1.14.13.33: 4-hydroxybenzoate 3-monooxygenase [NAD(P)H]
This is an abbreviated version!
For detailed information about 4-hydroxybenzoate 3-monooxygenase [NAD(P)H], go to the full flat file.
Reaction
Synonyms
4-HBA 3-hydroxylase, 4-HBA 3-monooxygenase, 4-hydroxybenzoate 3-hydroxylase, 4-hydroxybenzoate 3-monooxygenase (NAD(P)H), 4-hydroxybenzoate 3-monooxygenase (NAD(P)H2), 4-hydroxybenzoate-3-hydroxylase, 4HB 3-hydroxylase, NAD(P)H-dependent PHBHCn1, NADPH-dependent PHBH, oxygenase, 4-hydroxybenzoate 3-mono- (reduced nicotinamide adenine dinucleotide (phosphate)), p-hydroxybenzoate hydroxylase, para-hydroxybenzoate-3-hydroxylases, PHBH, PHBHCn1, PHBHRo, PHBHRo1CP, PHBHRr, PobA, PRAI, Reut_B5020, Xcc0356
ECTree
1.14.13.33 4-hydroxybenzoate 3-monooxygenase [NAD(P)H]Advanced search results
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General Information on EC 1.14.13.33 - 4-hydroxybenzoate 3-monooxygenase [NAD(P)H]
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
metabolism
the enzyme is involved in the degradation of 4-hydroxybenzoate. The 4-hydroxybenzoate degradation pathway is required for full pathogenicity of Xanthomonas campestris pv. campestris in radish
physiological function
additional information
evolution
amino acid sequences of NADH-preferring PHBHs of putative PHBHs identified in currently available bacterial genomes, phylogenetic analysis, overview. The pyridine nucleotide coenzyme specificity of PHBH emerged through adaptive evolution, and the NADH-preferring enzymes are the older versions of PHBH. Structural comparison and distance tree analysis of group A flavoprotein monooxygenases indicates that a similar protein segment as being responsible for the pyridine nucleotide coenzyme specificity of PHBH is involved in determining the pyridine nucleotide coenzyme specificity of the other group A members. Evolutionary rate calculation. Among the actinobacterial sequences presently available, most comprise the NADH-preferring fingerprint. However, Mycobacteria have a mixed type motif, often the first or both arginine(s) of the NADH-fingerprint are present but the remaining part is lacking. In addition, many mycobacterial sequences have parts of the NADPH-preferring fingerprint, especially, x(D/E)YVL(G/S)R
evolution
amino acid sequences of NADH-preferring PHBHs of putative PHBHs identified in currently available bacterial genomes, phylogenetic analysis, overview. The pyridine nucleotide coenzyme specificity of PHBH emerged through adaptive evolution, and the NADH-preferring enzymes are the older versions of PHBH. Structural comparison and distance tree analysis of group A flavoprotein monooxygenases indicates that a similar protein segment as being responsible for the pyridine nucleotide coenzyme specificity of PHBH is involved in determining the pyridine nucleotide coenzyme specificity of the other group A members. Evolutionary rate calculation. Among the actinobacterial sequences presently available, most comprise the NADH-preferring fingerprint. However, Mycobacteria have a mixed type motif, often the first or both arginine(s) of the NADH-fingerprint are present but the remaining part is lacking. In addition, many mycobacterial sequences have parts of the NADPH-preferring fingerprint, especially, x(D/E)YVL(G/S)R
evolution
amino acid sequences of NADH-preferring PHBHs of putative PHBHs identified in currently available bacterial genomes, phylogenetic analysis, overview. The pyridine nucleotide coenzyme specificity of PHBH emerged through adaptive evolution, and the NADH-preferring enzymes are the older versions of PHBH. Structural comparison and distance tree analysis of group A flavoprotein monooxygenases indicates that a similar protein segment as being responsible for the pyridine nucleotide coenzyme specificity of PHBH is involved in determining the pyridine nucleotide coenzyme specificity of the other group A members. Evolutionary rate calculation. Among the actinobacterial sequences presently available, most comprise the NADH-preferring fingerprint. However, Mycobacteria have a mixed type motif, often the first or both arginine(s) of the NADH-fingerprint are present but the remaining part is lacking. In addition, many mycobacterial sequences have parts of the NADPH-preferring fingerprint, especially, x(D/E)YVL(G/S)R
evolution
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amino acid sequences of NADH-preferring PHBHs of putative PHBHs identified in currently available bacterial genomes, phylogenetic analysis, overview. The pyridine nucleotide coenzyme specificity of PHBH emerged through adaptive evolution, and the NADH-preferring enzymes are the older versions of PHBH. Structural comparison and distance tree analysis of group A flavoprotein monooxygenases indicates that a similar protein segment as being responsible for the pyridine nucleotide coenzyme specificity of PHBH is involved in determining the pyridine nucleotide coenzyme specificity of the other group A members. Evolutionary rate calculation. Among the actinobacterial sequences presently available, most comprise the NADH-preferring fingerprint. However, Mycobacteria have a mixed type motif, often the first or both arginine(s) of the NADH-fingerprint are present but the remaining part is lacking. In addition, many mycobacterial sequences have parts of the NADPH-preferring fingerprint, especially, x(D/E)YVL(G/S)R
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evolution
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amino acid sequences of NADH-preferring PHBHs of putative PHBHs identified in currently available bacterial genomes, phylogenetic analysis, overview. The pyridine nucleotide coenzyme specificity of PHBH emerged through adaptive evolution, and the NADH-preferring enzymes are the older versions of PHBH. Structural comparison and distance tree analysis of group A flavoprotein monooxygenases indicates that a similar protein segment as being responsible for the pyridine nucleotide coenzyme specificity of PHBH is involved in determining the pyridine nucleotide coenzyme specificity of the other group A members. Evolutionary rate calculation. Among the actinobacterial sequences presently available, most comprise the NADH-preferring fingerprint. However, Mycobacteria have a mixed type motif, often the first or both arginine(s) of the NADH-fingerprint are present but the remaining part is lacking. In addition, many mycobacterial sequences have parts of the NADPH-preferring fingerprint, especially, x(D/E)YVL(G/S)R
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physiological function
the transformation of 4-hydroxybenzoate (4-HBA) to protocatechuate (PCA) is catalyzed by flavoprotein oxygenases known as para-hydroxybenzoate-3-hydroxylases (PHBHs)
physiological function
the transformation of 4-hydroxybenzoate (4-HBA) to protocatechuate (PCA) is catalyzed by flavoprotein oxygenases known as para-hydroxybenzoate-3-hydroxylases (PHBHs)
additional information
energy profiling from enzyme protein structure is realized by means of a coarse-grained residue-level pair potential function modeling, overview
additional information
energy profiling from enzyme protein structure is realized by means of a coarse-grained residue-level pair potential function modeling, overview
additional information
energy profiling from enzyme protein structure is realized by means of a coarse-grained residue-level pair potential function modeling, overview
additional information
the X-ray crystal structure of PraI is solved and reveals absolute conservation of the active site architecture to other PHBH structures despite their differing cofactor preferences
additional information
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energy profiling from enzyme protein structure is realized by means of a coarse-grained residue-level pair potential function modeling, overview
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additional information
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energy profiling from enzyme protein structure is realized by means of a coarse-grained residue-level pair potential function modeling, overview
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