Piscinibacter sakaiensis · seed A0A0K8P6T7 · 290 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026
Open in CODSWALLOP UniProt A0A0K8P6T7 RCSB by accession PDBe-KB AlphaFold DB InterPro CATH 3.40.50.1820 SCOP 8103753 SCOP 8085716 SCOP 8094901 SCOP 8085712 SCOP 8085714 RCSB 8VEM PDBe
CATH and SCOP identifiers come from the RCSB's own structure annotations, which the Domains panel already reads, so these are looked up rather than guessed at.
Every figure here is counted over the whole family rather than quoted from one entry.
8VEM, the structure every other member of this family is superposed onto. Rendered by the RCSB and embedded here: the live app shows an interactive viewport, which a document that fetches nothing cannot.
How many of this family's constructs contain each residue of the seed. A trough is a stretch nobody has put in a construct, which is a construct-design answer rather than a disorder one.
178 distinct constructs across 212 entries. 168 polymer entities differ from the UniProt canonical sequence in some way, 76 carry a recognised expression tag and 0 carry a fusion partner.
"Differs from canonical" is not the same as "engineered". The canonical sequence is the full gene product, so a secreted protein whose structures all start after its signal peptide counts every one of them as different: lysozyme's most-used construct, residues 19–147 on 1,239 entities, is simply the mature protein. Read the construct column below for what was actually done, rather than this count.
| Entities | Length | Best (Å) | Best entry | What was made |
|---|---|---|---|---|
| 5 | 258 | 1.45 | 7CUV | no UniProt reference for this entity, so it cannot be diffed against a canonical sequence |
| 5 | 298 | 0.92 | 6EQE | His6 |
| 4 | 260 | 1.38 | 8Z2I | residues 45-304; Q45G, D46P, Q123H +7 more |
| 4 | 263 | 1.10 | 7CTS | residues 45-304; Q45G, D46P, Q123H +7 more |
| 4 | 265 | 1.12 | 5ZRQ | residues 43-304; T43G, A44P, S176A +2 more |
| 3 | 258 | 1.38 | 7E31 | no UniProt reference for this entity, so it cannot be diffed against a canonical sequence |
| 3 | 260 | 1.10 | 8GZD | residues 30-289 |
| 3 | 260 | 1.90 | 8JMP | residues 34-293; A34G, Q35M, Y127G +4 more |
| 3 | 262 | 1.20 | 5XH2 | residues 29-290; T29M, R132G, S160A |
| 3 | 273 | 1.45 | 4WFI | residues 36-304; 1-residue insertion after 45; V36M, A37R, A39S +8 more |
| 2 | 261 | 2.31 | 7XTV | no UniProt reference for this entity, so it cannot be diffed against a canonical sequence |
| 2 | 267 | 1.64 | 9RD2 | His6; residues 35-293; Q35M, Y127G, D238C +2 more |
| 2 | 267 | 1.70 | 8BRA | matches the canonical sequence |
| 2 | 272 | 2.02 | 6ANE | His6; residues 27-290; A27M |
| 2 | 282 | 1.40 | 4CG1 | His6; residues 41-301; S58R, T176S |
| 2 | 291 | 1.68 | 7VPB | matches the canonical sequence |
| 2 | 293 | 1.69 | 7VMD | matches the canonical sequence |
| 2 | 306 | 1.68 | 3WYN | His6 |
| 1 | 254 | 1.75 | 9IW9 | residues 41-292; 1 internal deletion; 2-residue insertion after 178; P41M, S43F, T45D +98 more |
| 1 | 256 | 1.61 | 9XUE | no UniProt reference for this entity, so it cannot be diffed against a canonical sequence |
| 1 | 257 | 1.51 | 9QYU | residues 36-292; L84Y, Y127G, D238C +2 more |
| 1 | 257 | 1.64 | 9QYT | residues 36-292; L84Y, Y127G, T144E +3 more |
| 1 | 258 | 1.10 | 6THS | residues 36-293; S165A |
| 1 | 258 | 1.14 | 6THT | residues 36-293; Y127G, S165A, D238C +2 more |
| 1 | 258 | 1.50 | 4EB0 | residues 36-293 |
Showing the 25 most-used of 178.
Columns where the wild-type residue still dominates but a real minority carries something else, which is a different question from "what varies across species".
| Oligomeric state | Chains | Entries | Share |
|---|---|---|---|
| monomeric | 1 | 203 | 95.8% |
| dimeric | 2 | 9 | 4.2% |
76 entries have the depositor's assembly corroborated by PISA, 134 carry the depositor's word alone and 2 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 2 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 9JQW, 9LJ7.
Every source's own domains on the seed axis, one row each. They are not merged: Pfam, CATH, SCOP and InterPro disagree about boundaries, and a merged track would state a consensus none of them gave.
| Domain | Source | Span (seed) | Chains |
|---|---|---|---|
| Alpha/Beta hydrolase fold, catalytic domain | CATH 3.40.50.1820 | 31–290 | 51 |
| alpha/beta-Hydrolases | SCOP2B 8103753 | 29–290 | 2 |
| alpha/beta-Hydrolases | SCOP2B 8085716 | 31–290 | 56 |
| alpha/beta-Hydrolases | SCOP2B 8094901 | 31–290 | 5 |
| alpha/beta-Hydrolases | SCOP2B 8085712 | 31–290 | 2 |
| alpha/beta-Hydrolases | SCOP2B 8085714 | 32–289 | 17 |
| Component | Class | Name | Entries | Best (Å) |
|---|---|---|---|---|
| GOL | cryoprotectant | Glycerol | 40 | 1.12 |
| SO4 | ion | Sulfate Ion | 36 | 1.12 |
| CL | ion | Chloride Ion | 34 | 0.92 |
| CA | ion | Calcium Ion | 31 | 1.09 |
| EDO | cryoprotectant | 1,2-Ethanediol | 24 | 1.08 |
| NA | ion | Sodium Ion | 21 | 0.92 |
| PEG | cryoprotectant | Di(Hydroxyethyl)ether | 15 | 1.20 |
| ACT | cryoprotectant | Acetate Ion | 12 | 1.08 |
| CIT | buffer | Citric Acid | 9 | 1.12 |
| MG | ion | Magnesium Ion | 8 | 1.38 |
| C9C | ligand | 4-(2-Hydroxyethyloxycarbonyl)benzoic Acid | 7 | 1.40 |
| PG4 | cryoprotectant | Tetraethylene Glycol | 6 | 1.43 |
| ZN | ion | Zinc Ion | 5 | 1.12 |
| DIO | cryoprotectant | 1,4-Diethylene Dioxide | 4 | 1.10 |
| IMD | buffer | Imidazole | 4 | 1.14 |
| J1K | ligand | 4-(2-Hydroxyethylcarbamoyl)benzoic Acid | 4 | 1.68 |
| NAG | cofactor | 2-Acetamido-2-Deoxy-Beta-D-Glucopyranose | 4 | 1.49 |
| PO4 | ion | Phosphate Ion | 3 | 1.35 |
| MPD | cryoprotectant | (4s)-2-Methyl-2,4-Pentanediol | 3 | 1.40 |
| PGE | cryoprotectant | Triethylene Glycol | 3 | 1.38 |
Parsed from the free text 208 depositors typed into
_exptl_crystal_grow.pdbx_details, out of 209
entries that recorded anything at all.
Median pH 6.5
(range 3.7 to 10.5).
212 entries carry a wwPDB validation report: 184 clean, 28 worth a check and 0 with something to explain. Median clashscore 2.5, median RSRZ outliers 1.36%, median R-free minus R-work 0.031. 211 have released structure factors.
| Organism | Entries | Best (Å) | Ligand-bound | Seed covered |
|---|---|---|---|---|
| Pseudideonella sakaiensis | 56 | 0.92 | 8 | 100% |
| Saccharomonospora viridis | 18 | 1.09 | 7 | 89% |
| Thermobifida fusca | 13 | 1.08 | 3 | 85% |
| unidentified prokaryotic organism | 13 | 1.28 | 3 | 97% |
| uncultured bacterium | 12 | 1.10 | 0 | 90% |
| compost metagenome | 10 | 0.89 | 0 | 88% |
| unidentified | 10 | 1.30 | 6 | 90% |
| Cryptosporangium aurantiacum | 8 | 1.22 | 0 | 93% |
| synthetic construct | 7 | 1.42 | 0 | 90% |
| Rhizobacter gummiphilus | 4 | 1.08 | 0 | 98% |
| Thermomonospora curvata DSM 43183 | 4 | 1.10 | 1 | 88% |
| Thermobifida cellulosilytica | 4 | 1.45 | 0 | 85% |
290 residues, numbered every ten. Every identity figure in this document is measured against this sequence.
active or binding site modified residue or glycosylation disulphide cysteine transmembrane or signal the 15 most-substituted positions
Sites are UniProt's curated features where the seed is a UniProt accession; the substituted positions are measured from this family's own alignment rather than annotated, and only the fifteen most substituted are marked: every position carrying a minority substitution would be most of the protein, because the family holds orthologues. A residue can carry more than one and is drawn with the first that applies, in the order of the key above.
One record per paper, not per entry.
| Year | Citation |
|---|---|
| 2026 | Computational engineering of the polyester hydrolase PHL7 for efficient poly(ethylene terephthalate) degradation in biocatalytic recycling processes. Nat Commun doi:10.1038/s41467-026-70868-4 |
| 2026 | Cellular Upcycling of Polyethylene Terephthalate (PET) With an Engineered Human Saliva Metagenomic PET Hydrolase. Chemsuschem doi:10.1002/cssc.202502560 |
| 2026 | Effect of surface electrostatic potential on pH-activity profile in PET depolymerases. J Hazard Mater doi:10.1016/j.jhazmat.2026.142179 |
| 2026 | Mechanistic insights into modulation of productive substrate accessibility for efficient PET depolymerization. Nat Commun doi:10.1038/s41467-026-74839-7 |
| 2026 | Development of a highly active engineered PETase enzyme for polyester degradation. Febs J. doi:10.1111/febs.70228 |
| 2025 | Trade-Offs between Stability and Activity of Glycosylated and Non-Glycosylated Polyester Hydrolases PHL7 and PHL7mut3. Acs Es T Eng doi:10.1021/acsestengg.5c00272 |
| 2025 | Landscape profiling of PET depolymerases using a natural sequence cluster framework. Science doi:10.1126/science.adp5637 |
| 2025 | Enhancing the specificity of a thermostable PET hydrolase toward aromatic polyesters via Piscinibacter sakaiensis PETase-inspired mutations. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2025.149745 |
| 2025 | Combined approaches to enhance the Pichia pastoris-expressed PET hydrolase. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2025.145862 |
| 2025 | Functional and Structural Characterization of PETase SM14 from Marine-Sponge Streptomyces sp. Active on Polyethylene Terephthalate. Acs Sustain Chem Eng doi:10.1021/acssuschemeng.5c00737 |
| 2025 | Application of a Rational Crystal Contact Engineering Strategy on a Poly(ethylene terephthalate)-Degrading Cutinase. Bioengineering (Basel) doi:10.3390/bioengineering12060561 |
| 2025 | Ancestral reconstruction of polyethylene terephthalate degrading cutinases reveals a rugged and unexplored sequence-fitness landscape. Sci Adv doi:10.1126/sciadv.ads8318 |
| 2025 | Harnessing protein language model for structure-based discovery of highly efficient and robust PET hydrolases. Nat Commun doi:10.1038/s41467-025-61599-z |
| 2025 | Machine Learning-Guided Identification of PET Hydrolases from Natural Diversity. Acs Catalysis doi:10.1021/acscatal.5c03460 |
| 2025 | Computational loop reconstruction based design of efficient PET hydrolases. Commun Biol doi:10.1038/s42003-025-08364-6 |
| 2024 | Enhancing PET Degrading Enzymes: A Combinatory Approach. Chembiochem doi:10.1002/cbic.202400084 |
| 2024 | Structural dynamics of the Ca 2+ -regulated cutinase towards structure-based improvement of PET degradation activity. Int.J.Biol.Macromol. doi:10.1016/j.ijbiomac.2024.136597 |
| 2024 | Streamlined screening of extracellularly expressed PETase libraries for improved polyethylene terephthalate degradation. Biotechnol J doi:10.1002/biot.202400021 |
| 2024 | Understanding the Catalytic Efficiency of Two Polyester Degrading Enzymes: An Experimental and Theoretical Investigation. Acs Omega doi:10.1021/acsomega.4c06528 |
| 2024 | The metagenome-derived esterase PET40 is highly promiscuous and hydrolyses polyethylene terephthalate (PET). Febs J. doi:10.1111/febs.16924 |
| 2024 | Exploring the pH dependence of an improved PETase. Biophys.J. doi:10.1016/j.bpj.2024.04.026 |
| 2024 | The unique salt bridge network in GlacPETase: a key to its stability. Appl.Environ.Microbiol. doi:10.1128/aem.02242-23 |
| 2024 | beta-sheet Engineering of IsPETase for PET Depolymerization Engineering (Beijing) doi:10.1016/j.eng.2024.10.015 |
| 2023 | Concentration-Dependent Inhibition of Mesophilic PETases on Poly(ethylene terephthalate) Can Be Eliminated by Enzyme Engineering. ChemSusChem doi:10.1002/cssc.202202277 |
| 2023 | Ancestral Sequence Reconstruction Identifies Structural Changes Underlying the Evolution of Ideonella sakaiensis PETase and Variants with Improved Stability and Activity. Biochemistry doi:10.1021/acs.biochem.2c00323 |
| 2023 | Discovery and rational engineering of PET hydrolase with both mesophilic and thermophilic PET hydrolase properties. Nat Commun doi:10.1038/s41467-023-40233-w |
| 2023 | Complete decomposition of poly(ethylene terephthalate) by crude PET hydrolytic enzyme produced in Pichia pastoris Chem Eng J doi:10.1016/j.cej.2023.148418 |
| 2023 | Engineering the catalytic activity of an Antarctic PET-degrading enzyme by loop exchange. Protein Sci. doi:10.1002/pro.4757 |
| 2023 | Structure and function of the metagenomic plastic-degrading polyester hydrolase PHL7 bound to its product. Nat Commun doi:10.1038/s41467-023-37415-x |
| 2023 | Complete bio-degradation of poly(butylene adipate-co-terephthalate) via engineered cutinases. Nat Commun doi:10.1038/s41467-023-37374-3 |
| 2023 | Remodeling the polymer-binding cavity to improve the efficacy of PBAT-degrading enzyme. J Hazard Mater doi:10.1016/j.jhazmat.2023.132965 |
| 2023 | Functional tailoring of a PET hydrolytic enzyme expressed in Pichia pastoris. Bioresour Bioprocess doi:10.1186/s40643-023-00648-1 |
| 2023 | Improvement of thermostability and activity of PET-degrading enzyme Cut190 towards a detailed understanding and application of the enzymatic reaction mechanism. Biorxiv doi:10.1101/2023.02.26.529345 |
| 2022 | Low Carbon Footprint Recycling of Post-Consumer PET Plastic with a Metagenomic Polyester Hydrolase. ChemSusChem doi:10.1002/cssc.202101062 |
| 2022 | Multiple Substrate Binding Mode-Guided Engineering of a Thermophilic PET Hydrolase. Acs Catalysis doi:10.1021/acscatal.2c02275 |
| 2022 | Investigation of the halophilic PET hydrolase PET6 from Vibrio gazogenes. Protein Sci. doi:10.1002/pro.4500 |
| 2022 | Sourcing thermotolerant poly(ethylene terephthalate) hydrolase scaffolds from natural diversity Nat Commun doi:10.1038/s41467-022-35237-x |
| 2022 | Machine learning-aided engineering of hydrolases for PET depolymerization. Nature doi:10.1038/s41586-022-04599-z |
| 2022 | Comparative Performance of PETase as a Function of Reaction Conditions, Substrate Properties, and Product Accumulation. ChemSusChem doi:10.1002/cssc.202101932 |
| 2022 | Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin. Nat Commun doi:10.1038/s41467-022-34908-z |