STRINGSTRING
glyA glyA purN purN rlmI rlmI tgt tgt metH metH folD folD APB33126.1 APB33126.1 APB33154.1 APB33154.1 APB33182.1 APB33182.1 purU purU APB33460.1 APB33460.1 purH purH APB33695.1 APB33695.1 fmt fmt APB34304.1 APB34304.1 APB34305.1 APB34305.1 APB34639.1 APB34639.1 metF metF APB34989.1 APB34989.1 APB35139.1 APB35139.1
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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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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
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. (420 aa)
purNPhosphoribosylglycinamide formyltransferase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. (206 aa)
rlmIPUA domain-containing protein. (396 aa)
tgtQueuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] (368 aa)
metHMethionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. (1182 aa)
folDMethenyltetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. (291 aa)
APB33126.1Hypothetical protein. (209 aa)
APB33154.1HNH endonuclease. (198 aa)
APB33182.1Hypothetical protein. (494 aa)
purUFormyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). (277 aa)
APB33460.1RDD family protein. (260 aa)
purHBifunctional purine biosynthesis protein purH / phosphoribosylaminoimidazolecarboxamide formyltransferase. (512 aa)
APB33695.1Hypothetical protein. (313 aa)
fmtmethionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. (332 aa)
APB34304.1Urea carboxylase-associated protein 1. (211 aa)
APB34305.1Urea carboxylase-associated protein 2. (262 aa)
APB34639.1Restriction endonuclease. (165 aa)
metFPutative methylenetetrahydrofolate reductase; Belongs to the methylenetetrahydrofolate reductase family. (328 aa)
APB34989.15-formyltetrahydrofolate cyclo-ligase; Belongs to the 5-formyltetrahydrofolate cyclo-ligase family. (170 aa)
APB35139.1Glycine cleavage system aminomethyltransferase T. (352 aa)
Your Current Organism:
Gloeomargarita lithophora
NCBI taxonomy Id: 1188229
Other names: Candidatus Gloeomargarita lithophora D10, G. lithophora Alchichica-D10, Gloeomargarita lithophora Alchichica-D10, Gloeomargarita lithophora PMC 919.15
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