STRINGSTRING
queE queE VS_1141 VS_1141 VS_1050 VS_1050 moaA moaA miaB miaB lipA lipA rlmN rlmN VS_0475 VS_0475 VS_0243 VS_0243 VS_0116 VS_0116 VS_3093 VS_3093 VS_II0252 VS_II0252 VS_II0290 VS_II0290 VS_II0455 VS_II0455 VS_II0712 VS_II0712 VS_2689 VS_2689 VS_II0868 VS_II0868 bioB bioB
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:
queEOrganic radical activating enzyme; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. (222 aa)
VS_1141Hypothetical protein. (792 aa)
VS_1050Pyruvate formate-lyase 1-activating enzyme; Activation of pyruvate formate-lyase under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine; Belongs to the organic radical-activating enzymes family. (246 aa)
moaAMolybdenum cofactor biosynthesis protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (334 aa)
miaBHypothetical protein; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. (474 aa)
lipALipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. (321 aa)
rlmNPredicted Fe-S-cluster redox enzyme; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. (380 aa)
VS_0475Putative Fe-S oxidoreductase. (317 aa)
VS_0243Hypothetical protein. (340 aa)
VS_0116Oxygen-independent coproporphyrinogen III oxidase; Belongs to the anaerobic coproporphyrinogen-III oxidase family. (463 aa)
VS_3093ThiH. (375 aa)
VS_II0252Radical SAM. (403 aa)
VS_II0290Oxygen-independent coproporphyrinogen III oxidase. (469 aa)
VS_II0455Pyruvate formate-lyase activating enzyme. (295 aa)
VS_II0712Anaerobic ribonucleoside-triphosphate reductase-activating protein; Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine. (156 aa)
VS_2689Oxygen-independent coproporphyrinogen III oxidase-like protein; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (395 aa)
VS_II0868Arylsulfatase regulator. (443 aa)
bioBBiotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family. (350 aa)
Your Current Organism:
Vibrio tasmaniensis
NCBI taxonomy Id: 575788
Other names: V. tasmaniensis LGP32, Vibrio lentus MEL32, Vibrio splendidus LGP32, Vibrio tasmaniensis LGP32
Server load: low (16%) [HD]