Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA3456
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: mnmC PA3456
Status: annotated
Amino acids: 654
Structure source: AlphaFold

GO

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. 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:0016645 Catalysis of an oxidation-reduction (redox) reaction in which a CH-NH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor. GO:0004808 Catalysis of the reaction: 5-aminomethyl-2-thiouridine34 in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine34 in tRNA + H+ + S-adenosyl-L-homocysteine. This enzyme specifically adds the terminal methyl group of 5-[(methylamino)methyl]-2-thiouridylate. GO:0032259 The process in which a methyl group is covalently attached to a molecule. GO:0002098 The process in which a uridine at position 34 of a tRNA is post-transcriptionally modified. The wobble nucleoside of the tRNA sequence (position 34) corresponds to the first position of the anticodon.

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 0.67

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MSDFQHAQLDWDENGQPLSRAFGDVYFSRHSGLNETRHVFLATNRLAERFAALGDGEVLCIGETGFGTGLNFLCAWQLFERVAPAGARLEFVSVEKFPLAAADLRRALALWPELAPWSEALLGQYLAVHPGFQRLAFAGGRVGLTLLLGDALECLPQLDARVDAWFLDGFAPAKNPDMWSPVLFAELARLSAPQATLGTFTSAGFVRRGLVEAGFAMQRVPGYGQKREMLSGTYQGPPANAGKPWYARPAPHAGRRAALVVGGGLAGCASAASLAARGWQVTLIERHPGLAREASGNPQGVLYLKLSAHGTPLSRLVLSGFGHTRRLLERLRRGHDWDACGVLQLAFDAKEAQRQAQLAAAFPADLLHGLEREQAERLAGVALPAGGLFYPEAGWVHPPALCQALAATPGITLLSGRAVRLRREGDDWCAYAGDECLARAPLAILATAADIRDFPPAAELPLKRIRGQVTRLPATPQSRALRTVVCAEGYVAPPRGDEHTLGASFDFKSEDLAPTLAEHQGNLELLREISPDLLQRLGADDLPLERLEGRAAFRCTSPDYLPLVGPLAERAAFDEAYAVLARDARQVPERACPWLPGLYLNSGHGSRGLISAPLSGELLAAWICGEPLPLPRAVAEACHPNRFLLRDLVRGQRG

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

9 GO

Gene Ontology (GO)

9

GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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:0016645 Catalysis of an oxidation-reduction (redox) reaction in which a CH-NH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
GO:0004808 Catalysis of the reaction: 5-aminomethyl-2-thiouridine34 in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine34 in tRNA + H+ + S-adenosyl-L-homocysteine. This enzyme specifically adds the terminal methyl group of 5-[(methylamino)methyl]-2-thiouridylate.
GO:0032259 The process in which a methyl group is covalently attached to a molecule.
GO:0002098 The process in which a uridine at position 34 of a tRNA is post-transcriptionally modified. The wobble nucleoside of the tRNA sequence (position 34) corresponds to the first position of the anticodon.
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:0008033 The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group.
GO:0008168 Catalysis of the transfer of a methyl group to an acceptor molecule.

Sequence Features

Domain/signature hits from InterPro and related databases.

21 records

Show feature table

Start	End	DB	Term	Name
257	648	Gene3D	G3DSA:3.50.50.60	-
257	648	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
112	234	Pfam	PF05430	S-adenosyl-L-methionine-dependent methyltransferase
112	234	InterPro	IPR008471	MnmC-like methyltransferase
259	622	Pfam	PF01266	FAD dependent oxidoreductase
259	622	InterPro	IPR006076	FAD dependent oxidoreductase
253	650	PANTHER	PTHR13847	SARCOSINE DEHYDROGENASE-RELATED
258	651	NCBIfam	TIGR03197	FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC
258	651	InterPro	IPR017610	tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC, C-terminal
5	646	Hamap	MF_01102	tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC [mnmC].
5	646	InterPro	IPR023032	tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC
259	650	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
259	650	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
465	543	SUPERFAMILY	SSF54373	FAD-linked reductases, C-terminal domain
17	233	NCBIfam	NF033855	tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD
17	233	InterPro	IPR047785	tRNA mnm(5)s(2)U biosynthesis bifunctional protein MnmC, N-terminal
9	204	SUPERFAMILY	SSF53335	S-adenosyl-L-methionine-dependent methyltransferases
9	204	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
7	239	Gene3D	G3DSA:3.40.50.150	Vaccinia Virus protein VP39
7	239	InterPro	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily
339	557	Gene3D	G3DSA:3.30.9.10	-

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

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA3456	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				0.67
3				0.451
2				0.377

PA3456