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JQMD01000002_gene2000 protein (Zobellia uliginosa) - STRING interaction network
"JQMD01000002_gene2000" - annotation not available in Zobellia uliginosa
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
JQMD01000002_gene2000annotation not available (313 aa)    
Predicted Functional Partners:
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP (510 aa)
       
    0.832
mnmA
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 (396 aa)
              0.829
JQMD01000002_gene3033
3-oxoacyl-[acyl-carrier-protein] synthase 2; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP (417 aa)
 
  0.791
JQMD01000002_gene991
annotation not available (150 aa)
 
   
  0.786
JQMD01000002_gene3498
annotation not available (401 aa)
 
  0.782
fabZ
Multifunctional fusion protein; Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis; Belongs to the thioester dehydratase family. FabZ subfamily (461 aa)
       
  0.762
JQMD01000002_gene3492
annotation not available (122 aa)
       
  0.758
JQMD01000002_gene3501
annotation not available (382 aa)
   
 
  0.758
lipA
Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (291 aa)
       
    0.755
lipB
Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (233 aa)
       
    0.754
Your Current Organism:
Zobellia uliginosa
NCBI taxonomy Id: 143224
Other names: ACAM 538, ATCC 14397, Agarbacterium uliginosum, CCUG 33448, CECT 4277, CIP 104808, Cellulophaga uliginosa, Cytophaga uliginosa, DSM 2061, Flavibacterium uliginosum, Flavobacterium uliginosum, IFO 14962, JCM 21152, LMG 3809, NBRC 14962, Z. uliginosa, Zobellia uliginosa, strain ZoBell 553
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