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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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[Homology]
Score
azo0481Conserved hypothetical protein; Putative translation initiation inhibitor yjgF family. (117 aa)    
Predicted Functional Partners:
pheA
Bifunctional chorismate mutase/prephenate dehydratase P-protein, pheA,; High confidence in function and specificity.
    
 0.670
azo0482
Conserved hypothetical membrane protein. Homology to yqaA of Nitrosomonas europaea of 50% (trembl|Q82TH7(SRS)) No domains predicted. Signal peptide present. TMHMM2 reporting presence of 2 TMH's; Conserved hypothetical protein.
       0.650
tyrB
Probable aromatic-amino-acid aminotransferase. Homology to tyrB of E. coli of 52% (sprot|TYRB_ECO). Is involved in biosynthesis of phe, tyr, asp and leu. Catalyse the reactiion: an aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + l-glutamate. Pfam: Aminotransferase class I and II no signal peptide no TMHs; High confidence in function and specificity.
   
  0.604
pabB
Para-aminobenzoate synthase component I (EC 4.1.3.-) (ADC synthase). CATALYZES THE BIOSYNTHESIS OF 4-AMINO-4-DEOXYCHORISMATE (ADC) FROM CHORISMATE AND GLUTAMINE. InterPro: Anthranilate synthase component I and chorismate binding enzyme pabB: para-aminobenzoate synthase component I; Specificity unclear.
    
 0.576
tim
Putative triosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family.
  
 
 0.541
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.
  
 
 0.512
azo0480
Conserved hypothetical irons-sulfur binding oxidase. Homology to cv4235 of C. violaceum of 70% (trembl|Q7NQA5) Pfam: FAD binding domain; FAD linked oxidase, Cterminal domain Tigrfam: glcD: glycolate oxidase subunit GlcD no signal peptide no TMHs; Family membership.
       0.506
azo0483
Conserved hypothetical secreted protein. Homology to PA4874 of P.aeruginosa of 36% (trembl|Q9HUT9(SRS)) No domains predicted. Signal petide present. No TMH present; Conserved hypothetical protein.
       0.444
nnrD
Conserved hypothetical protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair o [...]
  
    0.420
fusA1
Putative elongation factor EF-G. Homology to FusA of E. coli of 29% (sprot|EFG_ECOLI(SRS)) This protein promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome. Interpro: Elongation factor G, C-terminus (IPR000640); Elongation factor Tu domain 2 (IPR004161); GTP-binding elongation factor (IPR000795); ATP/GTP-binding site motifA (P-loop) (IPR001687) Tigrfam: EF-G: translation elongation factor G Pfam: Elongation factor Tu domain 2; Elongation factor Tu GTP binding domain; Elongation factor G C-terminus no signal peptide no TMHs [...]
    
  0.405
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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