STRINGSTRING
ARJ30325.1 ARJ30325.1 cysK cysK ARJ30885.1 ARJ30885.1 ARJ28565.1 ARJ28565.1 pcrB pcrB metK metK ribE ribE ribH ribH hemC hemC ARJ29682.1 ARJ29682.1 aroA aroA miaA miaA ARJ29917.1 ARJ29917.1 ctaB ctaB menA menA ARJ30647.1 ARJ30647.1 thiE thiE murA-2 murA-2 murA murA ARJ28884.1 ARJ28884.1 ARJ28857.1 ARJ28857.1
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:
ARJ30325.1FosB/FosD family fosfomycin resistance thiol transferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (139 aa)
cysKCysteine synthase A; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the cysteine synthase/cystathionine beta- synthase family. (310 aa)
ARJ30885.1Cysteine synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. (298 aa)
ARJ28565.1Dehydrosqualene synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. (287 aa)
pcrBGeranylgeranylglyceryl/heptaprenylglyceryl phosphate synthase; Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond- formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. (230 aa)
metKMethionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. (398 aa)
ribECatalyzes the formation of riboflavin from 6,7-dimethyl-8-(1-D-ribityl)lumazine; Derived by automated computational analysis using gene prediction method: Protein Homology. (210 aa)
ribH6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin; Belongs to the DMRL synthase family. (152 aa)
hemCHydroxymethylbilane synthase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. (310 aa)
ARJ29682.1Geranyl transferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FPP/GGPP synthase family. (294 aa)
aroA3-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. (431 aa)
miaAtRNA dimethylallyltransferase; Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family. (316 aa)
ARJ29917.1Isoprenyl transferase; Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. (253 aa)
ctaBProtoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (303 aa)
menA1,4-dihydroxy-2-naphthoate polyprenyltransferase; Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK); Belongs to the MenA family. Type 1 subfamily. (312 aa)
ARJ30647.1Dihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. (267 aa)
thiEThiamine phosphate synthase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Belongs to the thiamine-phosphate synthase family. (212 aa)
murA-2UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine; Belongs to the EPSP synthase family. MurA subfamily. (421 aa)
murAUDP-N-acetylglucosamine 1-carboxyvinyltransferase; Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine; Belongs to the EPSP synthase family. MurA subfamily. (422 aa)
ARJ28884.1O-acetylhomoserine aminocarboxypropyltransferase; Catalyzes the formation of L-methionine and acetate from O-acetyl-L-homoserine and methanethiol; Derived by automated computational analysis using gene prediction method: Protein Homology. (426 aa)
ARJ28857.1Thiamine phosphate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. (196 aa)
Your Current Organism:
Staphylococcus lugdunensis
NCBI taxonomy Id: 28035
Other names: ATCC 43809, CCUG 25348, CIP 103642, DSM 4804, LMG 13346, LMG:13346, NCTC 12217, NRRL B-14774, S. lugdunensis, strain N860297
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.