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ribF protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"ribF" - Riboflavin biosynthesis protein in Desulfovibrio vulgaris Hildenborough
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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ribFRiboflavin biosynthesis protein; Identified by similarity to SP-P08391; match to protein family HMM PF01687; match to protein family HMM TIGR00083; Belongs to the ribF family (314 aa)    
Predicted Functional Partners:
ribE
Riboflavin synthase, alpha subunit; Identified by similarity to SP-P16440; match to protein family HMM PF00677; match to protein family HMM TIGR00187 (220 aa)
 
  0.961
truB
tRNA pseudouridine synthase B; Responsible for synthesis of pseudouridine from uracil- 55 in the psi GC loop of transfer RNAs (304 aa)
 
   
  0.895
DVU_0451
Identified by match to protein family HMM PF00571; match to protein family HMM PF00654 (603 aa)
              0.893
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)
 
   
  0.881
ileS
Isoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as ’pretransfer’ editing and involves the hydrolysis of activated Val-AMP. The other activity is designated ’posttransfer’ editing and involves deacylation of mischarged Val-tRNA(Ile) (938 aa)
 
   
  0.863
ispD
Bifunctional enzyme IspD/IspF; 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 (395 aa)
 
   
  0.832
cmk
Cytidylate kinase; Identified by similarity to SP-P23863; match to protein family HMM PF02224; match to protein family HMM TIGR00017; Belongs to the cytidylate kinase family. Type 1 subfamily (232 aa)
        0.802
trmU
tRNA-specific 2-thiouridylase MnmA; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34 (346 aa)
        0.799
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)
 
   
  0.765
sun
Sun protein; Identified by match to protein family HMM PF01029; match to protein family HMM PF01189; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family (507 aa)
 
   
  0.741
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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