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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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Experiments
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[Homology]
Score
azo3716Hypothetical protein. (164 aa)    
Predicted Functional Partners:
icmF
Probable methylmalonyl-coa mutase protein; Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly.
    
  0.576
mutB
Probable Methylmalonyl-CoA mutase large subunit; FUNCTION: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates (By similarity). ACtivity:- (R)-2-Methylmalonyl-CoA = succinyl-CoA Entry name :- MUTB_PORGI Primary accession number :-Q59677 Identities = 467/679 (68%) InterPro :-IPR006159; Acid_CoA_mut_C. IPR006158; B12-binding. IPR006099; MMCoA_mutase. IPR006098; MMCoA_mutase_N. IPR006100; MMCoA_mutase_sub. Pfam PF02310; B12-binding; 1. PF01642; MM_CoA_mutase; 1. Prediction: Non-secretory protein Signal [...]
     
  0.574
azo3717
Hypothetical protein; Region start changed from 4071796 to 4071769 (-27 bases), Changed start from att to next atg.
       0.553
lapP
Phenol hydroxylase P5 protein (EC 1.14.13.7) (Phenol 2-monooxygenase P5 component). Probable electron transfer from NADPH via FAD and the 2Fe-2S center to the oxygenase activity site of the enzyme; High confidence in function and specificity.
    
  0.543
poxF
Probable phenol hydroxylase (EC 1.14.13.7) (Phenol 2-monooxygenase P5 component). Probable electron transfer from NADPH via FAD and the 2Fe-2S center to the oxygenase activity site of the enzyme. InterPro: Oxidoreductase FAD and NAD(P)-binding domain hisT_truA: tRNA pseudouridine synthase A; Specificity unclear.
    
  0.543
nagAa
Naphthalene 12-dioxygenase system ferredoxin--NAD(+) reductase component COMPONENT OF NAPHTHALENE DIOXYGENASE (NDO) MULTICOMPONENT ENZYME SYSTEM WHICH CATALYZES THE INCORPORATION OF BOTH ATOMS OF MOLECULAR OXYGEN INTO NAPHTHALENE TO FORM CIS- NAPHTHALENE DIHYDRODIOL. TRANSFERS ELECTRONS FROM FERREDOXIN (NDOA) TO NADH; High confidence in function and specificity.
    
  0.543
ascD
Probable CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase reductase. Homology to ascD of Y. pestis of 41% (sprot|ASCD_YERPE). PARTICIPATES IN THE CONVERSION OF CDP-6-DEOXY-D-GLYCERO- L-THREO-4-HEXULOSE TO 36-DIDEOXY-D-GLYCERO-D-GLYCERO-4-HEXULOSE TOGETHER WITH CDP-6-DEOXY-D-GLYCERO-L-THREO-4-HEXULOSE-3-DEHYDRASE (E1) IN TWO CONSECUTIVE STEPS. THE DETAILED MECHANISM OF E3 IS NOT YET RESOLVED. InterPro: Oxidoreductase FAD and NAD(P)-binding domain (IPR001433); NadH:cytochrome b5 reductase (CBR) (IPR000134); 2Fe-2S Ferredoxin (IPR006057); Phenol hydroylase reductase family (IPR001221) [...]
    
  0.543
azo3715
Hypothetical membrane protein. Homology to an orf of E. coli of 29% (trembl|Q8VNQ4). no domains predricted. no signal peptide. 3 TMHs.
       0.515
azo3718
Conserved hypothetical protein.
    
 0.500
azo2654
Lactoylglutathione lyase; Glyoxalase family protein, 54% identity (67% similarity) to TrEMBL;Q88HB6. Has PF00903,Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;IPR004360, Gly_bleo_diox: Glyoxalase I catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyp [...]
 
  
  0.420
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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