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query proteins and first shell of interactors
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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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proBGlutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. (380 aa)    
Predicted Functional Partners:
proA
Gamma-glutamyl phosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family.
 
 0.999
proC
Pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
 
 0.963
EFH90138.1
COGs: COG0069 Glutamate synthase domain 2; InterProIPR013785:IPR000583:IPR006982:IPR002932:IPR 002489:IPR017932; KEGG: tro:trd_1105 glutamate synthase [nadph] large chain precursor; PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein; PRIAM: Glutamate synthase (ferredoxin); SPTR: B9L0N4 Glutamate synthase [nadph] large chain; PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II.
 
  
 0.774
Krac_8583
COGs: COG0506 Proline dehydrogenase; InterPro IPR008219:IPR002872; KEGG: ttr:Tter_0599 proline dehydrogenase; PFAM: Proline dehydrogenase; SPTR: D1C8A2 Proline dehydrogenase; PFAM: Proline dehydrogenase.
    
 0.768
Krac_2940
COGs: COG0160 4-aminobutyrate aminotransferase and related aminotransferase; InterPro IPR005814:IPR015424:IPR015421:IPR004632; KEGG: psb:Psyr_0146 4-aminobutyrate aminotransferase; PFAM: aminotransferase class-III; SPTR: C1XPP3 4-aminobutyrate aminotransferase; TIGRFAM: 4-aminobutyrate aminotransferase; PFAM: Aminotransferase class-III; TIGRFAM: 4-aminobutyrate aminotransferase, prokaryotic type; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
   
 
 0.704
Krac_7969
Aminotransferase class-III; COGs: COG4992 Ornithine/acetylornithine aminotransferase; InterPro IPR005814:IPR015424:IPR015421; KEGG: dba:Dbac_2006 aminotransferase class-III; PFAM: aminotransferase class-III; SPTR: C7LNC4 Aminotransferase class-III; PFAM: Aminotransferase class-III; TIGRFAM: putrescine aminotransferase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
   
 0.698
argD
COGs: COG4992 Ornithine/acetylornithine aminotransferase; InterProIPR015424:IPR005814:IPR004636:IPR015422:IPR 015421; KEGG: det:DET1258 acetylornithine aminotransferase; PFAM: aminotransferase class-III; PRIAM: Acetylornithine transaminase; SPTR: Q3Z729 Acetylornithine aminotransferase; TIGRFAM: acetylornithine and succinylornithine aminotransferase; PFAM: Aminotransferase class-III; TIGRFAM: acetylornithine and succinylornithine aminotransferases; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
   
 0.682
lysJ
Acetylornithine and succinylornithine aminotransferase; Catalyzes the release of L-lysine from [LysW]-gamma-L-lysine. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. LysJ subfamily.
   
 0.682
Krac_8350
COGs: COG0423 Glycyl-tRNA synthetase (class II); InterPro IPR002314:IPR004154:IPR006195:IPR002315; KEGG: tde:TDE0020 glycyl-tRNA synthetase; PFAM: tRNA synthetase class II (G H P and S); Anticodon-binding domain protein; SPTR: Q73RR5 Glycyl-tRNA synthetase; TIGRFAM: glycyl-tRNA synthetase; manually curated; PFAM: Anticodon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); TIGRFAM: glycyl-tRNA synthetase, dimeric type.
 
 
    0.644
atpH
ATP synthase F1, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family.
    
 0.617
Your Current Organism:
Ktedonobacter racemifer
NCBI taxonomy Id: 485913
Other names: K. racemifer DSM 44963, Ktedonobacter racemifer DSM 44963, Ktedonobacter racemifer str. DSM 44963, Ktedonobacter racemifer strain DSM 44963
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