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AGC68719.1 AGC68719.1 nadC nadC hpt hpt upp upp pncB pncB hisG hisG pdp pdp purF2 purF2 hisF2 hisF2 punA punA ylmD ylmD trpD trpD hisF1 hisF1 hisH hisH xpt xpt tgt tgt purF1 purF1 AGC67662.1 AGC67662.1 AGC67429.1 AGC67429.1
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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:
AGC68719.1Hypothetical protein. (214 aa)
nadCNicotinate-nucleotide pyrophosphorylase; Carboxylating; Belongs to the NadC/ModD family. (276 aa)
hptHypoxanthine-guanine phosphoribosyltransferase Hpt; Belongs to the purine/pyrimidine phosphoribosyltransferase family. (172 aa)
uppUracil phosphoribosyltransferase Upp; Catalyzes the conversion of uracil and 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) to UMP and diphosphate. (212 aa)
pncBNicotinate phosphoribosyltransferase PncB; 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. (487 aa)
hisGATP phosphoribosyltransferase HisG; 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. (214 aa)
pdpPyrimidine-nucleoside phosphorylase Pdp. (433 aa)
purF2Amidophosphoribosyltransferase PurF; In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family. (466 aa)
hisF2Imidazole 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. (255 aa)
punAPurine nucleoside phosphorylase 1; 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)
ylmDLaccase domain-containing protein YlmD; Belongs to the multicopper oxidase YfiH/RL5 family. (265 aa)
trpDAnthranilate phosphoribosyltransferase TrpD; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). (336 aa)
hisF1Imidazole 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. (251 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. (201 aa)
xptXanthine phosphoribosyltransferase Xpt; 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. (191 aa)
tgtQueuine tRNA-ribosyltransferase Tgt; 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 fo [...] (377 aa)
purF1Amidophosphoribosyltransferase PurF; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. (471 aa)
AGC67662.1Hypothetical protein. (288 aa)
AGC67429.1Phage head morphogenesis protein, SPP1 gp7 family. (443 aa)
Your Current Organism:
Thermoclostridium stercorarium
NCBI taxonomy Id: 1121335
Other names: Clostridium stercorarium subsp. stercorarium DSM 8532, T. stercorarium subsp. stercorarium DSM 8532, Thermoclostridium stercorarium subsp. stercorarium DSM 8532
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