STRINGSTRING
folC folC gyrB gyrB gyrA gyrA embC embC embC-2 embC-2 embB embB embC-3 embC-3 eryK eryK eryCII eryCII eryCIII eryCIII eryG eryG eryF eryF metK metK inhA inhA metK-2 metK-2 katG katG embC-4 embC-4 embC-5 embC-5 embC-6 embC-6 SACE_5599 SACE_5599 mutB mutB atpE atpE rplC rplC rpsL rpsL rpoB rpoB
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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
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:
folCFolylpolyglutamate synthase; Belongs to the folylpolyglutamate synthase family. (455 aa)
gyrBDNA gyrase subunit B; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. (630 aa)
gyrADNA gyrase subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. (831 aa)
embCProbable arabinosyltransferase, membrane protein. (1042 aa)
embC-2Integral membrane indolylacetylinositol arabinosyltransferase EmbC (arabinosylindolylacetylinositol synthase). (1043 aa)
embBArabinosyl transferase. (999 aa)
embC-3Arabinosyl transferase. (1111 aa)
eryKCytochrome P450 Erythromycin B/D C-12 hydroxylase; Responsible for the C-12 hydroxylation of the macrolactone ring of erythromycin. Thus, EryK catalyzes the hydroxylation of erythromycin D (ErD) at the C-12 position to produce erythromycin C (ErC). Erythromycin B (ErB) is not a substrate for this enzyme. (397 aa)
eryCIITDP-4-keto-6-deoxy-glucose 3,4-isomerase; Involved in the erythromycin biosynthesis pathway. Acts by forming a complex and stabilizing the desosaminyl transferase EryCIII. (361 aa)
eryCIIIGlycosyl transferase, NDP-D-desosamine : 3-L-mycarosyl erythronolide B; Catalyzes the conversion of alpha-L-mycarosylerythronolide B into erythromycin D in the erythromycin biosynthesis pathway. (421 aa)
eryGErythromycin C methlytransferase; S-adenosyl-L-methionine-dependent O-methyltransferase that catalyzes the last step in the erythromycin biosynthesis pathway. Methylates the position 3 of the mycarosyl moiety of erythromycin C, forming the most active form of the antibiotic, erythromycin A. Can also methylate the precursor erythromycin D, forming erythromycin B. (306 aa)
eryF6-deoxyerythronolide B hydroxylase (6-DEB hydroxylase); Catalyzes the conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB. Requires the participation of a ferredoxin and a ferredoxin reductase for the transfer of electrons from NADPH to the monooxygenase. (404 aa)
metKMethionine adenosyltransferase 1 (AdoMet synthetase); 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. (393 aa)
inhAEnoyl-[acyl-carrier-protein] reductase. (252 aa)
metK-2Putative S-adenosylmethionine synthetase; 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. (387 aa)
katGCatalase/peroxidase HPI; Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity; Belongs to the peroxidase family. Peroxidase/catalase subfamily. (737 aa)
embC-4Putative arabinosyl transferase. (392 aa)
embC-5Arabinosyl transferase. (1099 aa)
embC-6Arabinosyl transferase. (1098 aa)
SACE_5599Conserved hypothetical protein present in several antibiotic biosynthetic clusters. (184 aa)
mutBmethylmalonyl-CoA mutase (MCM). (764 aa)
atpEATP synthase C chain; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (88 aa)
rplC50S ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family. (216 aa)
rpsL30S ribosomal protein S12; With S4 and S5 plays an important role in translational accuracy. (124 aa)
rpoBDNA-directed RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. (1164 aa)
Your Current Organism:
Saccharopolyspora erythraea
NCBI taxonomy Id: 405948
Other names: S. erythraea NRRL 2338, Saccharopolyspora erythraea ATCC 11635, Saccharopolyspora erythraea DSM 40517, Saccharopolyspora erythraea JCM 4748, Saccharopolyspora erythraea NRRL 2338, Saccharopolyspora erythraea str. NRRL 2338, Saccharopolyspora erythraea strain NRRL 2338
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