Protein target profile

KP13_04825

High-molecular-weight protein 1

Genome: KpKP13 Gene: AHE43792.1 irp1 3D evidence: Unavailable UniProt A0A0H3GQF9
Export view
Length 3163
Direct ligand evidence 0 59 total records
Functional annotation 0 EC 13 GO
Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Ligand evidence via structure/bioactivity 9 structural and 0 bioactivity records.

Risks to review

Human similarity Top human hit identity: 31.071%. Microbiome similarity 4 of 4744 screened genomes (0.1%) have a significant similarity hit. Mixed conservation Core/accessory calls are not fully concordant.

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein. No FPocket pocket score No selected computational pocket-druggability value is available. No P2Rank pocket score No second computational pocket-prediction value is available. No structure loaded No structure/model is available for visual inspection.
Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target
Hit
Human identity (%)
31.071 Lower values reduce human off-target concern.
Human E-value
1.59e-25
Gut microbiome similarity
0.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG)
N
DEG identity (%)
0.0 Higher values support similarity to known essential genes.

Localization

Localization
CytoplasmicMembrane
Core conservation Accessory gene
Roary accessory
CoreCruncher accessory
Gut microbiome 4 / 4744 genomes with a hit
Prevalence 0.1%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GQF9

Sequence

Primary amino-acid sequence viewer.

MDNLRFSSAPTADSIDASIAQHYPDCEPVAVIGYACHFPESPDGETFWQNLLEGRECSRRFTREELLAVGLDAAIIDDPHYVNIGTVLDNADCFDATLFGYSRQEAESMDPQQRLFLQAVWHALEHAGYAPGAVPHKTGVFASSRMSTYPGREALNVTEVAQVKGLQSLMGNDKDYIATRAAYKLNLHGPALSVQTACSSSLVAVHLACESLRAGESDMAVAGGVALSFPQQAGYRYQPGMIFSPDGHCRPFDASAEGTWAGNGLGCVVLRRLRDALLSGDPIISVILSSAVNNDGNRKVGYTAPSVAGQQAVIEEALMLAAIDDRQVGYIETHGTGTPLGDAIEIEALRNVYAPRPQDQRCALGSVKSNMGHLDTAAGIAGLLKTVLAVSRGQIPPLLNFHTPNPALKLEESPFTIPVSAQAWQDEMRYAGVSSFGIGGTNCHMIVASLPDALNARLPNTDSGRKSTALLLSAASDSALRRLATDYAGALRENADASSLAFTALHARRLDLPFRLAAPLNRETAEALSAWAGEKSGALVYSGHGASGKQVWLFTGQGSHWRTMGQTMYQHSTAFADTLDRCFSACSEMLTPSLREAMFNPDSAQLDNMAWAQPAIVAFEIAMAAHWRAEGLKPDFAIGHSVGEFAAAVVCGHYTIEQVMPLVCRRGALMQQCASGAMVAVFADEDTLMPLARQFELDLAANNGTQHTVFSGPEAHLAVFCATLSQHDINYRRLSVTGAAHSALLEPILDRFQDACAGLHAEPGQIPIISTLTADVIDESTLNQADYWRRHMRQPVRFIQSIQVAHQLGARVFLEMGPDAQLVACGQREYRDNAYWIASARRNKEASDVLNQALLQLYAAGVALPWADLLAGDGQRIAAPCYPFDTERYWKERVSPACEPADAALSAGLEVASRAATALDLPRLEALKQCATRLHAIYVDQLVQRCTGDAIENGVDAMTIMRRGRLLPRYQQLLQRLLNNCVVDGDYRCTDGRYVRARPIEHQQRESLLTELAGYCEGFQAIPDTIARAGDRLYEMMSGAEEPVAIIFPQSASDGVEVLYQEFSFGRYFNQIAAGVLRGIVQTRQPRQPLRILEVGGGTGGTTAWLLPELNGVPALEYHFTDISALFTRRAQQKFADYDFVKYSELDLEKEAQSQGFQAQSYDLIVAANVIHATRHIGRTLDNLRPLLKPGGRLLMREITQPMRLFDFVFGPLVLPLQDLDAREGELFLTTAQWQQQCRHAGFSKVAWLPQDGSPTAGMSEHIILATLPGQAVSAVTFTAPSEPVLGQALTDNGDYLADWSDCAGQPERFNARWQEAWRLLSQRHGDALPVEPPPVAAPEWLGKVRLSWQNEAFSRGQMRVEARHPAGEWLPLSPAAPLPAPQTHYQWRWTPLNVASIDHPLTFSFSAGTLARSDELAQYGIIHDPHASSRLMIVEESEDTLALAEKVIAALTASAAGLIVVTRRAWRVEENEALSASHHALWALLRVAANEQPERLLAAIDLAENTPWETLHQGLSAVSLSQRWLAARGDTLWLPSLAPNTGCAAELPANVFTGDSRWHLVTGAFGGLGRLAVNWLREKGARRIALLAPRVDESWLRDVEGGQTRVCRCDVGDAGQLATVLDDLAANGGIAGAIHAAGVLADAPLQELDDHQLAAVFAVKAQAASQLLQTLRNHDGRYLILYSSAAATLGAPGQSAHALACGYLDGLAQQFSTLDAPKTLSVAWGAWGESGRAATPEMLATLASRGMGALSDAEGCWHLEQAVMRGAPWRLAMRVFTDKMPPLQQALFNISATEKAATPVIPPADDNAFNGSLSDETAVMAWLKKRIAVQLRLSDPASLHPNQDLLQLGMDSLLFLELSSDIQHYLGVRINAERAWQDLSPHGLTQLICSKPEATPAASQPEVLRHDADERYAPFPLTPIQHAYWLGRTHLIGYGGVACHVLFEWDKRHDEFDLAILEKAWNQLIARHDMLRMVVDADGQQRILATTPEYHIPRDDLRALSPEEQRIALEKRRHELSYRVLPADQWPLFELVVSEIDDCHYRLHMNLDLLQFDVQSFKVMMDDLAQVWRGETLAPLAITFRDYVMAEQARRQTSAWHDAWDYWQEKLPQLPLAPELPVVETPPETPHFTTFKSTIGKTEWQAVKQRWQQQGVTPSAALLTLFAATLERWSRTTTFTLNLTFFNRQPIHPQINQLIGDFTSVTLVDFNFSAPVTLQEQMQQTQQRLWQNMAHSEMNGVEVIRELGRLRGSQRQPLMPVVFTSMLGMTLEGMTIDQAMSHLFGEPCYVFTQTPQVWLDHQVMESDGELMFSWYCMDNVLEPGAAEAMFNDYCAILQAVIAAPESLKTLTSGIAGHIPRRRWPLNAQADYDLRDIEQATLEYPGIRQARAEITEQGALTLDIVMADDPSPSAAMPDEHELTQLALPLPEQAQLDELEATWRWLEARALQGIAATLNRHGLFTTPEIAHRFSAIVQALSAQASHQRLLRQWLQCLTEREWLIREGESWRCRIPLSEIPEPQEACPQSQWSQALAQYLETCIARHDALFSGQCSPLELLFNEQHRVTDALYRDNPASACLNRYTAQIAALCSAERILEVGAGTAATTAPVLKATRNTRQSYHFTDVSAQFLNDARARFHDESQVSYALFDINQPLDFTAHPEAGYDLIVAVNVLHDASHVVQTLRRLKLLLKAGGRLLIVEATERNSVFQLASVGFIEGLSGYRDFRRRDEKPMLTRSAWQEVLVQAGFANELAWPAQESSPLRQHLLVARSPGVNRPDKKAVSRYLQQRFGTGLPILQIRQREALFTPLHAPSDAPTEPAKPTPVAGGNPALEKQVAELWQSLLSRPVARHHDFFELGGDSLMATRMVAQLNRRGIARANLQDLFSHSTLSDFCAHLQAATSGEDNPIPLCQGDGEETLFVFHASDGDISAWLPLASALNRRVFGLQAKSPQRFATLDQMIDEYVGCIRRQQPHGPYVLAGWSYGAFLAAGAAQRLYAKGEQVRMVLIDPVCRQDFCCENRAALLRLLAEGQTPLALPEHFDQQTPDSQLADFISLAKTAGMVSQNLTLQAAETWLDNIAHLLRLLTEHTPGESVPVPCLMVYAAGRPARWTPAETEWQGWINNADDAVIEASHWQIMMEAPHVQACAQHITRWLCATSTQPENSL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

13 GO

Gene Ontology (GO)

13
  • GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
  • GO:0004315 Catalysis of the reaction: acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein].
  • GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
  • GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
  • GO:0031177 Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate).
  • 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:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
  • GO:0004312 Catalysis of the reaction: acetyl-CoA + n malonyl-CoA + 2n NADPH + 2n H+ = long-chain fatty acid + n+1 CoA + n CO2 + 2n NADP+.
  • GO:0016874 Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient.
  • GO:0071770 The aggregation, arrangement and bonding together of a set of components, including (phenyl)phthiocerol, phthiodiolone, phthiotriol dimycocerosate and diphthioceranate, to form the DIM/DIP layer of the Actinobacterium-type cell wall.
  • GO:0009403 The chemical reactions and pathways resulting in the formation of toxin, a poisonous compound (typically a protein) that is produced by cells or organisms and that can cause disease when introduced into the body or tissues of an organism.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

96 records
Show feature table
Start End DB Term Name
551 846 Pfam PF00698 Acyl transferase domain
551 846 InterPro IPR014043 Acyl transferase
1948 2263 Pfam PF00668 Condensation domain
1948 2263 InterPro IPR001242 Condensation domain
2575 2750 SUPERFAMILY SSF53335 S-adenosyl-L-methionine-dependent methyltransferases
2575 2750 InterPro IPR029063 S-adenosyl-L-methionine-dependent methyltransferase superfamily
1560 1729 Pfam PF08659 KR domain
1560 1729 InterPro IPR013968 Polyketide synthase, ketoreductase domain
3163 3163 Coils Coil Coil
551 847 Gene3D G3DSA:3.40.366.10 -
551 847 InterPro IPR001227 Acyl transferase domain superfamily
2824 2898 ProSiteProfiles PS50075 Carrier protein (CP) domain profile.
2824 2898 InterPro IPR009081 Phosphopantetheine binding ACP domain
1557 1786 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
1557 1786 InterPro IPR036291 NAD(P)-binding domain superfamily
2813 2902 Gene3D G3DSA:1.10.1200.10 -
2813 2902 InterPro IPR036736 ACP-like superfamily
550 835 SUPERFAMILY SSF52151 FabD/lysophospholipase-like
550 835 InterPro IPR016035 Acyl transferase/acyl hydrolase/lysophospholipase
997 1255 Gene3D G3DSA:3.40.50.150 Vaccinia Virus protein VP39
997 1255 InterPro IPR029063 S-adenosyl-L-methionine-dependent methyltransferase superfamily
2444 2767 Gene3D G3DSA:3.40.50.150 Vaccinia Virus protein VP39
2444 2767 InterPro IPR029063 S-adenosyl-L-methionine-dependent methyltransferase superfamily
27 447 CDD cd00833 PKS
2096 2343 FunFam G3DSA:3.30.559.30:FF:000006 Yersiniabactin polyketide/non-ribosomal peptide synthetase
19 473 Gene3D G3DSA:3.40.47.10 -
19 473 InterPro IPR016039 Thiolase-like
1823 1889 Pfam PF00550 Phosphopantetheine attachment site
1823 1889 InterPro IPR009081 Phosphopantetheine binding ACP domain
2832 2894 Pfam PF00550 Phosphopantetheine attachment site
2832 2894 InterPro IPR009081 Phosphopantetheine binding ACP domain
1818 1902 Gene3D G3DSA:1.10.1200.10 -
1818 1902 InterPro IPR036736 ACP-like superfamily
2905 3157 Gene3D G3DSA:3.40.50.1820 alpha/beta hydrolase
2905 3157 InterPro IPR029058 Alpha/Beta hydrolase fold
27 276 Pfam PF00109 Beta-ketoacyl synthase, N-terminal domain
27 276 InterPro IPR014030 Beta-ketoacyl synthase, N-terminal
2095 2347 Gene3D G3DSA:3.30.559.30 Nonribosomal peptide synthetase, condensation domain
1435 1776 CDD cd05274 KR_FAS_SDR_x
285 401 Pfam PF02801 Beta-ketoacyl synthase, C-terminal domain
285 401 InterPro IPR014031 Beta-ketoacyl synthase, C-terminal
2918 3152 SMART SM00824 Thioesterase
2918 3152 InterPro IPR020802 Polyketide synthase, thioesterase domain
2853 2868 ProSitePatterns PS00012 Phosphopantetheine attachment site.
2853 2868 InterPro IPR006162 Phosphopantetheine attachment site
1910 2088 FunFam G3DSA:3.30.559.10:FF:000023 Non-ribosomal peptide synthetase
2830 2898 SMART SM00823 Phosphopantetheine attachment site
2830 2898 InterPro IPR020806 Polyketide synthase, phosphopantetheine-binding domain
1821 1893 SMART SM00823 Phosphopantetheine attachment site
1821 1893 InterPro IPR020806 Polyketide synthase, phosphopantetheine-binding domain
2098 2343 SUPERFAMILY SSF52777 CoA-dependent acyltransferases
1818 1893 ProSiteProfiles PS50075 Carrier protein (CP) domain profile.
1818 1893 InterPro IPR009081 Phosphopantetheine binding ACP domain
1435 1455 Coils Coil Coil
1915 2341 CDD cd19535 Cyc_NRPS
1911 2109 SUPERFAMILY SSF52777 CoA-dependent acyltransferases
1558 1731 SMART SM00822 This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
2828 2894 SUPERFAMILY SSF47336 ACP-like
2828 2894 InterPro IPR036736 ACP-like superfamily
189 205 ProSitePatterns PS00606 Ketosynthase family 3 (KS3) active site signature.
189 205 InterPro IPR018201 Beta-ketoacyl synthase, active site
2915 3006 Pfam PF00975 Thioesterase domain
2915 3006 InterPro IPR001031 Thioesterase
26 449 ProSiteProfiles PS52004 Ketosynthase family 3 (KS3) domain profile.
26 449 InterPro IPR020841 Polyketide synthase, beta-ketoacyl synthase domain
1093 1194 Pfam PF08242 Methyltransferase domain
1093 1194 InterPro IPR013217 Methyltransferase type 12
2593 2693 Pfam PF08242 Methyltransferase domain
2593 2693 InterPro IPR013217 Methyltransferase type 12
1762 3021 PANTHER PTHR43775 FATTY ACID SYNTHASE
1848 1863 ProSitePatterns PS00012 Phosphopantetheine attachment site.
1848 1863 InterPro IPR006162 Phosphopantetheine attachment site
1366 1540 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
1366 1540 InterPro IPR036291 NAD(P)-binding domain superfamily
29 452 SMART SM00825 Beta-ketoacyl synthase
29 452 InterPro IPR020841 Polyketide synthase, beta-ketoacyl synthase domain
1817 1928 SUPERFAMILY SSF47336 ACP-like
1817 1928 InterPro IPR036736 ACP-like superfamily
2898 3152 SUPERFAMILY SSF53474 alpha/beta-Hydrolases
2898 3152 InterPro IPR029058 Alpha/Beta hydrolase fold
474 890 Gene3D G3DSA:3.30.70.3290 -
23 496 FunFam G3DSA:3.40.47.10:FF:000042 Polyketide synthase Pks13
23 447 SUPERFAMILY SSF53901 Thiolase-like
23 447 InterPro IPR016039 Thiolase-like
675 736 SUPERFAMILY SSF55048 Probable ACP-binding domain of malonyl-CoA ACP transacylase
675 736 InterPro IPR016036 Malonyl-CoA ACP transacylase, ACP-binding
404 515 Pfam PF16197 Ketoacyl-synthetase C-terminal extension
404 515 InterPro IPR032821 Polyketide synthase, C-terminal extension
2805 2826 MobiDBLite mobidb-lite consensus disorder prediction
1910 2090 Gene3D G3DSA:3.30.559.10 -
1910 2090 InterPro IPR023213 Chloramphenicol acetyltransferase-like domain superfamily
1345 1795 Gene3D G3DSA:3.40.50.720 -
1060 1250 SUPERFAMILY SSF53335 S-adenosyl-L-methionine-dependent methyltransferases
1060 1250 InterPro IPR029063 S-adenosyl-L-methionine-dependent methyltransferase superfamily
553 844 SMART SM00827 Acyl transferase domain in polyketide synthase (PKS) enzymes.
553 844 InterPro IPR014043 Acyl transferase

3D structure

No structural model is available for this protein.

Structure unavailable

No pre-computed model was found in the AlphaFold database and no ColabFold prediction is available for this protein.

Sequence length: 3163 aa

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.

59 records
Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records
Transferred evidence 9 records from similar proteins
Structural ligands 9 0 loaded crystals
Measured bioactivity 0 direct and transferred ChEMBL records
Proposed compounds 50 similarity-based ZINC candidates
Best available ligand signal
57H PDB via homolog 122.1 Da · LogP 0.35 · TPSA 57.5 Open detail RCSB PDB
8H6 PDB via homolog Detail RCSB PDB
AKG PDB via homolog Detail RCSB PDB
DUV PDB via homolog Detail RCSB PDB
DUW PDB via homolog Detail RCSB PDB

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
57H RCSB PDB
5D3Z
Q03133 122.1 Da LogP 0.35 TPSA 57.5 ✓ Ro5 ✓ Clean C=CCP(=O)(O)O
8H6 RCSB PDB
5XWV
Q93NW7 390.5 Da LogP -0.14 TPSA 132.8 ✓ Ro5 ✓ Clean CCC(=O)[C@@H](C)C(=O)SCCNC(=O)CCNC(=O)[C@@H](C(…
AKG RCSB PDB
3NNF
Q6DNF2 146.1 Da LogP -0.50 TPSA 91.7 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)C(=O)O
DUV RCSB PDB
5YDL
A0A0E3JLZ0 154.2 Da LogP 0.69 TPSA 54.4 ✓ Ro5 ✓ Clean C#CCCCC(C=O)C(=O)O
DUW RCSB PDB
5YDM
A0A0E3JLZ0 178.2 Da LogP 1.13 TPSA 54.4 ✓ Ro5 ✓ Clean c1ccc(cc1)C[C@H](C=O)C(=O)O
E5U RCSB PDB
6L3M
Q8KUH4 134.1 Da LogP -0.83 TPSA 83.8 ✓ Ro5 ✓ Clean COC(C(=O)O)C(=O)O
LMR RCSB PDB
3MJS
Q93NW7 134.1 Da LogP -1.09 TPSA 94.8 ✓ Ro5 ✓ Clean C([C@@H](C(=O)O)O)C(=O)O
MLT RCSB PDB
3MJS
Q93NW7 134.1 Da LogP -1.09 TPSA 94.8 ✓ Ro5 ✓ Clean C([C@H](C(=O)O)O)C(=O)O
PNS RCSB PDB
2LIW
Q6DNF2 358.4 Da LogP -0.96 TPSA 145.2 1 viol. ✓ Clean CC(C)(COP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCS)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.