KpATCC43816 Protein target profile

L-xylulose 5-phosphate 3-epimerase

Accession: VK055_2873

Gene: AIK81462.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GHC9

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Length 284

Pocket druggability (P2Rank · AlphaFold DB model) 0.796

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 54 total records

Functional annotation 0 EC 4 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Metabolic chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Central metabolic position More central than 90.8% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

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: No hit
Gut microbiome similarity: 2.5% 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.

Structure confidence

ColabFold pLDDT: 96.46 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.796

Structure A0A0H3GHC9

Pocket Pocket 1

Druggability (FPocket) 0.515

Structure A0A0H3GHC9

Pocket Pocket 2

ColabFold model

P2Rank 0.747 · Pocket 1

FPocket 0.493 · Pocket 3

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 117 / 4744 genomes with a hit

Prevalence 2.5%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Attractive metabolic target: catalyzes a consuming chokepoint reaction in Ascorbate and aldarate metabolism, no isoenzyme backup detected, more central than 90.8% of genes in this genome, no human homolog detected.

Relative network centrality 90.8% more central than 90.8% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MLAKSIPLGIYEKALPAGECWLERLKLAKALGFDFVEMSLDETDARLARLDWSPEQRLALVKAVAETGVRVPSMCLSAHRRFPLGSEDDAVRHQGLEIMRKAIQLAQDVGIRVIQLAGYDVYYQQANDETRRRFRDGLKQSVEMASRAQVTLAMEIMDYPLMNSISKALGYAHYLNNPWFQLYPDIGNLSAWDNDVQMELKAGSGHIVAVHVKDTKPGVFKNVPFGEGVVDFERCFETLKQTGYCGPYLIEMWSETSADPLAEVAKARDWVKARMARAGLMEAA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
GO:0016861 Catalysis of an oxidation-reduction (redox) reaction in which the hydrogen donor and acceptor, which is an aldose or a ketose, are the same molecule, and no oxidized product appears.
GO:0034015 Catalysis of the reaction: L-ribulose 5-phosphate = L-xylulose 5-phosphate.
GO:0019852 The chemical reactions and pathways involving L-ascorbic acid, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate; L-ascorbic acid is vitamin C and has co-factor and anti-oxidant activities in many species.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

9 records

Show feature table

Start	End	DB	Term	Name
9	274	PANTHER	PTHR43489	ISOMERASE
1	284	Gene3D	G3DSA:3.20.20.150	-
1	284	FunFam	G3DSA:3.20.20.150:FF:000003	L-ribulose-5-phosphate 3-epimerase UlaE
25	272	Pfam	PF01261	Xylose isomerase-like TIM barrel
25	272	InterPro	IPR013022	Xylose isomerase-like, TIM barrel domain
5	281	NCBIfam	TIGR00542	putative hexulose-6-phosphate isomerase
5	281	InterPro	IPR004560	L-ribulose-5-phosphate 3-epimerase
21	278	SUPERFAMILY	SSF51658	Xylose isomerase-like
21	278	InterPro	IPR036237	Xylose isomerase-like superfamily

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.796

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Surrounding area

Pocket 2 P2Rank #2

0.089

Likely same site as FPocket 2 0.8 Å 14 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.012

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Surrounding area

Pocket 4 P2Rank #4

0.002

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Surrounding area

Pocket 5 P2Rank #5

0.001

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #2

0.515

Likely same site as P2Rank 2 0.8 Å 14 shared residues 100% of smaller site

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Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.747

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Surrounding area

Pocket 2 P2Rank #2

0.073

Likely same site as FPocket 3 1.2 Å 11 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.041

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Surrounding area

Pocket 4 P2Rank #4

0.006

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3GHC9	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_2873	ColabFold	—	—	full sequence	—	Loaded

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.

54 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 5 records from similar proteins

Structural ligands 5 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 49 similarity-based ZINC candidates

Best available ligand signal

FUD PDB via homolog 180.2 Da · LogP -3.38 · TPSA 118.2 Open detail RCSB PDB

FZU PDB via homolog Detail RCSB PDB

LTG PDB via homolog Detail RCSB PDB

PSJ PDB via homolog Detail RCSB PDB

SOL PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
FUD RCSB PDB	7CJ9	A0A172U6X0	180.2 Da LogP -3.38 TPSA 118.2	✓ Ro5	✓ Clean	`C([C@H]([C@H]([C@@H](C(=O)CO)O)O)O)O`
FZU RCSB PDB	7CJ7	A0A172U6X0	180.2 Da LogP -3.22 TPSA 110.4	✓ Ro5	✓ Clean	`C1[C@@H]([C@H]([C@H]([C@](O1)(CO)O)O)O)O`
LTG RCSB PDB	7CJ7	A0A172U6X0	180.2 Da LogP -3.38 TPSA 118.2	✓ Ro5	✓ Clean	`C([C@@H]([C@H]([C@H](C(=O)CO)O)O)O)O`
PSJ RCSB PDB	7CJ6	A0A172U6X0	180.2 Da LogP -3.38 TPSA 118.2	✓ Ro5	✓ Clean	`C([C@H]([C@H]([C@H](C(=O)CO)O)O)O)O`
SOL RCSB PDB	7CJ7	A0A172U6X0	180.2 Da LogP -3.38 TPSA 118.2	✓ Ro5	✓ Clean	`C([C@@H]([C@H]([C@@H](C(=O)CO)O)O)O)O`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC100036265 ZINC	0.857	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC100071552 ZINC	0.857	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)CO`
ZINC113074329 ZINC	0.857	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC13522679 ZINC	0.857	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)CO`
ZINC4353160 ZINC	0.857	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)CO`
ZINC8579422 ZINC	0.857	210.2 Da LogP -4.02 TPSA 138.5	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC15218560 ZINC	0.571	237.2 Da LogP -3.54 TPSA 139.5	1 viol.	✓ Clean	`O=C(O)CNC[C@]1(O)OC[C@H](O)[C@@H](O)[C@@H]1O`
ZINC257390960 ZINC	0.571	237.2 Da LogP -3.54 TPSA 139.5	1 viol.	✓ Clean	`O=C(O)CNC[C@]1(O)OC[C@H](O)[C@@H](O)[C@H]1O`
ZINC257390961 ZINC	0.571	237.2 Da LogP -3.54 TPSA 139.5	1 viol.	✓ Clean	`O=C(O)CNC[C@]1(O)OC[C@H](O)[C@H](O)[C@H]1O`
ZINC85765425 ZINC	0.571	237.2 Da LogP -3.54 TPSA 139.5	1 viol.	✓ Clean	`O=C(O)CNC[C@]1(O)OC[C@H](O)[C@H](O)[C@@H]1O`
ZINC150049482 ZINC	0.543	221.3 Da LogP -2.21 TPSA 102.2	✓ Ro5	✓ Clean	`CCCNC[C@@]1(O)OC[C@@H](O)[C@@H](O)[C@@H]1O`
ZINC31771706 ZINC	0.543	249.3 Da LogP -2.88 TPSA 102.6	✓ Ro5	✓ Clean	`O[C@H]1[C@H](O)[C@H](O)CO[C@@]1(O)CN1CCOCC1`
ZINC31771707 ZINC	0.543	249.3 Da LogP -2.88 TPSA 102.6	✓ Ro5	✓ Clean	`O[C@H]1[C@H](O)[C@H](O)CO[C@]1(O)CN1CCOCC1`
ZINC4096594 ZINC	0.543	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@]1(O)OC[C@@H](O)[C@@H](O)[C@@H]1O`
ZINC4578915 ZINC	0.543	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@]1(O)OC[C@H](O)[C@H](O)[C@@H]1O`
ZINC4578916 ZINC	0.543	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@]1(O)OC[C@@H](O)[C@H](O)[C@@H]1O`
ZINC4578917 ZINC	0.543	260.1 Da LogP -3.10 TPSA 156.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@]1(O)OC[C@H](O)[C@@H](O)[C@@H]1O`
ZINC5496244 ZINC	0.543	249.3 Da LogP -2.88 TPSA 102.6	✓ Ro5	✓ Clean	`O[C@@H]1CO[C@](O)(CN2CCOCC2)[C@H](O)[C@@H]1O`
ZINC5496246 ZINC	0.543	249.3 Da LogP -2.88 TPSA 102.6	✓ Ro5	✓ Clean	`O[C@@H]1CO[C@@](O)(CN2CCOCC2)[C@H](O)[C@@H]1O`
ZINC4726346 ZINC	0.538	225.2 Da LogP -4.73 TPSA 164.5	1 viol.	✓ Clean	`NC(=O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H…`
ZINC4726347 ZINC	0.538	225.2 Da LogP -4.73 TPSA 164.5	1 viol.	✓ Clean	`NC(=O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H]…`
ZINC4726348 ZINC	0.538	225.2 Da LogP -4.73 TPSA 164.5	1 viol.	✓ Clean	`NC(=O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H]…`
ZINC4726349 ZINC	0.538	225.2 Da LogP -4.73 TPSA 164.5	1 viol.	✓ Clean	`NC(=O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](…`
ZINC100065511 ZINC	0.533	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC100085043 ZINC	0.533	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC104869937 ZINC	0.533	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC13537943 ZINC	0.533	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC18140538 ZINC	0.533	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC85994845 ZINC	0.533	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC199775419 ZINC	0.516	251.2 Da LogP -3.48 TPSA 150.3	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)OCC(=O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC11592819 ZINC	0.500	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)CO`
ZINC11592820 ZINC	0.500	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@H](O)[C@H](O)[C@@H](O)…`
ZINC11592821 ZINC	0.500	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@@H](O…`
ZINC1531006 ZINC	0.500	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)[C@H](O…`
ZINC1531007 ZINC	0.500	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)…`
ZINC1570003633 ZINC	0.500	324.3 Da LogP -4.03 TPSA 186.6	1 viol.	✓ Clean	`C/C(=N\N=C(/C)[C@@H](O)[C@@H](O)[C@H](O)CO)[C@H…`
ZINC33991088 ZINC	0.500	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H]…`
ZINC34049524 ZINC	0.500	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@@H](O)[C@H](O)[C@@H](O…`
ZINC34370883 ZINC	0.500	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@@H](O)[C@H](O)[C@@H](O)[C@@H](…`
ZINC4403706 ZINC	0.500	256.2 Da LogP -4.77 TPSA 178.9	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H…`
ZINC4403707 ZINC	0.500	256.2 Da LogP -4.77 TPSA 178.9	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H…`
ZINC4403708 ZINC	0.500	256.2 Da LogP -4.77 TPSA 178.9	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H]…`
ZINC4403709 ZINC	0.500	256.2 Da LogP -4.77 TPSA 178.9	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H]…`
ZINC4521295 ZINC	0.500	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H…`
ZINC4521296 ZINC	0.500	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H]…`
ZINC4521297 ZINC	0.500	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H]…`
ZINC4521298 ZINC	0.500	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)[C@H](…`
ZINC5830322 ZINC	0.500	226.2 Da LogP -4.13 TPSA 158.7	1 viol.	✓ Clean	`O=C(O)[C@H](O)[C@H](O)[C@H](O)[C@@H](O)[C@H](O)…`
ZINC95864989 ZINC	0.500	342.3 Da LogP -5.40 TPSA 189.5	2 viol.	✓ Clean	`OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@](O)(CO)OC[C@…`

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.

Cross-references

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

Sequence

UniProt A0A0H3GHC9

Pathways

KEGG R03244 BioCyc LXULRU5P-RXN