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DVU_1912 DVU_1912 DVU_0864 DVU_0864 nnrD nnrD tsaD tsaD DVU_1911 DVU_1911 alr alr DVU_1913 DVU_1913 DVU_1914 DVU_1914 acpS acpS ispD ispD pdxJ pdxJ
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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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Known Interactions
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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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DVU_1912Conserved hypothetical protein TIGR00150; Identified by match to protein family HMM PF02367; match to protein family HMM TIGR00150. (162 aa)    
Predicted Functional Partners:
DVU_0864
Glycoprotease family protein, putative; Identified by match to protein family HMM PF00814.
  
 
 0.972
nnrD
YjeF-related 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 of both epi [...]
  
 
 0.958
tsaD
Metalloendopeptidase, putative, glycoprotease family; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
  
 
 0.925
DVU_1911
CBS domain protein; Identified by similarity to OMNI:NTL01TE1801; match to protein family HMM PF00571.
  
    0.781
alr
Alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family.
 
  
 0.660
DVU_1913
Aspartate kinase, monofunctional class; Identified by similarity to SP:P41403; match to protein family HMM PF00696; match to protein family HMM PF01842; match to protein family HMM TIGR00656; match to protein family HMM TIGR00657; Belongs to the aspartokinase family.
  
    0.644
DVU_1914
2-isopropylmalate synthase/homocitrate synthase family protein; Identified by match to protein family HMM PF00682; match to protein family HMM TIGR00977; Belongs to the alpha-IPM synthase/homocitrate synthase family.
       0.600
acpS
Holo-(acyl-carrier-protein) synthase; Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein; Belongs to the P-Pant transferase superfamily. AcpS family.
  
    0.554
ispD
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D- erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4- diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C- methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF); In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
     
 0.544
pdxJ
Pyridoxal phosphate biosynthetic protein PdxJ; Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino- 2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
       0.540
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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