[2, 5]
141	KEAWPHIKTIFQGIA	acetylation	[1]
141	KEAWPHIKTIFQGIA	ubiquitination	[2, 3, 5]
150	IFQGIAAKVGTGEPC	ubiquitination	[2, 5, 12]
235	KFQDTDGKHLLPKIR	ubiquitination	[2, 5]
252	AGQKGTGKWTAISAL	ubiquitination	[5]
281	ARCLSSLKDERIQAS	ubiquitination	[5, 8]
296	KKLKGPQKFQFDGDK	acetylation	[2]
303	KFQFDGDKKSFLEDI	acetylation	[2]
303	KFQFDGDKKSFLEDI	ubiquitination	[2, 5]
304	FQFDGDKKSFLEDIR	ubiquitination	[5]
364	SVFLGKIKDAFDRNP	ubiquitination	[2, 4, 5, 6]
447	HTYELLAKPGQFIHT	ubiquitination	[5]

Reference

 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] 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]
 [4] 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]
 [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] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [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] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [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]
 [11] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [12] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 

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

 REGION 116 118 Substrate binding (By similarity).
 REGION 174 175 Substrate binding (By similarity).
 ACT_SITE 171 171 Proton acceptor (By similarity).
 ACT_SITE 178 178 Proton donor (By similarity).
 BINDING 90 90 Substrate (By similarity).
 BINDING 179 179 Substrate (By similarity).
 BINDING 248 248 Substrate; via amide nitrogen (By
 BINDING 275 275 Substrate (By similarity).
 BINDING 434 434 Substrate; shared with dimeric partner
 BINDING 440 440 Substrate; shared with dimeric partner  

Keyword

 Complete proteome; NADP; Oxidoreductase; Pentose shunt; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 470 AA 

Protein Sequence

Gene Ontology

 GO:0050661; F:NADP binding; IEA:InterPro.
 GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:EC.
 GO:0019322; P:pentose biosynthetic process; IEA:Compara.
 GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway. 

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