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
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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
azo2613Hypothetical protein, 50% identity (59% simialrity)to TrEMBL;Q92TJ5. Has PF04828, Protein of unknown function (DUF636);IPR006913, GFA;This family of proteins has no known function, but several strongly conserved cysteine residues. Glutathione-dependent formaldehyde-activating enzymes catalyze the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione. All known members of this family contain 5 strongly conserved cysteine residues. NO Signal peptide or TMH present; Function unclear. (133 aa)    
Predicted Functional Partners:
exaA4
Quinoprotein ethanol dehydrogenase precursor (QEDH). Oxidizes primary alcohols and also acts on secondary alcohol, but not highly active on methanol. 37% Bac_PQQ.IPR002372; Bac_PQQ_repeat. Pfam:PF01011; PQQ; 2. Signal peptide:present; High confidence in function and specificity.
     
 0.638
azo2612
GAF/GGDEF-domain containing protein,; Conserved hypothetical protein.
       0.636
adhC
Alcohol dehydrogenase class III (Formaldehyde dehydrogenase (glutathione)). Homology to fdh of E. coli of 72% (trembl|Q59399) CLASS-III ADH IS REMARKABLY INEFFECTIVE IN OXIDIZING ETHANOL BUT IT READILY CATALYZES THE OXIDATION OF LONG-CHAIN PRIMARY ALOCHOLS AND THE OXIDATION OF S-(HYDROXYMETHYL) GLUTATHIONE (BY SIMILARITY). InterPro: Zinc-containing alcohol dehydrogenase superfamily (IPR002085) Zinc-containing alcohol dehydrogenase (IPR002328) Pfam: zinc-binding dehydrogenase Tigrfam: tdh: L-threonine 3-dehydrogenase. no signal peptide. 2 TMHs; High confidence in function and specificity.
    
 0.621
azo3624
Probable esterase; Serine hydrolase involved in the detoxification of formaldehyde.
    
 0.617
azo2616
Lactoylglutathione lyase; Puatative Glyoxalase sub unit, 37% identitcal to TrEMBL;Q89MF5 Has PF00903, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I, catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruv [...]
 
     0.600
gltB
Ferredoxin-dependent glutamate synthase,; Specificity unclear.
     
 0.558
ribAB
GTP cyclohydrolase II; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; Belongs to the DHBP synthase family.
     
  0.551
azo2615
Hypothetical protein,45% similarity to TrEMBL;Q6LHM7. No Good homology over entire length in the DB. No signal Peptide or TMH present; Function unclear.
 
     0.518
qhpA
Probable quinohemoprotein amine dehydrogenase,alpha subunit. Homology to qhpA of P.putida of 50% (gi|18655859|pdb|1JMZ|A(PDB (RCSB))). Quinoproteins are a class of amine-oxidising enzymes that catalyse the oxidation of biological amines, using quinone as a redox cofactor to store reducing equivalents. Quinohemoprotein amine dehydrogenase (QH-AmDH) from bacteria represents a new class of quinoproteins that contains both quinone and one or two hemes as redox active groups. The presence of extra redox active groups allows for intramolecular electron transfer. QH-AmDH is a heterotrimeric e [...]
     
 0.506
gcvT
Glycine cleavage T proteins are part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. The T-protein is an aminomethyl transferase that catalyses the following reaction: (6S)-tetrahydrofolate + S-aminomethyldihydrolipoylprotein = (6R)-5,10-methylenetetrahydrofolate + NH3 + dihydrolipoylprotein Similar to sprot|GCST_NITEU (60%). Pfam: Glycine cleavage T-protein (aminomethyltransferase) TIGRfam (TIGR00528): Glycine cleavage T-protein (aminomethyl transferase); High confidence in function and specificity.
     
  0.505
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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