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Information on EC 3.1.2.28 - 1,4-dihydroxy-2-naphthoyl-CoA hydrolase and Organism(s) Synechocystis sp. and UniProt Accession Q55777

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.28 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
IUBMB Comments
This enzyme participates in the synthesis of menaquinones , phylloquinone , as well as several plant pigments [1,2]. The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 does not accept benzoyl-CoA or phenylacetyl-CoA as substrates .
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This record set is specific for:
Synechocystis sp.
UNIPROT: Q55777
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Word Map
The taxonomic range for the selected organisms is: Synechocystis sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dhna-coa thioesterase, slr0204, atdhnat1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DHNA-CoA thioesterase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
-
SYSTEMATIC NAME
IUBMB Comments
1,4-dihydroxy-2-naphthoyl-CoA hydrolase
This enzyme participates in the synthesis of menaquinones [4], phylloquinone [3], as well as several plant pigments [1,2]. The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 does not accept benzoyl-CoA or phenylacetyl-CoA as substrates [3].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4-dihydroxy-2-naphthoyl-CoA + H2O
CoA + 1,4-dihydroxy-2-naphthoate
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
1,4-dihydroxy-2-naphthoyl-CoA + H2O
CoA + 1,4-dihydroxy-2-naphthoate
show the reaction diagram
the reaction is involved in phylloquinone (vitamin K1) biosynthesis
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
knockout mutant accumulates 1,4-dihydroxy-2-naphthoyl-CoA, contains 13fold less phylloquinone than the wild-type and displays typical photosensitivity to high light intensities associated with phylloquinone deficiency in cyanobacteria
physiological function
the reaction is involved in phylloquinone (vitamin K1) biosynthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15478
x * 15478, calculated from sequence
15700
4 * 15700, calculated
77400
sedimentation-equilibrium ultracentrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 15478, calculated from sequence
tetramer
4 * 15700, calculated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.9 A resolution. The core structure is defined by a 5-6-stranded antiparallel beta-sheet that partially wraps around a prominent five-turn alpha-helix. Isoform Slr0204 has a 25-amino-acid extension at its C-terminus, residues 113-138. Slr0204 is a facial tetramer that features a dimer-dimer interface near the hotdog alpha-helices, which point inward towards the center of the tetramer. The binding site for substrate 1,4-dihydroxy-2-naphthoyl-CoA spans the dimer interface
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D16N
active site mutant, modeling of substrate bound to active site
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a recombinant His-fusion protein
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Widhalm, J.R.; van Oostende, C.; Furt, F.; Basset, G.J.
A dedicated thioesterase of the Hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1
Proc. Natl. Acad. Sci. USA
106
5599-5603
2009
Synechocystis sp. (Q55777)
Manually annotated by BRENDA team
Furt, F.; Allen, W.J.; Widhalm, J.R.; Madzelan, P.; Rizzo, R.C.; Basset, G.; Wilson, M.A.
Functional convergence of structurally distinct thioesterases from cyanobacteria and plants involved in phylloquinone biosynthesis
Acta Crystallogr. Sect. D
69
1876-1888
2013
Arabidopsis thaliana (Q9SX65), Arabidopsis thaliana, Synechocystis sp. (Q55777), Synechocystis sp.
Manually annotated by BRENDA team