Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA5327
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA5327
Status: annotated
Amino acids: 442
Structure source: AlphaFold

GO

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0003885 Catalysis of the reaction: D-arabinono-1,4-lactone + O2 = dehydro-D-arabinono-1,4-lactone + H2O2 + H+. GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. GO:0051872 The chemical reactions and pathways resulting in the breakdown of sphingosine (sphing-4-enine), trans-D-erytho-2-amino-octadec-4-ene-1,3-diol, a long chain amino diol sphingoid base that occurs in most sphingolipids in animal tissues. GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): N
Localization: Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.745

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MVGNPALAELLRAPRLIPWRNWSGAQSCLPLAREAPKDLDELVRIIRQASGRIRPVGSGHSFSALVPTDGTLLSLAYFSGLLSHDSVTLQAEFGGGTPMSQMGAPLKEIGQALVNMADIDYQTLAGAIATSTHGTGVGFGSYSAQVRGLQLVTASGEVLECDAKRNVEVFDAARVSLGALGVVTRVRLQNRAAYRLRERQWIARTEELLEDVEKNTRENQHWEMLVVTHSDYALSIALNETDEPKTPPLDPAKEGGNEFVGLIEGLDKYLSDFPETRRTLLNSLRHFARFDERVDDSYAVYANVRNVRFNEMEYSVPAEHGPACLREILALIRDKDLRTWFPIEYRYVKADDIPLSMFEGRDSCSISVHQHYSMDHHNFFAAVEPIFWKYAGRPHWGKLHGLNAHQLQGLYPRWKAFAEVRQALDPRGRFLNAHLSSILGVT

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

7

GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0003885 Catalysis of the reaction: D-arabinono-1,4-lactone + O2 = dehydro-D-arabinono-1,4-lactone + H2O2 + H+.
GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0051872 The chemical reactions and pathways resulting in the breakdown of sphingosine (sphing-4-enine), trans-D-erytho-2-amino-octadec-4-ene-1,3-diol, a long chain amino diol sphingoid base that occurs in most sphingolipids in animal tissues.
GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0016899 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces an oxygen molecule.

Sequence Features

Domain/signature hits from InterPro and related databases.

21 records

Show feature table

Start	End	DB	Term	Name
310	401	Gene3D	G3DSA:3.30.70.2520	-
19	440	NCBIfam	TIGR01679	FAD-linked oxidoreductase
310	401	FunFam	G3DSA:3.30.70.2520:FF:000002	FAD-linked oxidoreductase
186	436	Pfam	PF04030	D-arabinono-1,4-lactone oxidase
186	436	InterPro	IPR007173	D-arabinono-1,4-lactone oxidase, C-terminal domain
15	189	SUPERFAMILY	SSF56176	FAD-binding/transporter-associated domain-like
15	189	InterPro	IPR036318	FAD-binding, type PCMH-like superfamily
15	79	Gene3D	G3DSA:3.30.43.10	-
15	79	InterPro	IPR016167	FAD-binding, type PCMH, subdomain 1
26	193	ProSiteProfiles	PS51387	PCMH-type FAD-binding domain profile.
26	193	InterPro	IPR016166	FAD-binding domain, PCMH-type
36	161	Pfam	PF01565	FAD binding domain
36	161	InterPro	IPR006094	FAD linked oxidase, N-terminal
11	441	PIRSF	PIRSF000136	LGO_GLO
11	441	InterPro	IPR010031	L-gulonolactone/D-arabinono-1,4-lactone oxidase-like
81	206	Gene3D	G3DSA:3.30.465.10	-
81	206	InterPro	IPR016169	FAD-binding, type PCMH, subdomain 2
404	440	Gene3D	G3DSA:1.10.45.10	-
404	440	InterPro	IPR016171	Vanillyl-alcohol oxidase, C-terminal subdomain 2
19	439	PANTHER	PTHR43762	L-GULONOLACTONE OXIDASE
19	439	InterPro	IPR010031	L-gulonolactone/D-arabinono-1,4-lactone oxidase-like

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA5327	AlphaFold	—	—	full sequence	—	Viewing

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
1				0.745
6				0.441

PA5327