Summary: Glucose-6-phosphate dehydrogenase, C-terminal domain

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Wikipedia: Glucose-6-phosphate dehydrogenase
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Glucose-6-phosphate dehydrogenase Edit Wikipedia article

Glucose-6-phosphate dehydrogenase

Identifiers

Databases

PDB structures

AmiGO / EGO

Search
PMC	articles
PubMed	articles
NCBI	proteins

Glucose-6-phosphate dehydrogenase, NAD binding domain

glucose 6-phosphate dehydrogenase from leuconostoc mesenteroides

Identifiers

Symbol

G6PD_N

Pfam clan

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Glucose-6-phosphate dehydrogenase, C-terminal domain

Identifiers

Symbol

G6PD_C

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Glucose-6-phosphate dehydrogenase

PDB rendering based on 1qki.

Available structures

PDB

Ortholog search: PDBe, RCSB

List of PDB id codes
1QKI, 2BH9, 2BHL

Identifiers

Symbols

G6PD; G6PD1

External IDs

OMIM: 305900 MGI: 105979 HomoloGene: 37906 ChEMBL: 5347 GeneCards: G6PD Gene

EC number

1.1.1.49

Gene Ontology
Molecular function	• glucose-6-phosphate dehydrogenase activity • glucose binding • protein homodimerization activity • NADP binding
Cellular component	• cytoplasm • centrosome • cytosol • internal side of plasma membrane • intracellular membrane-bounded organelle
Biological process	• cytokine production • carbohydrate metabolic process • pentose-phosphate shunt • lipid metabolic process • cholesterol biosynthetic process • NADPH regeneration • glutathione metabolic process • pentose-phosphate shunt, oxidative branch • negative regulation of protein glutathionylation • pentose biosynthetic process • cellular response to oxidative stress • erythrocyte maturation • small molecule metabolic process • ribose phosphate biosynthetic process • glucose 6-phosphate metabolic process • oxidation-reduction process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr HG1497_PATCH:
153.74 – 153.76 Mb

Chr X:
74.41 – 74.43 Mb

PubMed search

[1]

[2]

Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) is a cytosolic enzyme in the pentose phosphate pathway (see image), a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). The NADPH in turn maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage. Of greater quantitative importance is the production of NADPH for tissues actively engaged in biosynthesis of fatty acids and/or isoprenoids, such as the liver, mammary glands, adipose tissue, and the adrenal glands. G6PD reduces nicotinamide adenine dinucleotide phosphate (NADP) to NADPH while oxidizing glucose-6-phosphate.^[1]

It is notable in humans when there is a genetic deficiency of G6PD which predisposes to non-immune hemolytic anemia .

[edit] Species distribution

G6PD is widely distributed in many species from bacteria to humans. In higher plants, several isoforms of G6PDH have been reported, which are localized in the cytosol, the plastidic stroma, and peroxisomes.^[2]

[edit] Regulation

Glucose-6-phosphate dehydrogenase is stimulated by its substrate Glucose 6 Phosphate. The usual ratio of NADPH/NADP⁺ in the cytosol of tissues engaged in biosyntheses is about 100/1. Increased utilization of NADPH for fatty acid biosynthesis will dramatically increase the level of NADP⁺, thus stimulating G6PD to produce more NADPH.

G6PD converts glucose-6-phosphate into 6-phosphoglucono-δ-lactone and is the rate-limiting enzyme of the pentose phosphate pathway.

G6PD is one of a number of glycolytic enzymes activated by the transcription factor Hypoxia-inducible factor 1 (HIF1).^[3]

[edit] Clinical significance

G6PD is remarkable for its genetic diversity. Many variants of G6PD, mostly produced from missense mutations, have been described with wide ranging levels of enzyme activity and associated clinical symptoms. Two transcript variants encoding different isoforms have been found for this gene.^[4]

Glucose-6-phosphate dehydrogenase deficiency is very common worldwide, and causes acute hemolytic anemia in the presence of simple infection, ingestion of fava beans, or reaction with certain medicines, antibiotics, antipyretics, and antimalarials.^[5]

Cell growth and proliferation are affected by G6PD.^[6] G6PD inhibitors are under investigation to treat cancers and other conditions.^[3] DHEA is a G6PD inhibitor.^[6]

[edit] See also

[edit] References

^ Aster J, Kumar V, Robbins SL, Abbas AK, Fausto N, Cotran RS (2010). Robbins and Cotran pathologic basis of disease. Saunders/Elsevier. pp. Kindle Locations 33340–33341. ISBN 1-4160-3121-9.
^ Corpas FJ, Barroso JB, Sandalio LM, Distefano S, Palma JM, Lupiáñez JA, Del Río LA (March 1998). "A dehydrogenase-mediated recycling system of NADPH in plant peroxisomes". Biochem. J. 330 ( Pt 2) (Pt 2): 777–84. PMC 1219205. PMID 9480890.
^ ^a ^b de Lartigue J (2012-06-12). "Cancer Research Moves Beyond the Original Hallmarks of Cancer". OncLive.
^ "Entrez Gene: G6PD glucose-6-phosphate dehydrogenase".
^ Cappellini MD, Fiorelli G (January 2008). "Glucose-6-phosphate dehydrogenase deficiency". Lancet 371 (9606): 64–74. doi:10.1016/S0140-6736(08)60073-2. PMID 18177777.
^ ^a ^b Tian WN, Braunstein LD, Pang J, Stuhlmeier KM, Xi QC, Tian X, Stanton RC (April 1998). "Importance of glucose-6-phosphate dehydrogenase activity for cell growth". J. Biol. Chem. 273 (17): 10609–17. doi:10.1074/jbc.273.17.10609. PMID 9553122.

[edit] Further reading

Vulliamy T, Beutler E, Luzzatto L (1993). "Variants of glucose-6-phosphate dehydrogenase are due to missense mutations spread throughout the coding region of the gene". Hum. Mutat. 2 (3): 159–67. doi:10.1002/humu.1380020302. PMID 8364584.
Mason PJ (1996). "New insights into G6PD deficiency". Br. J. Haematol. 94 (4): 585–91. PMID 8826878.
Wajcman H, Galactéros F (2004). "[Glucose 6-phosphate dehydrogenase deficiency: a protection against malaria and a risk for hemolytic accidents]". C. R. Biol. 327 (8): 711–20. doi:10.1016/j.crvi.2004.07.010. PMID 15506519.

[edit] External links

PDB gallery

1qki: X-RAY STRUCTURE OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE (VARIANT CANTON R459L) COMPLEXED WITH STRUCTURAL NADP+

2bh9: X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP

2bhl: X-RAY STRUCTURE OF HUMAN GLUCOSE-6-PHOSPHATE DEHYDROGENASE (DELETION VARIANT) COMPLEXED WITH GLUCOSE-6-PHOSPHATE

Oxidoreductases: alcohol oxidoreductases (EC 1.1)

1.1.1: NAD/NADP acceptor

Hydroxysteroid dehydrogenase: 3 Beta
- 3-beta-HSD
- NSDHL
11 Beta
- HSD11B1
- HSD11B2
17 Beta

1.1.2: cytochrome acceptor

1.1.3: oxygen acceptor

1.1.4: disulfide as acceptor

1.1.5: quinone/similar acceptor

1.1.99: other acceptors

B
enzm
1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
2.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
2.7.10
2.7.11-12
3.1
- - 3.1.3.48
- 2
- 3
- 4
  - 3.4.21
- 5
- 6
- 7
- 22
- 23
- 24
4.1
- 2
- 3
- 4
- 5
- 6
5.1
- 2
- 3
- 4
- 99
6.1-3
- 4
- 5-6

Metabolism: carbohydrate metabolism · pentose phosphate pathway enzymes

oxidative

Glucose-6-phosphate dehydrogenase
6-phosphogluconolactonase
Phosphogluconate dehydrogenase

nonoxidative

M: MET

mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m

k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon

m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)

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Glucose-6-phosphate dehydrogenase, C-terminal domain Provide feedback

No Pfam abstract.

Literature references

Cosgrove MS, Naylor C, Paludan S, Adams MJ, Levy HR; , Biochemistry. 1998;37:2759-2767.: On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. PUBMED:9485426 EPMC:9485426

External database links

PANDIT:	PF02781
PRINTS:	PR00079
PROSITE:	PDOC00067
Pseudofam:	PF02781
SCOP:	1dpg
SYSTERS:	G6PD_C

This tab holds annotation information from the InterPro database.

InterPro entry IPR022675

Glucose-6-phosphate dehydrogenase (EC) (G6PDH) is a ubiquitous protein, present in bacteria and all eukaryotic cell types [PUBMED:2838391]. The enzyme catalyses the the first step in the pentose pathway, i.e. the conversion of glucose-6-phosphate to gluconolactone 6-phosphate in the presence of NADP, producing NADPH. The ubiquitous expression of the enzyme gives it a major role in the production of NADPH for the many NADPH-mediated reductive processes in all cells [PUBMED:3393536]. Deficiency of G6PDH is a common genetic abnormality affecting millions of people worldwide. Many sequence variants, most caused by single point mutations, are known, exhibiting a wide variety of phenotypes [PUBMED:3393536].

This entry represents the C-terminal domain of glucose-6-phosphate dehydrogenase.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Molecular function	NADP binding (GO:0050661)
	glucose-6-phosphate dehydrogenase activity (GO:0004345)
Biological process	glucose metabolic process (GO:0006006)
	oxidation-reduction process (GO:0055114)

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

There are various ways to view or download the sequence alignments that we store. We provide several sequence viewers and a plain-text Stockholm-format file for download.

Alignment types

We make a range of alignments for each Pfam-A family:

seed: the curated alignment from which the HMM for the family is built
full: the alignment generated by searching the sequence database using the HMM
RP15/RP35/RP55/RP75: Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
NCBI: alignment generated by searching the NCBI sequence database using the family HMM
meta: alignment generated by searching the metagenomics sequence database using the family HMM

Viewing

You can see the alignments as HTML or in three different sequence viewers:

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Pfam viewer: an HTML-based viewer that uses DAS to retrieve alignment fragments on request

Reformatting

You can download (or view in your browser) a text representation of a Pfam alignment in various formats:

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You may find that large alignments cause problems for the viewers and the reformatting tool, so we also provide all alignments in Stockholm format. You can download either the plain text alignment, or a gzipped version of it.

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

	Seed (11)	Full (5312)	Representative proteomes				NCBI (3992)	Meta (928)
	Seed (11)	Full (5312)	RP15 (350)	RP35 (709)	RP55 (987)	RP75 (1208)	NCBI (3992)	Meta (928)
Jalview	View	View	View	View	View	View	View	View
HTML	View		View	View	View	View
PP/heatmap	₁		View	View	View	View
Pfam viewer	View	View

¹Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: available, not generated, — not available.

Format an alignment

	Seed (11)	Full (5312)	Representative proteomes				NCBI (3992)	Meta (928)
	Seed (11)	Full (5312)	RP15 (350)	RP35 (709)	RP55 (987)	RP75 (1208)	NCBI (3992)	Meta (928)
Alignment:
Format:
Order:	Tree Alphabetical
Sequence:	Inserts lower case All upper case
Gaps:
Download/view:	Download View

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

	Seed (11)	Full (5312)	Representative proteomes				NCBI (3992)	Meta (928)
	Seed (11)	Full (5312)	RP15 (350)	RP35 (709)	RP55 (987)	RP75 (1208)	NCBI (3992)	Meta (928)
Raw Stockholm	Download	Download	Download	Download	Download	Download	Download	Download
Gzipped	Download	Download	Download	Download	Download	Download	Download	Download

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation

Seed source:

Prosite

Previous IDs:

none

Type:

Domain

Author:

Finn RD, Griffiths-Jones SR

Number in seed:

11

Number in full:

5312

Average length of the domain:

265.50 aa

Average identity of full alignment:

41 %

Average coverage of the sequence by the domain:

59.39 %

HMM information

HMM build commands:

build method: hmmbuild -o /dev/null HMM SEED

search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq

Model details:

Parameter	Sequence	Domain
Gathering cut-off	19.5	19.5
Trusted cut-off	19.6	19.6
Noise cut-off	19.0	19.4

Model length:

294

Family (HMM) version:

11

Download:

download the raw HMM for this family

Species distribution

Sunburst
Tree

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.

How the sunburst is generated

The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.

In order to reduce the complexity of the representation, we reduce the number of taxonomic levels that we show. We consider only the following eight major taxonomic levels:

superkingdom
kingdom
phylum
class
order
family
genus
species

Colouring and labels

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Unmapped species names

The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.

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Sub-species

Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.

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Interactive tree

For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.

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Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.

We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.

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Interactions

There are 2 interactions for this family. More...

G6PD_C G6PD_N

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the G6PD_C domain has been found. There are 29 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

Loading structure mapping...

Archea	Eukaryota
Bacteria	Other sequences
Viruses	Unclassified
Viroids	Unclassified sequence

Family: G6PD_C (PF02781)

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Summary: Glucose-6-phosphate dehydrogenase, C-terminal domain

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Glucose-6-phosphate dehydrogenase Edit Wikipedia article

Contents

[edit] Species distribution

[edit] Regulation

[edit] Clinical significance

[edit] See also

[edit] References

[edit] Further reading

[edit] External links

Glucose-6-phosphate dehydrogenase, C-terminal domain Provide feedback

Literature references

External database links

InterPro entry IPR022675

Gene Ontology

Domain organisation

Alignments

Alignment types

Viewing

Reformatting

Downloading

View options

Format an alignment

Download options

External links

HMM logo

Trees

Curation and family details

Curation

HMM information

Species distribution

Sunburst controls

Weight segments by...

Change the size of the sunburst

Colour assignments

Selections

Currently selected:

How the sunburst is generated

Colouring and labels

Anomalies in the taxonomy tree

Missing taxonomic levels

Unmapped species names

Sub-species

Too many species/sequences

Tree controls

Annotation

Download tree

Selected sequences

Species trees

Interactive tree

Interactions

Structures