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
dsdAD-serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the serine/threonine dehydratase family. DsdA subfamily. (433 aa)    
Predicted Functional Partners:
sdaAB
Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family.
     
 0.944
sdaAA
Serine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the iron-sulfur dependent L-serine dehydratase family.
     
 0.932
ilvA
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.
     
 0.912
AMG19069.1
Glyoxalase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.800
hisI
Iron-siderophore ABC transporter substrate-binding protein; Internal stop; Derived by automated computational analysis using gene prediction method: Protein Homology; In the N-terminal section; belongs to the PRA-CH family.
       0.519
hisZ
May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.496
hisF
Imidazole glycerol phosphate synthase cyclase subunit; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
       0.470
hisA
1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide isomerase; Catalyzes the formation of 5-(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino-l- (5-hosphoribosyl)imidazole-4-carboxamide from 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.470
hisH
Imidazole glycerol phosphate synthase subunit HisH; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
       0.470
hisB
Imidazoleglycerol-phosphate dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.470
Your Current Organism:
Staphylococcus saprophyticus
NCBI taxonomy Id: 29385
Other names: ATCC 15305, BCRC 10786, CCM 883, CCRC 10786, CCRC:10786, CCUG 3706, CIP 76.125, DSM 20229, IAM 12452, JCM 2427, LMG 13350, LMG:13350, NBRC 102446, NCAIM B.01067, NCCB 73011, NCIB 8711, NCIB:8711, NCTC 7292, NRRL B-14751, S. saprophyticus, Staphylococcus sp. HAR3
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