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hisF hisF cobT cobT SSIL_1421 SSIL_1421 tgt tgt apt apt deoD deoD ylmD ylmD pdp pdp pyrE pyrE pyrR pyrR SSIL_3290 SSIL_3290 upp upp trpD trpD xpt xpt SSIL_0015 SSIL_0015 SSIL_0455 SSIL_0455 purF purF hisG hisG hisH hisH
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second shell of interactors
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proteins of unknown 3D structure
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hisFImidazoleglycerol-phosphate synthase; 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. (252 aa)
cobTNaMN:DMB phosphoribosyltransferase; Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). (352 aa)
SSIL_1421Hypothetical protein. (382 aa)
tgtQueuine/archaeosine 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 ribo [...] (385 aa)
aptAdenine/guanine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. (170 aa)
deoDPurine-nucleoside phosphorylase. (235 aa)
ylmDUncharacterized conserved protein; Belongs to the multicopper oxidase YfiH/RL5 family. (253 aa)
pdpThymidine phosphorylase. (434 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). (210 aa)
pyrRPyrimidine operon attenuation protein/uracil phosphoribosyltransferase; Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant; Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily. (180 aa)
SSIL_3290Predicted amidophosphoribosyltransferase. (201 aa)
uppUracil phosphoribosyltransferase; Catalyzes the conversion of uracil and 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) to UMP and diphosphate. (209 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). (345 aa)
xptAdenine/guanine phosphoribosyltransferase; Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. (190 aa)
SSIL_0015Hypoxanthine-guanine phosphoribosyltransferase; Belongs to the purine/pyrimidine phosphoribosyltransferase family. (180 aa)
SSIL_0455Nicotinic acid phosphoribosyltransferase; Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D- ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Belongs to the NAPRTase family. (489 aa)
purFGlutamine phosphoribosylpyrophosphate amidotransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. (472 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. Short subfamily. (207 aa)
hisHGlutamine amidotransferase; 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. (206 aa)
Your Current Organism:
Solibacillus silvestris
NCBI taxonomy Id: 1002809
Other names: S. silvestris StLB046, Solibacillus silvestris StLB046, Solibacillus silvestris str. StLB046, Solibacillus silvestris strain StLB046
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