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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
ycbLHypothetical protein ycbL. TREMBL:Q7P1X5-63% identity. Interpro:IPR001279-Blactamase like Pfam-GlyoxylaseII family relationship. Phosphoribosylglycinamide synthetase,Respiratory chain NADH dehydrogenase; KH domain and RTX toxin acyltransferase family relationship. ispD: 4-diphosphocytidyl-2C-methyl-D-ery; High confidence in function and specificity. (252 aa)    
Predicted Functional Partners:
gloA2
Lactoylglutathione lyase; Glyoxalase I catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. Similar to trembl|Q9HY85 (74%) and to sprot|LGUL_NEIMA (70%). Pfam (PF00903): Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily ProDom (PD002334): Glyoxalase I; High confidence in function and specificity.
  
 
 0.885
gloA1
Glyoxalase I (lactoylglutathione lyase) catalyzes the first step of the glyoxal pathway in the following reaction: glutathione + methylglyoxal = (R)-S-lactoylglutathione,; Function unclear.
    
  0.884
azo1211
Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs.
 
  
  0.667
imp
Inositol-1(or4)-monophosphatase 3IMPase3)(IMP3)(Inositol monophosphatase 3).Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides. 26% Inositol_P. Pfam:PF00459; Inositol_P; 1; High confidence in function and specificity.
       0.636
azo2999
Conserved hypothetical secreted protein. Homology to NE2572 of N.europaea of 46% (tremble:Q82RZ3). Has PF05951, Bacterial protein of unknown function (DUF882);IPR010275; This family consists of a series of hypothetical bacterial proteins of unknown function. Signal Peptide Present. No TMH present; Conserved hypothetical protein.
  
    0.630
azo3948
Putative DNA-directed polymerase III; Excinuclease cho (EC 3.1.25.-) (Endonuclease cho) (UvrC homolog protein). Incises the DNA at the 3 side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than uvrC. Not able to incise the 5 site of a lesion. When a lesion remains because uvrC is not able to induce the 3 incision cho incises the DNA. Then uvrC makes the 5 incision. The combined action of cho and uvrC broadens the substrate range of nucleotide excision repair (By similarity); Specificity unclear.
    
 0.628
gloB1
Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid.
     
 0.613
gloB2
Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid.
     
 0.613
azo1166
Conserved hypothetical iron-sulfur binding oxidase. Homology to pa4772 of P. aeruginosa of 53% (pir|H83050) InterPro: FAD linked oxidase C-terminal (IPR004413) Pfam: FAD binding domain; Fad linked oxidase, C-terminal domain Tigrfam: glcD: glycolate oxidase subunit GlcD no signal peptide no TMHs; Family membership.
    
 0.607
rph
Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
     
 0.601
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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