STRINGSTRING
yggS yggS yggT yggT yggU yggU rdgB rdgB yggW yggW
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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)
yggTConserved hypothetical integral membrane protein. (188 aa)
yggUUPF0235 family protein; Belongs to the UPF0235 family. (96 aa)
rdgBdITP/XTP pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Can also efficiently hydrolyze 2'- deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP). Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. To a much lesser extent, is als [...] (197 aa)
yggWHemN family putative oxidoreductase; Probably acts as a heme chaperone, transferring heme to the NarI subunit of the respiratory enzyme nitrate reductase; transfer may be stimulated by NADH. Binds one molecule of heme per monomer, possibly covalently. Heme binding is not affected by either [4Fe-4S] or S- adenosyl-L-methionine (SAM)-binding. Does not have coproporphyrinogen III dehydrogenase activity in vitro. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (Probable). (378 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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