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
hisCHypothetical protein; KEGG: ece:Z3183 4.1e-174 hisC; histidinol-phosphate aminotransferase K00817; COG: COG0079 Histidinol-phosphate/aromatic aminotransferase and cobyric acid decarboxylase; Psort location: Cytoplasmic, score:8.96; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. (359 aa)    
Predicted Functional Partners:
hisB
Hypothetical protein; KEGG: stm:STM2074 1.7e-184 hisB; histidinol-phosphatase / imidazoleglycerol-phosphate dehydratase K01089:K01693; COG: COG0131 Imidazoleglycerol-phosphate dehydratase; Psort location: Cytoplasmic, score:8.96; In the N-terminal section; belongs to the histidinol- phosphatase family.
 
 0.999
hisD
Hypothetical protein; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine.
  
 0.999
hisI
Hypothetical protein; KEGG: ssn:SSO_2097 6.9e-101 hisI; phosphoribosyl-amp cyclohydrolase; phosphoribosyl-ATP pyrophosphatase K01496:K01523; COG: COG0139 Phosphoribosyl-AMP cyclohydrolase; Psort location: Cytoplasmic, score:9.97; In the N-terminal section; belongs to the PRA-CH family.
 
  
 0.998
hisG
Hypothetical protein; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
 
  
 0.995
hisF
Hypothetical protein; 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.
 
  
 0.994
hisA
Hypothetical protein; KEGG: spt:SPA0795 5.8e-120 hisA; phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase K01814; COG: COG0106 Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase; Psort location: Cytoplasmic, score:9.97.
 
  
 0.994
hisH
Hypothetical protein; 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.
 
  
 0.994
CKO_03920
Hypothetical protein; KEGG: sty:STY2856 6.9e-188 tyrA; prephenate dehydrogenase / chorismate mutase K04092:K04517; COG: COG0287 Prephenate dehydrogenase; Psort location: Cytoplasmic, score:8.96.
 
 
 0.993
CKO_03919
Hypothetical protein; KEGG: ecj:JW2580 5.1e-192 pheA; fused chorismate mutase P and prephenate dehydratase K04093:K04518; COG: COG0077 Prephenate dehydratase; Psort location: Cytoplasmic, score:9.97.
 
 
 0.961
CKO_02139
Hypothetical protein; KEGG: ecj:JW0911 2.0e-204 aspC; aspartate aminotransferase, PLP-dependent K00813; COG: COG1448 Aspartate/tyrosine/aromatic aminotransferase; Psort location: Cytoplasmic, score:9.26.
   
 
 0.923
Your Current Organism:
Citrobacter koseri
NCBI taxonomy Id: 290338
Other names: C. koseri ATCC BAA-895, Citrobacter (diversus) koseri ATCC BAA-895, Citrobacter koseri ATCC BAA-895, Citrobacter koseri str. ATCC BAA-895, Citrobacter koseri strain ATCC BAA-895
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