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InterPro: IPR006424 Glyceraldehyde-3-phosphate dehydrogenase, type I

Protein matchesHelp
UniProtKB
Matches:
3904 proteins
AccessionHelp IPR006424 Glyceraldehyde-3-P_DH_1
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR000173 Glyceraldehyde 3-phosphate dehydrogenase subfamily
Contains IPR016040 NAD(P)-binding domain
IPR020828 Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
IPR020829 Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain
IPR020830 Glyceraldehyde 3-phosphate dehydrogenase, active site
IPR020832 Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain, subgroup
GO Term annotationHelp
Process GO:0006006 glucose metabolic process
GO:0055114 oxidation reduction
Function GO:0008943 glyceraldehyde-3-phosphate dehydrogenase activity
GO:0051287 NAD or NADH binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This group of sequences represent glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilise NAD (EC:1.2.1.12), NADP (EC:1.2.1.13) or either (EC:1.2.1.59). In some species, NAD- and NADP- utilising forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively [1]. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine [2]. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria [3]. This enzyme is described by IPR006422. These two groups of sequences exhibit a close evolutionary relationship. There exists the possibility that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to possess a limited E4PD activity as well as a robust GAPDH activity [4]).

Structural linksHelp
PDB - click here
SCOP: c.2.1.3 , d.81.1.1
Database linksHelp
Enzyme: EC:1.2.1.12

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR006424 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O14556 Glyceraldehyde-3-phosphate dehydrogenase, testis-specific

P00358 Glyceraldehyde-3-phosphate dehydrogenase 2

P04970 Glyceraldehyde-3-phosphate dehydrogenase 1

P07486 Glyceraldehyde-3-phosphate dehydrogenase 1

P16858 Glyceraldehyde-3-phosphate dehydrogenase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR020828 Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
IPR016040 NAD(P)-binding domain
IPR020829 Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain
IPR006424 Glyceraldehyde-3-phosphate dehydrogenase, type I
IPR020831 Glyceraldehyde 3-phosphate dehydrogenase family
IPR020830 Glyceraldehyde 3-phosphate dehydrogenase, active site
IPR000173 Glyceraldehyde 3-phosphate dehydrogenase subfamily
IPR020832 Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain, subgroup
SWISS-MODEL
PDB Chain
ModBase

PublicationsHelp
1. Fillinger S, Boschi-Muller S, Azza S, Dervyn E, Branlant G, Aymerich S.
Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium.
J. Biol. Chem. 275 14031-7 2000 [PubMed: 10799476]
http://dx.doi.org/10.1074/jbc.275.19.14031
2. Zhao G, Pease AJ, Bharani N, Winkler ME.
Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis.
J. Bacteriol. 177 2804-12 1995 [PubMed: 7751290]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7751290&action=stream&blobtype=pdf
3. Mittenhuber G.
Phylogenetic analyses and comparative genomics of vitamin B6 (pyridoxine) and pyridoxal phosphate biosynthesis pathways.
J. Mol. Microbiol. Biotechnol. 3 1-20 2001 [PubMed: 11200221]
4. Boschi-Muller S, Azza S, Pollastro D, Corbier C, Branlant G.
Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate dehydrogenase of Escherichia coli and phosphorylating glyceraldehyde-3-phosphate dehydrogenase.
J. Biol. Chem. 272 15106-12 1997 [PubMed: 9182530]
http://dx.doi.org/10.1074/jbc.272.24.15106

Additional ReadingHelp
Frayne J, Taylor A, Cameron G, Hadfield AT.
Structure of Insoluble Rat Sperm Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) via Heterotetramer Formation with Escherichia coli GAPDH Reveals Target for Contraceptive Design.
J. Biol. Chem. 284 2009 22703-12 [PubMed: 19542219]
http://dx.doi.org/10.1074/jbc.M109.004648
Robien MA, Bosch J, Buckner FS, Van Voorhis WC, Worthey EA, Myler P, Mehlin C, Boni EE, Kalyuzhniy O, Anderson L, Lauricella A, Gulde S, Luft JR, DeTitta G, Caruthers JM, Hodgson KO, Soltis M, Zucker F, Verlinde CL, Merritt EA, Schoenfeld LW, Hol WG.
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum at 2.25 A resolution reveals intriguing extra electron density in the active site.
Proteins 62 2006 570-7 [PubMed: 16345073]
http://dx.doi.org/10.1002/prot.20801
Fermani S, Sparla F, Falini G, Martelli PL, Casadio R, Pupillo P, Ripamonti A, Trost P.
Molecular mechanism of thioredoxin regulation in photosynthetic A2B2-glyceraldehyde-3-phosphate dehydrogenase.
Proc. Natl. Acad. Sci. U.S.A. 104 2007 11109-14 [PubMed: 17573533]
http://dx.doi.org/10.1073/pnas.0611636104
Moniot S, Bruno S, Vonrhein C, Didierjean C, Boschi-Muller S, Vas M, Bricogne G, Branlant G, Mozzarelli A, Corbier C.
Trapping of the thioacylglyceraldehyde-3-phosphate dehydrogenase intermediate from Bacillus stearothermophilus. Direct evidence for a flip-flop mechanism.
J. Biol. Chem. 283 2008 21693-702 [PubMed: 18480053]
http://dx.doi.org/10.1074/jbc.M802286200
Jenkins JL, Tanner JJ.
High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase.
Acta Crystallogr. D Biol. Crystallogr. 62 2006 290-301 [PubMed: 16510976]
http://dx.doi.org/10.1107/S0907444905042289
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InterPro 23.1