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AFG37193.1 AFG37193.1 AFG37266.1 AFG37266.1 AFG37505.1 AFG37505.1 tgt tgt AFG37637.1 AFG37637.1 AFG37946.1 AFG37946.1 apt apt purF purF AFG38191.1 AFG38191.1 AFG38266.1 AFG38266.1 hisF hisF hisH hisH trpD trpD AFG38857.1 AFG38857.1
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AFG37193.1Putative nicotinate 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. (490 aa)
AFG37266.1Purine 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. (276 aa)
AFG37505.1Pyrimidine-nucleoside phosphorylase; PFAM: Glycosyl transferase family, a/b domain; Pyrimidine nucleoside phosphorylase C-terminal domain; Glycosyl transferase family, helical bundle domain; TIGRFAM: pyrimidine-nucleoside phosphorylase; manually curated. (437 aa)
tgttRNA-guanine transglycosylase, queuosine-34-forming; 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 [...] (375 aa)
AFG37637.1PFAM: Phage portal protein; TIGRFAM: phage portal protein, HK97 family. (415 aa)
AFG37946.1Hypothetical protein; PFAM: Multi-copper polyphenol oxidoreductase laccase. (239 aa)
aptPRPP-binding protein, adenine/guanine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. (180 aa)
purFAmidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. (473 aa)
AFG38191.1Uracil phosphoribosyltransferase. (355 aa)
AFG38266.1ATP 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. (206 aa)
hisFImidazoleglycerol phosphate synthase, cyclase subunit; 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. (259 aa)
hisHImidazole glycerol phosphate synthase, glutamine amidotransferase subunit; 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)
trpDGlutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). (549 aa)
AFG38857.1Nicotinate-nucleotide pyrophosphorylase; PFAM: Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl transferase, N-terminal domain; TIGRFAM: nicotinate-nucleotide pyrophosphorylase; Belongs to the NadC/ModD family. (293 aa)
Your Current Organism:
Spirochaeta africana
NCBI taxonomy Id: 889378
Other names: S. africana DSM 8902, Spirochaeta africana DSM 8902, Spirochaeta africana Z-7692, Spirochaeta africana str. DSM 8902, Spirochaeta africana strain DSM 8902
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