STRINGSTRING
pdp pdp queC queC comB comB deoD deoD ADW21189.1 ADW21189.1 ADW21245.1 ADW21245.1 ADW21333.1 ADW21333.1 ADW21405.1 ADW21405.1 mqnB mqnB cdd cdd queA queA mtnN mtnN ADW22566.1 ADW22566.1 ADW22750.1 ADW22750.1 ADW22751.1 ADW22751.1 hpt hpt ADW22863.1 ADW22863.1 tgt tgt
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.
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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
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
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textmining
co-expression
protein homology
Your Input:
pdpPyrimidine-nucleoside phosphorylase; Pynp. (424 aa)
queCArchaeosine biosynthesis protein QueC; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). Belongs to the QueC family. (206 aa)
comBPutative 2-phosphosulfolactate phosphatase; Belongs to the ComB family. (252 aa)
deoDPurine nucleoside phosphorylase DeoD-type; PNP. (235 aa)
ADW21189.1Phosphoglucomutase/phosphomannomutase. (298 aa)
ADW21245.1Conserved hypothetical protein. (238 aa)
ADW21333.1Purine phosphoribosyltransferase. (154 aa)
ADW21405.1Purine nucleoside phosphorylase I, inosine and guanosine-specific; 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. (275 aa)
mqnBFutalosine nucleosidase; Catalyzes the hydrolysis of futalosine (FL) to dehypoxanthine futalosine (DHFL) and hypoxanthine, a step in the biosynthesis of menaquinone (MK, vitamin K2). (225 aa)
cddCytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family. (116 aa)
queAS-adenosylmethionine:tRNA ribosyltransferase-isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). (344 aa)
mtnNMTA/SAH nucleosidase; Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Belongs to the PNP/UDP phosphorylase family. MtnN subfamily. (221 aa)
ADW22566.1Iron-sulfur cluster-binding protein. (382 aa)
ADW22750.1Adenine phosphoribosyltransferase. (175 aa)
ADW22751.1Putative adenine phosphoribosyltransferase. (173 aa)
hptHypoxanthine phosphoribosyltransferase; Belongs to the purine/pyrimidine phosphoribosyltransferase family. (178 aa)
ADW22863.1Conserved hypothetical integral membrane protein; Involved in the import of queuosine (Q) precursors, required for Q precursor salvage; Belongs to the vitamin uptake transporter (VUT/ECF) (TC 2.A.88) family. Q precursor transporter subfamily. (222 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 [...] (385 aa)
Your Current Organism:
Thermus scotoductus
NCBI taxonomy Id: 743525
Other names: T. scotoductus SA-01, Thermus scotoductus SA-01, Thermus scotoductus str. SA-01, Thermus scotoductus strain SA-01, Thermus sp. SA-01
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