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Links from Protein

Items: 9

1.

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain

GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold. [1]. 7578111. Crystal structure of glycosomal glyceraldehyde-3-phosphate. dehydrogenase from Leishmania mexicana: implications for. structure-based drug design and a new position for the inorganic. phosphate binding site.. Kim H, Feil IK, Verlinde CL, Petra PH, Hol WG;. Biochemistry 1995;34:14975-14986. (from Pfam)

GO Terms:
Molecular Function:
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor (GO:0016620)
Date:
2024-08-14
Family Accession:
NF014818.5
Method:
HMM
2.

glyceraldehyde 3-phosphate dehydrogenase NAD-binding domain-containing protein

GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold. [1]. 7578111. Crystal structure of glycosomal glyceraldehyde-3-phosphate. dehydrogenase from Leishmania mexicana: implications for. structure-based drug design and a new position for the inorganic. phosphate binding site.. Kim H, Feil IK, Verlinde CL, Petra PH, Hol WG;. Biochemistry 1995;34:14975-14986. (from Pfam)

GO Terms:
Molecular Function:
NAD binding (GO:0051287)
Date:
2024-08-14
Family Accession:
NF012274.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

erythrose-4-phosphate dehydrogenase

erythrose-4-phosphate dehydrogenase catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate to 4-phosphoerythronate

Date:
2018-08-23
Family Accession:
11486684
Method:
Sparcle
8.

erythrose-4-phosphate dehydrogenase

Gene:
epd
GO Terms:
Biological Process:
pyridoxal phosphate biosynthetic process (GO:0042823)
Molecular Function:
erythrose-4-phosphate dehydrogenase activity (GO:0048001)
Molecular Function:
NAD binding (GO:0051287)
Date:
2021-09-22
Family Accession:
NF010058.0
Method:
HMM
9.

erythrose-4-phosphate dehydrogenase

This HMM represents the small clade of dehydrogenases in gamma-proteobacteria which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose [1]. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase, whose substrate differs only in the lack of one carbon relative to E4P. Accordingly, this model is very close to the corresponding models for GAPDH, and those sequences which hit above trusted here invariably hit between trusted and noise to the GAPDH model (TIGR01534). Similarly, it may be found that there are species outside of the gamma proteobacteria which synthesize pyridoxine and have more than one aparrent GAPDH gene of which one may have E4PD activity - this may necessitate a readjustment of these models. Alternatively, some of the GAPDH enzymes may prove to be bifunctional in certain species.

Gene:
epd
GO Terms:
Cellular Component:
cytoplasm (GO:0005737)
Biological Process:
pyridoxal phosphate biosynthetic process (GO:0042823)
Molecular Function:
erythrose-4-phosphate dehydrogenase activity (GO:0048001)
Molecular Function:
NAD binding (GO:0051287)
Date:
2024-05-29
Family Accession:
TIGR01532.1
Method:
HMM
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