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[Homology]
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LHA_0083Putative nucleoside diphosphate pyrophosphatase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. (204 aa)    
Predicted Functional Partners:
nudE
ADP-ribose diphosphatase; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
  
  
  0.915
LHA_1985
Ribose-phosphate pyrophosphokinase.
    
 0.908
prs
Ribose-phosphate pyrophosphokinase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
    
 0.908
deoB
Phosphopentomutase; Phosphotransfer between the C1 and C5 carbon atoms of pentose; Belongs to the phosphopentomutase family.
    
  0.903
algC
Phosphomannomutase/phosphoglucomutase.
   
  0.902
algC-2
Phosphomannomutase/phosphoglucomutase.
   
  0.902
thiM
Hydroxyethylthiazole kinase; Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ); Belongs to the Thz kinase family.
     
  0.900
ubiX
Putative aromatic acid decarboxylase; Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN; Belongs to the UbiX/PAD1 family.
   
 
  0.900
birA
Biotin synthetase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
   
    0.746
yjeF
Putative carbohydrate kinase; 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 of [...]
  
 0.722
Your Current Organism:
Legionella hackeliae
NCBI taxonomy Id: 449
Other names: ATCC 35250, CCUG 31232, CCUG 31232 A, CIP 103844, DSM 19214, JCM 7563, L. hackeliae, NCTC 11979, strain Lansing 2
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