Protein profile

PA0420

adenosylmethionine--8-amino-7-oxononanoate aminotransferase BioA

Genome: NC_002516.2

Gene: bioA PA0420 Structure source: AlphaFold UniProt Q9I693
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Amino acids 467
Annotations 7
Features 18
PDB binders 12
Druggability 0.735

Overview

Basic information about this protein and its source genome.

Accession
PA0420
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
bioA PA0420
Status
annotated
Amino acids
467
Structure source
AlphaFold
EC
2.6.1.62
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0004015 Catalysis of the reaction: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate. GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. GO:0009102 The chemical reactions and pathways resulting in the formation of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid. GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. GO:0008483 Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
28.774
Human E-value
1.22e-38
Gut microbiome off-target
hit
Essential (DEG)
Y
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 0.735
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MGLNADWMQRDLNVLWHPCTQMKDHERLPVIPIRRGEGVWLEDFEGKRYIDAVSSWWVNVFGHANPRINQRIKDQVDQLEHVILAGFSHQPVIELSERLVKITPPGLDRVFYADSGSAGIEVALKMSYHFWLNSGRPRKKRFVTLTNSYHGETIAAMSVGDVALFTETYKSLLLDTIKVPSPDCFLRPDGMCWEEHSRNMFAHMERTLAEGHDEIAAVIVEPLIQGAGGMRMYHPVYLKLLREACDRYGVHLIHDEIAVGFGRTGTMFACEQAGIAPDFLCLSKALTGGYLPMSAVLTSETIYRGFYDDYQTLRAFLHSHTYTGNPLACAAALATLDIFEEDKVIEANRALSTHMARATAHLADHPHVAEVRQTGMVLAIEMVQDKASRTPYPWQERRGLKVFQHGLERGALLRPLGSVVYFLPPYVITPEQIDFLAEVASEGIDIATRDAVSVAVSDFHPDHRDPG

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0004015 Catalysis of the reaction: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate.
  • GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
  • GO:0009102 The chemical reactions and pathways resulting in the formation of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid.
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
  • GO:0008483 Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.

Sequence Features

Domain/signature hits from InterPro and related databases.

18 records
Show feature table
Start End DB Term Name
65 342 FunFam G3DSA:3.40.640.10:FF:000078 Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
10 442 SUPERFAMILY SSF53383 PLP-dependent transferases
10 442 InterPro IPR015424 Pyridoxal phosphate-dependent transferase
252 289 ProSitePatterns PS00600 Aminotransferases class-III pyridoxal-phosphate attachment site.
252 289 InterPro IPR005814 Aminotransferase class-III
29 438 Pfam PF00202 Aminotransferase class-III
29 438 InterPro IPR005814 Aminotransferase class-III
14 440 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
14 440 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain
7 444 CDD cd00610 OAT_like
7 444 InterPro IPR005814 Aminotransferase class-III
7 444 Hamap MF_00834 Adenosylmethionine-8-amino-7-oxononanoate aminotransferase [bioA].
7 444 InterPro IPR005815 Adenosylmethionine--8-amino-7-oxononanoate aminotransferase BioA
68 344 Gene3D G3DSA:3.40.640.10 -
68 344 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major domain
9 444 PANTHER PTHR42684 ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE
15 442 NCBIfam TIGR00508 adenosylmethionine--8-amino-7-oxononanoate transaminase
15 442 InterPro IPR005815 Adenosylmethionine--8-amino-7-oxononanoate aminotransferase BioA

3D Structure

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

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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 PA0420
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 0.735
20 0.264
2 0.219

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

62 records

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
3G8
4W1W
P9WQ80 327.4 Da LogP 3.93 TPSA 50.5 ✓ Ro5 ✓ Clean CCN(CC)c1ccc2c(c1)OC(=O)C(=C2)C(=O)c3cccs3
3G9
4W1X
P9WQ80 342.8 Da LogP 3.51 TPSA 40.6 ✓ Ro5 ✓ Clean CC(=O)c1ccc(cc1)N2CCN(CC2)C(=O)c3cccc(c3)Cl
3GS
4W1V
P9WQ80 351.4 Da LogP 2.09 TPSA 74.6 ✓ Ro5 ✓ Clean COC(=O)c1c2n(c(c1C(=O)OC)c3cccc(c3)F)C[S@](=O)C2
6SQ
5KGT
P0A4X7 341.8 Da LogP 4.64 TPSA 37.4 ✓ Ro5 ✓ Clean CC(=O)c1ccc(cc1)N2CCC(CC2)C(=O)c3cccc(c3)Cl
6SR
5KGS
P0A4X7 364.4 Da LogP 2.51 TPSA 59.1 ✓ Ro5 ✓ Clean c1cc2c(cc1C(=O)N3CCN(CC3)c4ccc5c(c4)CCC5=O)OCO2
7B9
5TE2
P0A4X7 399.3 Da LogP 0.93 TPSA 165.0 1 viol. ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CNC2=CNC(=CC2=O)CCCO)O
ACZ
1MLY
P12995 196.2 Da LogP 0.25 TPSA 89.3 ✓ Ro5 ✓ Clean C1=CC(C=CC1CC[C@@H](C(=O)O)N)N
J4J
6ED7
P12995 227.2 Da LogP 0.68 TPSA 98.3 ✓ Ro5 ✓ Clean c1ccc(c(c1)[N+](=O)[O-])SCC(=O)NN
KAP
1QJ3
P12995 187.2 Da LogP 0.94 TPSA 80.4 ✓ Ro5 ✓ Clean C[C@@H](C(=O)CCCCCC(=O)O)N
LLP
6WNN
P53555 375.3 Da LogP 0.71 TPSA 175.6 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)/C=N/CCCCC(C(=O)O)N)O
PMP
6WNN
P53555 248.2 Da LogP 0.16 TPSA 125.9 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN)O
TAR
5UC7
D2TPI3 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@H]([C@@H](C(=O)O)O)(C(=O)O)O

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.