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
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
fhcAFormyltransferase/hydrolase complex Fhc subunit A; Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the formylmethanofuran (formyl-MFR). May be catalyze the hydrolysis of formylmethanofuran (formyl-MFR) to yield formate and MFR. Belongs to the metallo-dependent hydrolases superfamily. FwdA/FmdA family. (548 aa)    
Predicted Functional Partners:
fhcC
Formyltransferase/hydrolase complex Fhc subunit C; Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the formylmethanofuran (formyl-MFR).
 
 
 0.999
fhcD
Formyltransferase/hydrolase complex Fhc subunit D; Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the intermediate formylmethanofuran (formyl-MFR). Catalyzes the transfer of a formyl group from 5-formyl-H(4)MPT to MFR so as to produce tetrahydromethanopterin (H(4)MPT) and formyl-MFR, which is then hydrolyzed to formate and MFR; Belongs to the FTR family.
 
 
 0.999
fhcB
Formyltransferase/hydrolase complex Fhc subunit B; Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the formylmethanofuran (formyl-MFR).
 
 0.999
mch
N(5),N(10)-methenyltetrahydromethanopterin cyclohydrolase (methenyl-H4MPT cyclohydrolase); Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl- H(4)MPT.
 
  
 0.953
mtdB
NAD(P)-dependent methylene tetrahydromethanopterin dehydrogenase; Catalyzes the dehydrogenation of methylene-H(4)MPT.
 
   
 0.879
fae-2
Formaldehyde-activating enzyme; Catalyzes the condensation of formaldehyde with tetrahydromethanopterin (H(4)MPT) to 5,10- methylenetetrahydromethanopterin, a reaction which also proceeds spontaneously, but at a lower rate than that of the enzyme-catalyzed reaction. Is an essential enzyme for methylotrophic energy metabolism and formaldehyde detoxification of this bacterium.
 
   
 0.828
mtdA
NADP-dependent methylene-tetrahydromethanopterin/methylene- tetrahydrofolate dehydrogenase; Catalyzes the dehydrogenation of methylene-H(4)MPT. Can also catalyze the reversible dehydrogenation of methylene-H(4)F with 20-fold lower catalytic efficiency.
 
   
 0.826
ACS39618.1
Orf22. Involved in biosynthesis of tetrahydromethanopterin. Essential for formaldehyde oxidation; Function experimentally demonstrated in the studied strain; putative enzyme.
 
   
 0.814
ACS39617.1
Orf21. Involved in biosynthesis of tetrahydromethanopterin. Essential for formaldehyde oxidation; Function experimentally demonstrated in the studied strain; putative enzyme.
 
   
 0.811
ACS39413.1
Putative GXGXG-motif protein, glutamate synthase and formylmethanofuran dehydrogenase-like domain; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
  
 
 0.805
Your Current Organism:
Methylorubrum extorquens
NCBI taxonomy Id: 272630
Other names: M. extorquens AM1, Methylobacterium extorquens AM1, Methylorubrum extorquens AM1, Pseudomonas sp. AM1
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