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.
Node Color
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
Edges:
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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
dsdAD-serine dehydratase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit; TIGRFAM: D-serine ammonia-lyase; HAMAP: D-serine dehydratase; KEGG: ajs:Ajs_2250 D-serine dehydratase; Belongs to the serine/threonine dehydratase family. DsdA subfamily. (447 aa)    
Predicted Functional Partners:
AEB82560.1
L-serine dehydratase 1; TIGRFAM: Iron-sulphur-dependent L-serine dehydratase single chain form; KEGG: dia:Dtpsy_0112 L-serine dehydratase 1; PFAM: Serine dehydratase-like, alpha subunit; Serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.
    
 0.918
AEB82543.1
Threonine dehydratase; 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.
     
 0.906
ilvA
Threonine dehydratase, biosynthetic; 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.
     
 0.906
AEB86557.1
Threonine ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit.
     
 0.906
AEB85306.1
Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
     
 0.803
AEB84844.1
KEGG: dia:Dtpsy_1854 lactoylglutathione lyase.
     
 0.801
AEB82969.1
PFAM: Alanine racemase, N-terminal; KEGG: dia:Dtpsy_0501 alanine racemase domain protein.
     
  0.800
AEB85613.1
Glyoxylate reductase; KEGG: dia:Dtpsy_1370 D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain.
     
 0.800
AEB86459.1
Hydroxypyruvate reductase; KEGG: dia:Dtpsy_3039 D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding.
     
  0.800
rlmD
23S rRNA (uracil-5-)-methyltransferase rumA; Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmD subfamily.
       0.752
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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