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yliG yliG moaA moaA miaB miaB lipA lipA yggW yggW ygiQ ygiQ yhcC yhcC CAR20116.1 CAR20116.1 yjeK yjeK pflC pflC hemN hemN yfgB yfgB pflA pflA
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.
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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:
yliGPutative AdoMet-dependent methyltransferase, UPF0004 family; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (441 aa)
moaAMolybdopterin biosynthesis protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (329 aa)
miaBIsopentenyl-adenosine A37 tRNA methylthiolase; 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)
lipALipoate 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)
yggWPutative oxidoreductase; 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. (378 aa)
ygiQConserved hypothetical protein; Homologs of previously reported genes of unknown function. (739 aa)
yhcCPutative Fe-S oxidoreductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (309 aa)
CAR20116.1Putative oxygen independent coproporphyrinogen III oxidase (chuW-like); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (445 aa)
yjeKPutative lysine aminomutase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (342 aa)
pflCPyruvate formate lyase II activase; Function experimentally demonstrated in the studied species; enzyme. (292 aa)
hemNCoproporphyrinogen III oxidase, SAM and NAD(P)H dependent, oxygen-independent; Function experimentally demonstrated in the studied species; enzyme; Belongs to the anaerobic coproporphyrinogen-III oxidase family. (457 aa)
yfgBPutative Fe-S containing 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. (384 aa)
pflAPyruvate formate lyase activating enzyme 1; 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)
Your Current Organism:
Escherichia coli IAI39
NCBI taxonomy Id: 585057
Other names: E. coli IAI39
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