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InterPro: IPR006424 Glyceraldehyde-3-phosphate dehydrogenase, type I
Protein matches
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UniProtKB Matches: 3904 proteins |
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Accession
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IPR006424 Glyceraldehyde-3-P_DH_1 |
Type
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Family |
Signatures
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InterPro Relationships
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Parent
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IPR000173 Glyceraldehyde 3-phosphate dehydrogenase subfamily
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Contains
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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
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GO Term annotation
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Process
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GO:0006006 glucose metabolic process
GO:0055114 oxidation reduction
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Function
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GO:0008943 glyceraldehyde-3-phosphate dehydrogenase activity
GO:0051287 NAD or NADH binding
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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]).
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Structural links
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Database links
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Publications
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1.
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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
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2.
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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
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3.
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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]
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4.
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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
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Additional Reading
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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
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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
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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
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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
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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
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