STRINGSTRING
gltX gltX sat sat ANA79505.1 ANA79505.1 trpS trpS tyrS tyrS cysH cysH cysS cysS argG argG glnS glnS trpS-2 trpS-2 tilS tilS argS argS metG metG ANA80422.1 ANA80422.1 ANA80423.1 ANA80423.1 ANA80562.1 ANA80562.1 nadE nadE guaA guaA ANA80975.1 ANA80975.1 queC queC ANA81384.1 ANA81384.1 ANA81389.1 ANA81389.1 valS valS mnmA mnmA nadD nadD leuS leuS thiI thiI ileS ileS tyrS-2 tyrS-2 lysS-2 lysS-2 metG-2 metG-2 panC panC ANA82179.1 ANA82179.1 ANA82365.1 ANA82365.1 ANA82776.1 ANA82776.1 gluQ gluQ ANA83126.1 ANA83126.1 tmcAL tmcAL coaD coaD
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:
gltXglutamate--tRNA ligase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). (487 aa)
satATP sulfurylase; ATPS; converts ATP and sulfate to 5'phosphosulfate and pyrophosphate; in some organisms this enzyme is involved in the incorporation of inorganic sulfate while in others it is involved in the production of ATP in the reverse direction; the enzyme from Thermus thermophilus is dimeric and binds a zinc ion that is coordinated by cysteine and histidine residues that are not found in all related proteins but is found in some thermophilic organisms; Derived by automated computational analysis using gene prediction method: Protein Homology. (389 aa)
ANA79505.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (674 aa)
trpStryptophan--tRNA ligase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (328 aa)
tyrStyrosine--tRNA ligase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily. (419 aa)
cysHPhosphoadenosine phosphosulfate reductase; Reduction of activated sulfate into sulfite. Belongs to the PAPS reductase family. CysH subfamily. (230 aa)
cysScysteine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family. (468 aa)
argGArgininosuccinate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the argininosuccinate synthase family. Type 1 subfamily. (410 aa)
glnSglutamine--tRNA ligase; Catalyzes a two-step reaction, first charging a glutamine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; Derived by automated computational analysis using gene prediction method: Protein Homology. (572 aa)
trpS-2tryptophan--tRNA ligase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (327 aa)
tilStRNA(Ile)-lysidine synthetase; Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Belongs to the tRNA(Ile)-lysidine synthase family. (476 aa)
argSarginine--tRNA ligase; Catalyzes a two-step reaction, first charging an arginine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; class-I aminoacyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology. (559 aa)
metGmethionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (546 aa)
ANA80422.1Electron transfer flavoprotein subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. (325 aa)
ANA80423.1Electron transfer flavoprotein subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology. (255 aa)
ANA80562.1Histidine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (781 aa)
nadENAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source; Belongs to the NAD synthetase family. (269 aa)
guaAGlutamine-hydrolyzing GMP synthase; Catalyzes the synthesis of GMP from XMP. (512 aa)
ANA80975.1Universal stress protein UspA; Derived by automated computational analysis using gene prediction method: Protein Homology. (144 aa)
queC7-cyano-7-deazaguanine synthase QueC; Catalyzes the ATP-dependent conversion of 7-carboxy-7- deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). (225 aa)
ANA81384.1Asparagine synthetase B; Derived by automated computational analysis using gene prediction method: Protein Homology. (614 aa)
ANA81389.1arginine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family. (620 aa)
valSvaline--tRNA ligase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. (889 aa)
mnmAtRNA 2-thiouridine(34) synthase MnmA; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. (371 aa)
nadDNicotinic acid mononucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). (196 aa)
leuSleucine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family. (813 aa)
thiItRNA 4-thiouridine(8) synthase ThiI; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. (412 aa)
ileSisoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily. (1029 aa)
tyrS-2tyrosine--tRNA ligase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily. (417 aa)
lysS-2lysine--tRNA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family. (519 aa)
metG-2methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. (662 aa)
panCPantoate--beta-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. (296 aa)
ANA82179.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (217 aa)
ANA82365.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (111 aa)
ANA82776.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (202 aa)
gluQtRNA glutamyl-Q synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. (325 aa)
ANA83126.1Bifunctional riboflavin kinase/FMN adenylyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ribF family. (317 aa)
tmcALNucleotidyltransferase; Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac- AMP) and then transfers the acetyl group to tRNA to form ac(4)C34. (411 aa)
coaDPantetheine-phosphate adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family. (171 aa)
Your Current Organism:
Paenibacillus glucanolyticus
NCBI taxonomy Id: 59843
Other names: ATCC 49278, Bacillus glucanolyticus, CCUG 28523, CIP 106935, DSM 5162, HSCC 171, IFO 15330, LMG 12239, LMG:12239, NBRC 15330, NCIMB 12809, NRRL B-14679, P. glucanolyticus
Server load: low (28%) [HD]