Primary Information |
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| BoMiProt ID | Bomi352 |
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| Protein Name | D-3-phosphoglycerate dehydrogenase |
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| Organism | Bos taurus |
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| Uniprot ID | Q5EAD2 |
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| Milk Fraction | Exosome |
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| Ref Sequence ID | NP_001030189.1 |
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| Aminoacid Length | 533 |
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| Molecular Weight | 56452 |
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| FASTA Sequence |
Download |
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| Gene Name | PHGDH |
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| Gene ID | 505103 |
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| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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| Protein Function | catalyzes the first step in the pathway by converting D-3-
phosphoglycerate (PGA), an intermediate in glycolysis, to phosphohydroxypyruvate (PHP)
concomitant with the reduction of NAD+. PGDH is required for tumor cell proliferation, but extracellular l-serine is not able to support cell proliferation. |
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| Biochemical Properties | catalytic activity is regulated by feedback inhibition by L-serine; human enzyme appears to contain bound cofactor when isolated and the binding order appears to be coenzyme before substrate; slowly convert αKG to αHG. Three types of PGDH can be distinguished based on their domain structure. Type III PGDHs contain only a nucleotide binding and substrate binding domain. Type II PGDHs contain an additional regulatory domain (ACT domain), and Type I PGDHs contain a fourth domain, termed the ASB domain. There is no consistent pattern of domain content that correlates with organism type, and even when additional domains are present, they are not always functional. |
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| Significance in milk | synthesise L-serine, an important nutrient for brain function and development |
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| PTMs | N6-acetyllysine,Phosphoserine,Isopeptide bond,Ubl conjugation. |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | 1. Davis, J. L. and Fallon, H. J. (1970) ‘Studies on the role of 3-phosphoglycerate dehydrogenase in the regulation of serine biosynthesis in rat liver.’, The Journal of biological chemistry, 245(21), pp. 5838–46. Available at: http://www.ncbi.nlm.nih.gov/pubmed/5479453 (Accessed: 3 October 2019).
2. NAGAMACHI, S. et al. (2018) ‘Dietary L-serine modifies free amino acid composition of maternal milk and lowers the body weight of the offspring in mice’, Journal of Veterinary Medical Science, 80(2), pp. 235–241. doi: 10.1292/jvms.17-0577. 3.Grant GA. D-3-Phosphoglycerate Dehydrogenase. Front Mol Biosci. 2018 Dec 13;5:110. doi: 10.3389/fmolb.2018.00110. PMID: 30619878; PMCID: PMC6300728. |
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