STRINGSTRING
yggS yggS pdxK pdxK dxs dxs ybhA ybhA ydbC ydbC pdxY pdxY pdxH pdxH pdxB pdxB glyA glyA
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Your Input:
yggSUPF0001 family protein, PLP-binding; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis. May have a carrier function to deliver PLP to the target enzymes or a protective function so that PLP does not inactivate essential lysines in proteins. Does not have amino acid racemase activity. (234 aa)
pdxKPyridoxal-pyridoxamine kinase/hydroxymethylpyrimidine kinase; B6-vitamer kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxine (PN), pyridoxal (PL), and pyridoxamine (PM), forming their respective 5'-phosphorylated esters, i.e. PNP, PLP and PMP. Belongs to the pyridoxine kinase family. PdxK subfamily. (283 aa)
dxs1-deoxyxylulose-5-phosphate synthase, thiamine triphosphate-binding, FAD-requiring; Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D- xylulose-5-phosphate (DXP). (620 aa)
ybhAPyridoxal phosphate (PLP) phosphatase; Catalyzes the dephosphorylation of pyridoxal-phosphate (PLP). Can also hydrolyze erythrose-4-phosphate (Ery4P) and fructose-1,6-bis- phosphate (Fru1,6bisP); Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family. (272 aa)
ydbCPutative NAD(P)-binding oxidoreductase; Catalyzes the NAD(P)H-dependent reduction of pyridoxal to pyridoxine in vitro. Is not able to reduce 4-pyridoxate, and to oxidize pyridoxine or pyridoxamine. Has Kemp eliminase activity towards the non-physiological substrate 5-nitrobenzisoxazole, producing 4-nitro-2-cyanophenol; this activity is not considered to be physiologically relevant. Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily. (286 aa)
pdxYPyridoxamine kinase; Pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP in vivo, but shows very low activity compared to PdxK. Displays a low level of pyridoxine kinase activity when overexpressed, which is however not physiologically relevant. (287 aa)
pdxHPyridoxine 5'-phosphate oxidase; Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). (218 aa)
pdxBErythronate-4-phosphate dehydrogenase; Catalyzes the oxidation of erythronate-4-phosphate to 3- hydroxy-2-oxo-4-phosphonooxybutanoate; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily. (378 aa)
glyASerine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of allothreonine and 3-phenylserine. Also catalyzes the irreversible conversion of 5,10-m [...] (417 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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