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Information on EC 5.3.3.17 - trans-2,3-dihydro-3-hydroxyanthranilate isomerase and Organism(s) Pseudomonas fluorescens and UniProt Accession Q51792

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IUBMB Comments
The enzyme is involved in phenazine biosynthesis. The product probably spontaneously dimerises to 1,4,5a,6,9,10a-hexahydrophenazine-1,6-dicarboxylate
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Pseudomonas fluorescens
UNIPROT: Q51792
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The taxonomic range for the selected organisms is: Pseudomonas fluorescens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
phzF, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate isomerase
The enzyme is involved in phenazine biosynthesis. The product probably spontaneously dimerises to 1,4,5a,6,9,10a-hexahydrophenazine-1,6-dicarboxylate
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxylic acid
(1R,6S)-6-amino-5-hydroxycyclohexa-2,4-diene-1-carboxylic acid
show the reaction diagram
-
-
-
?
(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate
(1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxylic acid
(1R,6S)-6-amino-5-hydroxycyclohexa-2,4-diene-1-carboxylic acid
show the reaction diagram
-
-
-
?
(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate
(1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PHZF_PSEFL
278
0
30053
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
two protein species with MW 32048 Da and 32224 Da, MALDI-TOF mass-spectrometry
32218
2 * 32218, histidine-tagged enzyme
42000
gel filtration
66070
laser light scattering in solution
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.8 A crystal structure of PhzF, hanging drop vapor diffusion method
hanging-drop vapor-diffusion method. Crystals of unliganded PhzF belong to space group P3(2)21 with a a = b = 56 A, and c = 156 A and hold one monomer per asymmetric unit. Complexes of PhzF (with 3-hydroxyanthranilic acid and trans-2,3-dihydro-3-hydroxyanthranilic acid) crystallize in space group P2(1)2(1)2 with cell parameters of a = 93 A, b = 100 A, and c = 57 A and contain one dimer in the asymmetric unit
hanging-drop vapour-diffusion method. Crystallized from PEG 4000/ammonium sulfate/sodium citrate pH 5.6. The crystals belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 56.3, c = 156.4 A. They contain one monomer in the asymmetric unit and diffract to better than 1.7 A on synchrotron beamlines. Crystals of seleno-L-methionine-labelled PhzF have been obtained
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
large-scale expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mavrodi, D.V.; Bleimling, N.; Thomashow, L.S.; Blankenfeldt, W.
The purification, crystallization and preliminary structural characterization of PhzF, a key enzyme in the phenazine-biosynthesis pathway from Pseudomonas fluorescens 2-79
Acta Crystallogr. Sect. D
60
184-186
2004
Pseudomonas fluorescens (Q51792), Pseudomonas fluorescens Feb 79 (Q51792)
Manually annotated by BRENDA team
Parsons, J.F.; Song, F.; Parsons, L.; Calabrese, K.; Eisenstein, E.; Ladner, J.E.
Structure and function of the phenazine biosynthesis protein PhzF from Pseudomonas fluorescens 2-79
Biochemistry
43
12427-12435
2004
Pseudomonas fluorescens (Q51792), Pseudomonas fluorescens Feb 79 (Q51792)
Manually annotated by BRENDA team
Blankenfeldt, W.; Kuzin, A.P.; Skarina, T.; Korniyenko, Y.; Tong, L.; Bayer, P.; Janning, P.; Thomashow, L.S.; Mavrodi, D.V.
Structure and function of the phenazine biosynthetic protein PhzF from Pseudomonas fluorescens
Proc. Natl. Acad. Sci. USA
101
16431-16436
2004
Pseudomonas fluorescens (Q51792)
Manually annotated by BRENDA team
Liu, F.; Zhao, Y.; Wang, X.; Hu, H.; Peng, H.; Wang, W.; Wang, J.; Zhang, X.
Elucidation of enzymatic mechanism of phenazine biosynthetic protein PhzF using QM/MM and MD simulations
PLoS ONE
10
e0139081
2015
Pseudomonas fluorescens (Q51792)
Manually annotated by BRENDA team