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pdxJ protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"pdxJ" - Pyridoxine 5'-phosphate synthase in Desulfovibrio vulgaris Hildenborough
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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pdxJPyridoxine 5’-phosphate synthase; 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 (241 aa)    
Predicted Functional Partners:
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 (124 aa)
 
   
  0.941
DVU_0769
Pyridoxal kinase; Identified by similarity to SP-P40191; Belongs to the pyridoxine kinase family (292 aa)
         
  0.914
dxs
1-deoxy-D-xylulose-5-phosphate synthase; Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP); Belongs to the transketolase family. DXPS subfamily (641 aa)
         
  0.904
pdxA
Pyridoxal phosphate biosynthetic protein PdxA; Identified by similarity to SP-P19624; match to protein family HMM PF04166; match to protein family HMM TIGR00557; Belongs to the PdxA family (406 aa)
 
     
  0.868
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP (515 aa)
 
     
  0.765
nnrD
Multifunctional fusion 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; Belongs to the NnrD/CARKD family (574 aa)
              0.751
ribD
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5’-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5’-phosphate; In the C-terminal section; belongs to the HTP reductase family (377 aa)
         
  0.738
ribAB
Riboflavin biosynthesis protein RibBA; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the N-terminal section; belongs to the DHBP synthase family (409 aa)
         
  0.729
ugd
UDP-glucose 6-dehydrogenase; Identified by similarity to SP-O54068; match to protein family HMM PF00984; match to protein family HMM PF03720; match to protein family HMM PF03721 (445 aa)
              0.676
DVU_1911
CBS domain protein; Identified by similarity to OMNI-NTL01TE1801; match to protein family HMM PF00571 (150 aa)
   
        0.671
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 Hildenborough, 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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