STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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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SCO4387Putative pyridoxamine oxidase; Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). (234 aa)    
Predicted Functional Partners:
SCO1522
Conserved hypothetical protein SCL2.12c; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
    
 0.990
SCO1523
Conserved hypothetical protein SCL2.13c; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family.
    
 0.984
SCO4418
SC6F11.16c, probable oxidase, len: 222 aa; similar to TR:O88794 (EMBL:U91561) Rattus norvegicus pyridoxine 5'-phosphate oxidase PnpO, 261 aa; fasta scores: opt: 413 z-score: 479.7 E(): 3.2e-19; 38.0% identity in 184 aa overlap. Contains Pfam match to entry PF01243 Pyridox_oxidase, Pyridoxamine 5'-phosphate oxidase.
  
  
 
0.922
SCO0299
SC5G9.08, possible oxidoreductase, len: 294 aa; shows weak similarity to TR:P06632 (EMBL:M12799) Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase (278 aa), fasta scores; opt: 196 z-score: 229.3 E(): 2.1e-05, 27.6% identity in 286 aa overlap. Similar to many hypothetical oxidoreductases e.g. SW:YDBC_ECOLI (EMBL:X62680), YbcD, Escherichia coli hypothetical oxidoreductase (286 aa) (63.3% identity in 283 aa overlap). Also similar to SC5H1.28C (EMBL:AL049863) Streptomyces coelicolor putative oxidoreductase (305 aa) (46.5% identity in 301 aa overlap).
     
  0.900
SCO0429
SCF51A.07c, possible oxidoreductase, len: 315 aa. Weakly similar to many eukaryotic oxidoreductases e.g. Hordeum vulgare (Barley) TR:Q42837 (EMBL; Z48360) aldose reductase (EC 1.1.1.21) (aldehyde reductase) (320 aa), fasta scores opt: 236 z-score: 263.3 E(): 2.6e-07 27.0% identity in 296 aa overlap and many other putative oxidoreductases e.g. Streptomyces coelicolor TR:CAB42953 (EMBL:AL049863) putative oxidoreductase SC5H1.28C (305 aa), fasta scores opt: 563 z-score: 617.0 E(): 5.2e-27 39.7% identity in 305 aa overlap.
     
  0.900
SCO3730
SCH22A.08, possible oxidoreductase, len: 285 aa; similar to TR:Q9X7T6 (EMBL:AL049863) Streptomyces coelicolor putative oxidoreductase SC5H1.28c, 305 aa; fasta scores: opt: 778 z-score: 848.8 E(): 0; 52.1% identity in 288 aa overlap.
     
  0.900
SCO7264
SC5H1.28c, probable oxidoreductase, len: 305 aa; similar to many e.g. SW:MORA_PSEPU (EMBL:Q02198), morA, Pseudomonas putida morphine 6-dehydrogenase (295 aa), fasta scores; opt: 235 z-score: 281.5 E(): 2.3e-08, 28.1% identity in 274 aa overlap.
     
  0.900
SCO7200
Hypothetical protein SC1D2.03c; SC1D2.03c, unknown, len: 181 aa. Weakly similar to several proteins of unknown function e.g. Streptomyces coelicolor TR:CAB88434 (EMBL:AL353815) hypothetical 15.8 kd protein, SCD6.05C (139 aa), fasta scores opt: 147 z-score: 192.6 E(): 0.003 34.2% identity in 120 aa overlap.
    
 
 0.883
SCO1440
6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
     
 0.874
SCO4388
SCD10.20, probable citrate synthase, len: 387 aa; similar to SW:CISY_BACSU (EMBL:U05256) Bacillus subtilis citrate synthase I (EC 4.1.3.7) CitA, 366 aa; fasta scores: opt: 615 z-score: 685.9 E(): 9.9e-31; 36.7% identity in 360 aa overlap and to TR:O70008 (EMBL:AL022374) Streptomyces coelicolor citrate synthase (EC 4.1.3.7) SC5B8.22, 390 aa; fasta scores: opt: 780 z-score: 867.9 E(): 0; 41.0% identity in 371 aa overlap. Contains 2 Pfam matches to entry PF00285 citrate_synt, Citrate synthase and match to Prosite entry PS00480 Citrate synthase signature.
 
   
 0.801
Your Current Organism:
Streptomyces coelicolor
NCBI taxonomy Id: 100226
Other names: S. coelicolor A3(2), Streptomyces coelicolor A3(2)
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