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Kmo protein (Rattus norvegicus) - STRING interaction network
"Kmo" - Kynurenine 3-monooxygenase in Rattus norvegicus
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Predicted Interactions
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KmoKynurenine 3-monooxygenase; Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract; Belongs to the aromatic-ring hydroxylase family. KMO subfamily (478 aa)    
Predicted Functional Partners:
Kynu
Kynureninase; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity; Belongs to the kynureninase family (464 aa)
 
  0.999
Ccbl1
Kynurenine--oxoglutarate transaminase 1, mitochondrial; Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta- elimination of S-conjugates and Se-conjugates of L- (seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity) (457 aa)
     
 
  0.989
Haao
3-hydroxyanthranilate 3,4-dioxygenase; Catalyzes the oxidative ring opening of 3- hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate; Belongs to the 3-HAO family (286 aa)
   
   
  0.989
Aadat
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial; Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino- group acceptors, with a preference for 2-oxoglutarate, 2- oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro) (By similarity); Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family (425 aa)
     
 
  0.988
Afmid
Kynurenine formamidase; Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites (306 aa)
   
 
  0.987
Tdo2
Tryptophan 2,3-dioxygenase; Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L- tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety (406 aa)
   
   
  0.963
Acmsd
2-amino-3-carboxymuconate-6-semialdehyde decarboxylase; Converts alpha-amino-beta-carboxymuconate-epsilon- semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodegenerative disorders. In the presence of ACMSD, ACMS is converted to AMS, a benign catabolite. ACMSD ultimately controls the metabolic fate of tryptophan catabolism along the kynurenine pathway (270 aa)
 
   
  0.925
Qprt
Nicotinate-nucleotide pyrophosphorylase [carboxylating]; Involved in the catabolism of quinolinic acid (QA); Belongs to the NadC/ModD family (299 aa)
   
   
  0.914
ENSRNOG00000043426
Cysteine conjugate-beta lyase 2 (444 aa)
     
   
  0.863
Ido1
Indoleamine 2,3-dioxygenase 1; Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. Involved in the peripheral immune tolerance, contributing to maintain homeostasis by preventing autoimmunity or immunopathology that would result from uncontrolled and overreacting immune responses. Tryptophan shortage inhibits T lymphocytes division and accumulation of tryptophan catabolites induces T-cell apoptosis and differentiation of regulatory T- cells. Acts as a suppressor of anti-tumor immunity. Limits the growth of in [...] (407 aa)
     
   
  0.863
Your Current Organism:
Rattus norvegicus
NCBI taxonomy Id: 10116
Other names: Buffalo rat, Gunn rats, Norway rat, R. norvegicus, Rattus PC12 clone IS, Rattus norvegicus, Rattus rattiscus, Rattus sp. strain Wistar, Sprague-Dawley rat, Wistar rats, brown rat, laboratory rat, rat, rats, zitter rats
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