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ADZ76931.1 ADZ76931.1 ADZ77299.1 ADZ77299.1 ADZ77716.1 ADZ77716.1 ADZ78786.1 ADZ78786.1 apt apt mtgA mtgA tgt tgt ADZ79473.1 ADZ79473.1 ADZ79535.1 ADZ79535.1 pncB pncB trpD trpD pyrE pyrE ADZ80099.1 ADZ80099.1 hisG hisG hisH hisH hisF hisF
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query proteins and first shell of interactors
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second shell of interactors
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filled nodes:
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ADZ76931.1Purine 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. (272 aa)
ADZ77299.1PFAM: Phosphoribosyltransferase; KEGG: phe:Phep_4038 uracil phosphoribosyltransferase. (214 aa)
ADZ77716.1PFAM: Phosphoribosyltransferase; KEGG: phe:Phep_3621 bifunctional pyrimidine regulatory protein PyrR uracil phosphoribosyltransferase. (171 aa)
ADZ78786.1KEGG: phe:Phep_1174 uracil phosphoribosyltransferase; PFAM: Phosphoribosyltransferase. (183 aa)
aptAdenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. (175 aa)
mtgAMonofunctional biosynthetic peptidoglycan transglycosylase; Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors; Belongs to the glycosyltransferase 51 family. (261 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 [...] (376 aa)
ADZ79473.1KEGG: phe:Phep_3079 AMP nucleosidase; TIGRFAM: AMP nucleosidase, putative; PFAM: Nucleoside phosphorylase domain. (272 aa)
ADZ79535.1TIGRFAM: Nicotinate-nucleotide pyrophosphorylase; KEGG: phe:Phep_1198 nicotinate-nucleotide pyrophosphorylase; PFAM: Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl transferase, N-terminal; Belongs to the NadC/ModD family. (292 aa)
pncBNicotinate phosphoribosyltransferase; Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP; Belongs to the NAPRTase family. (394 aa)
trpDAnthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). (334 aa)
pyrEOrotate phosphoribosyltransferase; Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). (216 aa)
ADZ80099.1KEGG: dsy:DSY0804 hypothetical protein. (190 aa)
hisGATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Belongs to the ATP phosphoribosyltransferase family. Long subfamily. (283 aa)
hisHImidazole glycerol phosphate synthase subunit hisH; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. (196 aa)
hisFImidazole glycerol phosphate synthase subunit hisF; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. (262 aa)
Your Current Organism:
Sphingobacterium sp. 21
NCBI taxonomy Id: 743722
Other names: S. sp. 21
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