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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
EIJ34764.1PFAM: Aminotransferase class IV; TIGRFAM: D-amino acid aminotransferase; branched-chain amino acid aminotransferase, group I; COGs: COG0115 Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase; InterPro IPR001544:IPR005785; KEGG: mmt:Metme_2103 branched-chain amino acid aminotransferase; PFAM: Aminotransferase, class IV; SPTR: Branched chain amino acid aminotransferase; TIGRFAM: Branched-chain amino acid aminotransferase I. (290 aa)    
Predicted Functional Partners:
ilvD
PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; COGs: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; HAMAP: Dihydroxy-acid dehydratase; InterPro IPR000581:IPR004404; KEGG: tgr:Tgr7_0578 dihydroxy-acid dehydratase; PFAM: Dihydroxy-acid/6-phosphogluconate dehydratase; SPTR: Dihydroxy-acid dehydratase; TIGRFAM: Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.
  
 0.980
leuA
2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.
 
 0.973
EIJ35222.1
PFAM: domain; Pyruvate ferredoxin/flavodoxin oxidoreductase; Transketolase, C-terminal domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; COGs: COG0674 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductase alpha subunit; InterPro IPR002880:IPR019752:IPR001450:IPR011766; KEGG: alv:Alvin_1172 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate/ketoisovalerate oxidoreductase; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate [...]
  
 
 0.962
EIJ32841.1
Chorismate mutase; PFAM: Prephenate dehydratase; ACT domain; Chorismate mutase type II; TIGRFAM: chorismate mutase domain of proteobacterial P-protein, clade 2; COGs: COG0077 Prephenate dehydratase; InterPro IPR010957:IPR020822:IPR001086:IPR002912; KEGG: tgr:Tgr7_1538 chorismate mutase; PFAM: Prephenate dehydratase; Chorismate mutase, type II; Amino acid-binding ACT; SPTR: Chorismate mutase; TIGRFAM: Gamma/beta/epsilon proteobacterial P-protein, chorismate mutase domain.
    
 0.900
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.
  
 
 0.858
EIJ36551.1
PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain; COGs: COG0460 Homoserine dehydrogenase; InterPro IPR005106:IPR001342:IPR002912; KEGG: tgr:Tgr7_1439 homoserine dehydrogenase; PFAM: Homoserine dehydrogenase, catalytic; Aspartate/homoserine dehydrogenase, NAD-binding; Amino acid-binding ACT; SPTR: Homoserine dehydrogenase.
  
 
 0.839
EIJ36656.1
PFAM: Ketopantoate hydroxymethyltransferase; TIGRFAM: 3-methyl-2-oxobutanoate hydroxymethyltransferase; COGs: COG0413 Ketopantoate hydroxymethyltransferase; HAMAP: Ketopantoate hydroxymethyltransferase; InterPro IPR003700; KEGG: hha:Hhal_0675 3-methyl-2-oxobutanoate hydroxymethyltransferase; PFAM: Ketopantoate hydroxymethyltransferase; SPTR: 3-methyl-2-oxobutanoate hydroxymethyltransferase; TIGRFAM: Ketopantoate hydroxymethyltransferase.
     
 0.780
EIJ36523.1
PFAM: HMGL-like; TIGRFAM: homocitrate synthase NifV; COGs: COG0119 Isopropylmalate/homocitrate/citramalate synthase; InterPro IPR013477:IPR000891; KEGG: alv:Alvin_1499 homocitrate synthase; PFAM: Pyruvate carboxyltransferase; SPTR: Homocitrate synthase; TIGRFAM: Homocitrate synthase NifV-type.
 
 0.778
EIJ36307.1
KEGG: hau:Haur_3960 beta-ketoacyl synthase; SPTR: Beta-ketoacyl synthase.
  
 
 0.774
EIJ34763.1
Beta-lactamase hydrolase-family protein; PFAM: Putative phosphatase (DUF442); InterPro IPR005939; KEGG: cyc:PCC7424_4436 hypothetical protein; PFAM: Beta-lactamase hydrolase-like; SPTR: Putative uncharacterized protein.
       0.773
Your Current Organism:
Thiothrix nivea
NCBI taxonomy Id: 870187
Other names: T. nivea DSM 5205, Thiothrix nivea DSM 5205, Thiothrix nivea JP2, Thiothrix nivea str. DSM 5205, Thiothrix nivea strain DSM 5205
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