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JT27_11730 protein (Alcaligenes faecalis) - STRING interaction network
"JT27_11730" - MBL fold metallo-hydrolase in Alcaligenes faecalis
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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[Homology]
Score
JT27_11730MBL fold metallo-hydrolase; Derived by automated computational analysis using gene prediction method- Protein Homology (318 aa)    
Predicted Functional Partners:
JT27_11735
FAD-dependent oxidoreductase; Derived by automated computational analysis using gene prediction method- Protein Homology (557 aa)
 
   
  0.967
AFA_02770
DNA topoisomerase IV subunit B; Derived by automated computational analysis using gene prediction method- Protein Homology (69 aa)
 
          0.964
JT27_11750
Fumarylacetoacetase; Derived by automated computational analysis using gene prediction method- Protein Homology (441 aa)
 
        0.825
hmgA
Homogentisate 1,2-dioxygenase; Involved in the catabolism of homogentisate (2,5- dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring cleavage of the aromatic ring of homogentisate to yield maleylacetoacetate (434 aa)
 
        0.798
fpg
Formamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3’- and 5’-phosphates (275 aa)
              0.504
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Alcaligenes faecalis, Alcaligenes sp. BP11, CIP 55.84, CIP 60.80, DSM 30030, IAM 12369, IFO 13111, JCM 20522, JCM 20663, NBRC 13111, NCAIM B.01104, NCIMB 8156, NCTC 11953
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