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Information on EC 4.1.3.27 - anthranilate synthase and Organism(s) Pseudomonas aeruginosa and UniProt Accession P20580

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.27 anthranilate synthase
IUBMB Comments
In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase ), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)]. The native enzyme in the complex uses either glutamine or, less efficiently, NH3. The enzyme separated from the complex uses NH3 only.
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This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: P20580 not found.
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
anthranilate synthase, anthranilate synthetase, oasa1d, oasa1, oasa2, phnab, anthranilate synthase component i, trped, anthranilate synthase-phosphoribosyltransferase, caasa1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
anthranilate synthase
-
-
-
-
anthranilate synthetase
-
-
-
-
chorismate lyase
-
-
-
-
Glutamine amido-transferase
-
-
-
-
Glutamine amidotransferase
-
-
-
-
PhnAB anthranilate synthase
-
-
synthase, anthranilate
-
-
-
-
synthetase, anthranilate
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
chorismate pyruvate-lyase (amino-accepting; anthranilate-forming)
In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase ), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)]. The native enzyme in the complex uses either glutamine or, less efficiently, NH3. The enzyme separated from the complex uses NH3 only.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-59-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
TrpE and PhnA sequences reveal the evolutionary relationships of each anthranilate synthase enzyme to those of other species, phylogenetic analysis and tree, overview. TrpEG are most closely related to anthranilate synthases from other members of the fluorescent pseudomonad family, while PhnAB are most closely related to anthranilate synthases from more distantly related organisms. The absence of a phnAB-like operon in other pseudomonads is evidence that PhnAB acquisition occurred after the family's diversification
malfunction
metabolism
physiological function
conversion of the central metabolite chorismate to anthranilate by anthranilate synthase is required for Pseudomonas quinolone signal 2-heptyl-3-hydroxy-4-quinolone, PQS, biosynthesis. The reaction is also the first step in tryptophan biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8G4B9M0_PSEAI
530
0
58684
TrEMBL
-
A0A8G2VJU6_PSEAI
492
0
54526
TrEMBL
-
A0A7M3AZV9_PSEAI
530
0
58575
TrEMBL
-
A0A0A8RC77_PSEAI
496
0
55086
TrEMBL
-
A0A3S3XX33_PSEAI
492
0
54613
TrEMBL
-
A0A8G1VB95_PSEAI
200
0
21826
TrEMBL
-
A0A659BU98_PSEAI
530
0
58632
TrEMBL
-
A0A7M3A042_PSEAI
492
0
54541
TrEMBL
-
A0A8G2KY59_PSEAI
530
0
58695
TrEMBL
-
A0A2U2XSW6_PSEAI
530
0
58598
TrEMBL
-
A0A8G5MNI7_PSEAI
530
0
58612
TrEMBL
-
A0A8G7CZR4_PSEAI
530
0
58579
TrEMBL
-
A0A8G4D5E2_PSEAI
530
0
58628
TrEMBL
-
A0A8G6VS78_PSEAI
530
0
58626
TrEMBL
-
A0A8B5BN22_PSEAI
530
0
58664
TrEMBL
-
A0A8G3YEX3_PSEAI
492
0
54621
TrEMBL
-
A0A8G4ACD0_PSEAI
530
0
58637
TrEMBL
-
A0A8G3CGF4_PSEAI
492
0
54525
TrEMBL
-
A0A5F1BU06_PSEAI
136
0
14654
TrEMBL
-
A0A8G4YH70_PSEAI
492
0
54575
TrEMBL
-
A0A1Y0GNJ5_PSEAI
201
0
22046
TrEMBL
-
A0A8G3NSV8_PSEAI
492
0
54617
TrEMBL
-
A0A8G3JPH6_PSEAI
530
0
58695
TrEMBL
-
A0A8F9JPK7_PSEAI
530
0
58536
TrEMBL
-
A0A2R3IPY5_PSEAI
627
0
69181
TrEMBL
-
A0A2R3INE7_PSEAI
627
0
69207
TrEMBL
-
A0A8G6ZYF2_PSEAI
530
0
58624
TrEMBL
-
A0A232D828_PSEAI
530
0
58546
TrEMBL
-
A0A8G5U7U7_PSEAI
492
0
54583
TrEMBL
-
A0A3M5D8P8_PSEAI
496
0
55101
TrEMBL
-
A0A8G4DC06_PSEAI
530
0
58536
TrEMBL
-
A0A8G2NLT2_PSEAI
530
0
58628
TrEMBL
-
A0A8G7CN02_PSEAI
530
0
58539
TrEMBL
-
A0A8G7HSL4_PSEAI
530
0
58565
TrEMBL
-
A0A8G4N074_PSEAI
492
0
54456
TrEMBL
-
A0A485FUM5_PSEAI
523
0
57787
TrEMBL
-
A0A8G7LQ44_PSEAI
492
0
54597
TrEMBL
-
A0A8A4FZI8_PSEAI
530
0
58653
TrEMBL
-
A0A8G6L814_PSEAI
530
0
58597
TrEMBL
-
A0A509JKD4_PSEAI
492
0
54615
TrEMBL
-
A0A5E9W713_PSEAI
492
0
54572
TrEMBL
-
A0A8G7AFG4_PSEAI
530
0
58596
TrEMBL
-
A0A4P0TK70_PSEAI
64
0
7312
TrEMBL
-
A0A8G6U695_PSEAI
492
0
54571
TrEMBL
-
A0A8G4NV17_PSEAI
530
0
58656
TrEMBL
-
A0A080VNV3_PSEAI
200
0
21845
TrEMBL
-
A0A8G4AFD8_PSEAI
530
0
58614
TrEMBL
-
A0A3M5E1H6_PSEAI
523
0
57831
TrEMBL
-
A0A8G4MLL7_PSEAI
492
0
54617
TrEMBL
-
A0A6A9K0P1_PSEAI
492
0
54471
TrEMBL
-
A0A2R3ISP2_PSEAI
201
0
22122
TrEMBL
-
A0A8G7KHN6_PSEAI
492
0
54573
TrEMBL
-
A0A2R3J088_PSEAI
491
0
54305
TrEMBL
-
A0A8F8QYL5_PSEAI
530
0
58588
TrEMBL
-
A0A8G2VHV7_PSEAI
523
0
57914
TrEMBL
-
A0A8G5NC17_PSEAI
492
0
54614
TrEMBL
-
A0A6A9JZ93_PSEAI
530
0
58478
TrEMBL
-
A0A8G7SNY1_PSEAI
492
0
54522
TrEMBL
-
A0A8G3ALG8_PSEAI
530
0
58725
TrEMBL
-
A0A8G6YLS6_PSEAI
492
0
54529
TrEMBL
-
A0A8G5Q9N6_PSEAI
492
0
54583
TrEMBL
-
A0A485HIR0_PSEAI
491
0
54309
TrEMBL
-
A0A3S0J4K8_PSEAI
530
0
58533
TrEMBL
-
A0A8F9JPS6_PSEAI
492
0
54587
TrEMBL
-
A0A8G7PTQ8_PSEAI
530
0
58645
TrEMBL
-
A0A8G6CW88_PSEAI
492
0
54601
TrEMBL
-
A0A8G6II33_PSEAI
530
0
58584
TrEMBL
-
A0A8G4Z872_PSEAI
530
0
58545
TrEMBL
-
A0A8G7N9N8_PSEAI
530
0
58611
TrEMBL
-
A0A4P0V8V9_PSEAI
638
0
69853
TrEMBL
-
A0A444M6D4_PSEAI
530
0
58483
TrEMBL
-
A0A1Y0GMJ7_PSEAI
492
0
54555
TrEMBL
-
A0A8B5AJ00_PSEAI
530
0
58640
TrEMBL
-
A0A8G6T0E3_PSEAI
492
0
54587
TrEMBL
-
A0A4P0TKP5_PSEAI
500
0
55291
TrEMBL
-
A0A4P0TJ31_PSEAI
137
0
15070
TrEMBL
-
A0A8G3VRR0_PSEAI
492
0
54654
TrEMBL
-
A0A5E9LQK2_PSEAI
530
0
58626
TrEMBL
-
A0A8G4EY77_PSEAI
492
0
54602
TrEMBL
-
A0A8G4E4Y8_PSEAI
492
0
54573
TrEMBL
-
A0A8B4ZH96_PSEAI
530
0
58628
TrEMBL
-
A0A8G5HEI2_PSEAI
492
0
54601
TrEMBL
-
A0A8B5A0H5_PSEAI
492
0
54561
TrEMBL
-
A0A2R3IVA7_PSEAI
492
0
54339
TrEMBL
-
A0A0A8RD07_PSEAI
627
0
68938
TrEMBL
-
A0A0D7MPU3_PSEAI
492
0
54587
TrEMBL
-
A0A241XE92_PSEAI
627
0
69009
TrEMBL
-
A0A8G2S562_PSEAI
530
0
58670
TrEMBL
-
A0A8G2XRH8_PSEAI
530
0
58642
TrEMBL
-
A0A8G4HHF9_PSEAI
530
0
58641
TrEMBL
-
A0A8G3TNE7_PSEAI
492
0
54587
TrEMBL
-
A0A8G7BSJ4_PSEAI
530
0
58484
TrEMBL
-
A0A8G4KKZ8_PSEAI
530
0
58626
TrEMBL
-
A0A0F6RPJ2_PSEAI
492
0
54587
TrEMBL
-
A0A8F9JHM4_PSEAI
530
0
58536
TrEMBL
-
A0A485FT70_PSEAI
492
0
54294
TrEMBL
-
A0A8F9KGA7_PSEAI
530
0
58624
TrEMBL
-
A0A2R3J3W7_PSEAI
200
0
21837
TrEMBL
-
A0A263PVN5_PSEAI
201
0
22059
TrEMBL
-
A0A0A8RJ37_PSEAI
523
0
57759
TrEMBL
-
A0A8G1K2S7_PSEAI
530
0
58612
TrEMBL
-
A0A8H0X3Z6_PSEAI
530
0
58584
TrEMBL
-
A0A5E5QWF6_PSEAI
523
0
57789
TrEMBL
-
A0A0A8R9Z4_PSEAI
201
0
22105
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18000
-
1 * 18000 + 1 * 64000
64000
-
1 * 18000 + 1 * 64000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
1 * 18000 + 1 * 64000
additional information
-
the large component from Bacillus subtilis (IB) complements well with the small component from Pseudomonas aeruginosa (IIP) to reconstitute a glutamine-reactive anthranilate synthase. Complementation was also observed with the large component from Pseudomonas aeruginosa (Iv) and the small subunit from Bacillus subtilis (IIB)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of the genes phnA and phnB of the anthranilate synthase that participates in the synthesis of pyocyanin
-
gene phnAB, phylogenetic analysis, cloning in Escherichia coli strain Dh5alpha, enzyme expression in an enzyme-deficient Pseudomonas aeruginosa strain. Overexpression of anthranilate synthase genes trpE and phnAB results in pathway crosstalk, overview
gene trpE, phylogenetic analysis, cloning in Escherichia coli strain Dh5alpha, enzyme expression in an enzyme-deficient Pseudomonas aeruginosa strain. Overexpression of anthranilate synthase genes trpE and phnAB results in pathway crosstalk, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zalkin, H.
Anthranilate synthetase
Adv. Enzymol. Relat. Areas Mol. Biol.
38
1-39
1973
Klebsiella aerogenes, Aspergillus nidulans, Bacillus subtilis, Saccharomyces cerevisiae, Chromobacterium violaceum, Delftia acidovorans, Comamonas testosteroni, Escherichia coli, Neurospora crassa, Pseudomonas aeruginosa, Pseudomonas putida, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens
Manually annotated by BRENDA team
Essar, D.W.; Eberly, L.; Hadero, A.; Crawford, I.P.
Identification and characterization of genes for a second anthranilate synthase in Pseudomonas aeruginosa: interchangeability of the two anthranilate synthases and evolutionary implications
J. Bacteriol.
172
884-900
1990
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Patel, N.; Holmes, W.M.; Kane, J.F.
Intergeneric complementation of anthranilate synthase subunits
J. Bacteriol.
114
600-602
1973
Bacillus subtilis, Pseudomonas aeruginosa
Manually annotated by BRENDA team
Farrow, J.M.; Pesci, E.C.
Two distinct pathways supply anthranilate as a precursor of the Pseudomonas quinolone signal
J. Bacteriol.
189
3425-3433
2007
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Palmer, G.C.; Jorth, P.A.; Whiteley, M.
The role of two Pseudomonas aeruginosa anthranilate synthases in tryptophan and quorum signal production
Microbiology
159
959-969
2013
Pseudomonas aeruginosa (P09785 and P09786), Pseudomonas aeruginosa (P20576 and P20580), Pseudomonas aeruginosa
Manually annotated by BRENDA team