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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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[Homology]
Score
ybdLAminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes,such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies; these sequences are defined by the aminotransferases class-I pyridoxal-phosphate attachment site signature, which contains the lysine residue involved in pyridoxal-phosphate binding. Similar to trembl|Q8XXV2 (58%) and to sprot|YBDL_ECOLI (52%). Pfam (PF00155): Aminotransferases class-I pyridoxal-phosphate-binding [...] (405 aa)    
Predicted Functional Partners:
gltB
Ferredoxin-dependent glutamate synthase,; Specificity unclear.
    
 0.937
pheA
Bifunctional chorismate mutase/prephenate dehydratase P-protein, pheA,; High confidence in function and specificity.
 
 
 0.837
lpdA
Dihydrolipoamide dehydrogenase. Homology to lpdA of N. meningitides of 70% (trembl|Q59099). THE BRANCHED-CHAIN ALPHA-KETO DEHYDROGENASE COMPLEX CATALYZES THE OVERALL CONVERSION OF ALPHA-KETO ACIDS TO ACYL-COA AND CO(2). IT CONTAINS MULTIPLE COPIES OF 3 ENZYMATIC COMPONENTS: BRANCHED-CHAIN ALPHA-KETO ACID DECARBOXYLASE (E1) LIPOAMIDE ACYLTRANSFERASE (E2) AND LIPOAMIDE DEHYDROGENASE (E3) (BY SIMILARITY). InterPro: FAD-dependent pyridine nucleotide-disulphide oxidoreductase (IPR001327); Pyridine nucleotide-disulphide oxidoreductase, classI (IPR001100); biotin/Lipoyl attachment (IPR000089) [...]
  
 0.727
maeB1
Probable malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) (EC 1.1.1.40) (NADP-ME). Homology to dme of S. meliloti of 60% (sprot|MAO1_RHIME). Required for symbiotic nitrogen fixation. Plays a key role in the conversion of malate to acetyl-CoA for efficient tricarboxylic acid cycle function in nitrogen-fixating bacteria. Tigrfam: pta: phosphotransacetylase Pfam: Malic enzyme; Phosphate acetyl/butaryltransferase no signal peptide no TMHs; High confidence in function and specificity.
  
 0.719
maeB2
Probable malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+). Homology to dme of S. meliloti of 61% (sprot|MAO1_RHIME). Required for symbiotic nitrogen fixation. Plays a key role in the conversion of malate to acetyl-CoA for efficient tricarboxylic acid cycle function in nitrogen-fixating bacteria. InterPro: Phosphate acetyl/butaryl transferase (IPR002505); Malic enzyme (IPR001891) Pfam: Malic enzyme; Phosphate acetyl/butaryl transferase Tigrfam: pta: phosphotransacetylase no signal peptide no TMHs; High confidence in function and specificity.
  
 0.719
metH
Probable methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
    
 0.691
putA
Probable bifunctional PutA protein; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family.
     
 0.690
pabB
Para-aminobenzoate synthase component I (EC 4.1.3.-) (ADC synthase). CATALYZES THE BIOSYNTHESIS OF 4-AMINO-4-DEOXYCHORISMATE (ADC) FROM CHORISMATE AND GLUTAMINE. InterPro: Anthranilate synthase component I and chorismate binding enzyme pabB: para-aminobenzoate synthase component I; Specificity unclear.
   
 0.680
pilR
Two component system response regulator,; High confidence in function and specificity.
    
  0.662
aroA
3-phosphoshikimate 1-carboxyvinyltransferase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate; Belongs to the cytidylate kinase family. Type 1 subfamily.
  
 
 0.657
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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