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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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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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trpATryptophan synthase, alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. (259 aa)    
Predicted Functional Partners:
trpB
Tryptophan synthase, beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
 0.999
Lbys_2386
COGs: COG0134 Indole-3-glycerol phosphate synthase; InterPro IPR001468:IPR013798; KEGG: phe:Phep_4168 indole-3-glycerol-phosphate synthase; PFAM: Indole-3-glycerol phosphate synthase; PRIAM: Indole-3-glycerol-phosphate synthase; SPTR: Indole-3-glycerol-phosphate synthase; PFAM: Indole-3-glycerol phosphate synthase; Belongs to the TrpC family.
 
 0.999
trpF
COGs: COG0135 Phosphoribosylanthranilate isomerase; InterPro IPR001240; KEGG: sli:Slin_5476 phosphoribosylanthranilate isomerase; PFAM: N-(5'phosphoribosyl)anthranilate isomerase (PRAI); PRIAM: Phosphoribosylanthranilate isomerase; SPTR: N-(5'-phosphoribosyl)anthranilate isomerase; PFAM: N-(5'phosphoribosyl)anthranilate (PRA) isomerase; Belongs to the TrpF family.
  
 0.990
trpD
Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA).
  
 0.984
Lbys_2174
COGs: COG0512 Anthranilate/para-aminobenzoate synthase component II; InterProIPR006220:IPR011702:IPR001317:IPR006221:IPR 000991:IPR017926; KEGG: sli:Slin_5473 glutamine amidotransferase of anthranilate synthase; PFAM: glutamine amidotransferase class-I; SPTR: Glutamine amidotransferase of anthranilate synthase; TIGRFAM: glutamine amidotransferase of anthranilate synthase; PFAM: Glutamine amidotransferase class-I; TIGRFAM: glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase.
  
 0.980
Lbys_2173
COGs: COG0147 Anthranilate/para-aminobenzoate synthase component I; InterPro IPR019999:IPR006805:IPR015890; KEGG: dfe:Dfer_3790 anthranilate synthase; PFAM: Chorismate binding-like; Anthranilate synthase component I domain protein; PRIAM: Anthranilate synthase; SPTR: Anthranilate synthase; PFAM: Anthranilate synthase component I, N terminal region; chorismate binding enzyme.
 
  
 0.956
glyA
Glycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
 
   
 0.926
Lbys_3208
Chorismate binding protein; COGs: COG0147 Anthranilate/para-aminobenzoate synthase component I; InterPro IPR015890; KEGG: bth:BT_0767 para-aminobenzoate synthase component I; PFAM: Chorismate binding-like; SPTR: Putative para-aminobenzoate synthase component I; PFAM: chorismate binding enzyme.
 
  
 0.926
ilvA
L-threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
  
 
 0.918
Lbys_1842
COGs: COG1760 L-serine deaminase; InterPro IPR005131:IPR005130:IPR004644; KEGG: gvi:glr2358 L-serine dehydratase; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; PRIAM: L-serine ammonia-lyase; SPTR: L-serine dehydratase; TIGRFAM: L-serine dehydratase 1; PFAM: Serine dehydratase alpha chain; Serine dehydratase beta chain; TIGRFAM: L-serine dehydratase, iron-sulfur-dependent, single chain form.
   
 
 0.914
Your Current Organism:
Leadbetterella byssophila
NCBI taxonomy Id: 649349
Other names: L. byssophila DSM 17132, Leadbetterella byssophila 4M15, Leadbetterella byssophila DSM 17132, Leadbetterella byssophila str. DSM 17132, Leadbetterella byssophila strain DSM 17132
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