STRINGSTRING
hisG hisG AGB01161.1 AGB01161.1 AGB01423.1 AGB01423.1 hisD hisD hisC hisC hisE hisE hisI hisI AGB02351.1 AGB02351.1 hisH hisH aroA aroA aroA-2 aroA-2 aroB aroB AGB02622.1 AGB02622.1 AGB02623.1 AGB02623.1 aroA-3 aroA-3 aroE aroE aroC aroC AGB02787.1 AGB02787.1 hisH-2 hisH-2 hisB hisB hisA hisA hisG-2 hisG-2 hisF hisF trpE trpE AGB03867.1 AGB03867.1 trpD trpD AGB03869.1 AGB03869.1 trpF trpF trpB-2 trpB-2 trpA trpA AGB03873.1 AGB03873.1
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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
Others
textmining
co-expression
protein homology
Your Input:
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. (294 aa)
AGB01161.1PFAM: Chorismate mutase type II; TIGRFAM: chorismate mutase, archaeal type. (94 aa)
AGB01423.1PHP family phosphohydrolase, histidinol phosphatase; PFAM: PHP domain. (217 aa)
hisDHistidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. (414 aa)
hisCPFAM: Aminotransferase class I and II; TIGRFAM: histidinol-phosphate aminotransferase. (352 aa)
hisEPFAM: Phosphoribosyl-ATP pyrophosphohydrolase; TIGRFAM: phosphoribosyl-ATP pyrophosphohydrolase. (100 aa)
hisIphosphoribosyl-AMP cyclohydrolase; Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. (122 aa)
AGB02351.1Imidazoleglycerol-phosphate synthase; PFAM: Histidine biosynthesis protein; TIGRFAM: imidazoleglycerol phosphate synthase, cyclase subunit; manually curated; Belongs to the HisA/HisF family. (251 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. (200 aa)
aroAPutative phospho-2-dehydro-3-deoxyheptonate aldolase; Catalyzes a transaldol reaction between 6-deoxy-5- ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7- dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. (262 aa)
aroA-2Putative phospho-2-dehydro-3-deoxyheptonate aldolase; Catalyzes a transaldol reaction between 6-deoxy-5- ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7- dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. (261 aa)
aroBPutative alternative 3-dehydroquinate synthase; Catalyzes the oxidative deamination and cyclization of 2- amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3- dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis; Belongs to the archaeal-type DHQ synthase family. (328 aa)
AGB02622.1PFAM: Prephenate dehydrogenase. (274 aa)
AGB02623.1PFAM: Prephenate dehydratase; ACT domain. (265 aa)
aroA-33-phosphoshikimate 1-carboxyvinyltransferase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. (421 aa)
aroEShikimate 5-dehydrogenase; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). (463 aa)
aroCChorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. (329 aa)
AGB02787.1PLP-dependent enzyme, histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase; PFAM: Aminotransferase class I and II. (335 aa)
hisH-2Imidazole 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. (201 aa)
hisBPFAM: Imidazoleglycerol-phosphate dehydratase. (192 aa)
hisAPFAM: Histidine biosynthesis protein; TIGRFAM: phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase. (236 aa)
hisG-2ATP 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. (305 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. (268 aa)
trpEAnthranilate synthase component I; Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentr [...] (508 aa)
AGB03867.1PFAM: Glutamine amidotransferase class-I; TIGRFAM: glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase. (193 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). (339 aa)
AGB03869.1PFAM: Indole-3-glycerol phosphate synthase. (251 aa)
trpFPFAM: N-(5'phosphoribosyl)anthranilate (PRA) isomerase; Belongs to the TrpF family. (196 aa)
trpB-2Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (391 aa)
trpATryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. (263 aa)
AGB03873.1Putative hemolysin; PFAM: Domain of unknown function (DUF333). (136 aa)
Your Current Organism:
Methanoregula formicica
NCBI taxonomy Id: 593750
Other names: M. formicica SMSP, Methanomicrobiales archaeon SMSP, Methanoregula formicica SMSP, Methanoregula formicica str. SMSP, Methanoregula formicica strain SMSP
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.