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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
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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
gloB1Probable hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. (258 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.
 
 
 0.899
gloA1
Glyoxalase I (lactoylglutathione lyase) catalyzes the first step of the glyoxal pathway in the following reaction: glutathione + methylglyoxal = (R)-S-lactoylglutathione,; Function unclear.
    
  0.801
lguL
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|Q8YEJ0 (61%), to trembl|Q8DB12 (58%) and to trembl|Q8UCM7 (52%). Pfam (PF00903): Glyoxalase/Bleomycin resistance protein/Dioxygenase; Specificity unclear.
 
 
 0.786
azo1207
Hypothetical protein predicted by Glimmer/Critica. No homology to the data bank. No domains predicted. No signal peptide. No TMHs.
       0.773
FtsJ
Ribosomal RNA large subunit methyltransferase j; Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
  
  
  0.653
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
ycbL
Hypothetical 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.
     
 0.613
azo1211
Conserved hypothetical protein. Homology bll7767 of B. japonicum of 30% (trembl|Q89CN0) Pfam: WD domain, G-beta repeat no signal peptide no TMHs.
  
 
  0.606
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
azo2654
Lactoylglutathione lyase; Glyoxalase family protein, 54% identity (67% similarity) to TrEMBL;Q88HB6. 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-hydroxyp [...]
     
  0.599
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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