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A0A066WS52 A0A066WS52 A0A066WJE2 A0A066WJE2 A0A066WNQ0 A0A066WNQ0 A0A066WGI2 A0A066WGI2 A0A066WHJ6 A0A066WHJ6 A0A066WIT3 A0A066WIT3 A0A066V713 A0A066V713 A0A066VKA3 A0A066VKA3 A0A066VN15 A0A066VN15 A0A066VWS6 A0A066VWS6 A0A066VYR2 A0A066VYR2 A0A066VZP3 A0A066VZP3 A0A066W572 A0A066W572 A0A066W7W3 A0A066W7W3 A0A066W9J1 A0A066W9J1
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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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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Your Input:
A0A066WS52S-methyl-5'-thioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. (307 aa)
A0A066WJE2CAP10 domain-containing protein. (409 aa)
A0A066WNQ0Purine and uridine phosphorylase. (321 aa)
A0A066WGI2Glutamine amidotransferase type-1 domain-containing protein; Belongs to the HisA/HisF family. (628 aa)
A0A066WHJ6Amidophosphoribosyltransferase. (584 aa)
A0A066WIT3Uncharacterized protein. (574 aa)
A0A066V713Putative ATP phosphoribosyltransferase. (335 aa)
A0A066VKA3Adenine phosphoribosyltransferase. (184 aa)
A0A066VN15Orotate phosphoribosyltransferase. (243 aa)
A0A066VWS6Nicotinate-nucleotide pyrophosphorylase [carboxylating]; Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family. (327 aa)
A0A066VYR2Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. (323 aa)
A0A066VZP3Uncharacterized protein. (263 aa)
A0A066W572Initiator tRNA phosphoribosyl transferase. (546 aa)
A0A066W7W3Thiamine thiazole synthase; Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5- (2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron- dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance; Belongs to the T [...] (320 aa)
A0A066W9J1Putative uracil phosphoribosyltransferase. (221 aa)
Your Current Organism:
Tilletiaria anomala
NCBI taxonomy Id: 1037660
Other names: T. anomala UBC 951, Tilletiaria anomala ATCC 24038, Tilletiaria anomala CBS 436.72, Tilletiaria anomala UBC 951
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