Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0004497 monooxygenase activity	IEA GO_REF:0000002	REMOVE	Summary: InterPro-based (IEA) monooxygenase activity from the cytochrome P450 signature. EryCII is a P450 homologue that lacks the heme-binding sites and is catalytically dead; it has no monooxygenase activity. Its real role is as an allosteric activator of the EryCIII glycosyltransferase. Reason: Demonstrably incorrect. Beyond the UniProt CAUTION ("lacks the heme-binding sites"), the structure paper shows by structure-based alignment that EryCII lacks the conserved heme-ligating cysteine and is "not an active P450 enzyme", and the 2YJN structure is apo (no heme). EryCII functions as a GT activator, not a monooxygenase. Classic domain-propagation over-annotation of a pseudoenzyme. Supporting Evidence: file:SACEN/eryCII/eryCII-uniprot.txt Although related to the cytochrome P450 family, lacks the heme-binding sites. PMID:22056329 the conserved cysteine is absent (Supplementary Fig. S5); thus, they are not active P450 enzymes
GO:0005506 iron ion binding	IEA GO_REF:0000002	REMOVE	Summary: IEA iron ion binding inherited from the P450 signature (P450s bind a heme iron). EryCII lacks the heme-binding sites and does not bind a catalytic iron. Reason: Incorrect; depends on heme/iron cofactor binding that EryCII has lost. The UniProt CAUTION (lacks the heme-binding sites) and the structure (no heme; absent conserved Cys) agree. Supporting Evidence: file:SACEN/eryCII/eryCII-uniprot.txt Although related to the cytochrome P450 family, lacks the heme-binding sites. PMID:22056329 Having lost the heme group in the central core, the protein may be more conformationally dynamic
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen	IEA GO_REF:0000002	REMOVE	Summary: IEA oxidoreductase activity from the P450 signature. EryCII performs no oxygen-dependent oxidoreductase chemistry; it is a non-catalytic P450 homologue. Reason: Incorrect catalytic MF for a heme-less, non-catalytic P450 homologue (UniProt CAUTION plus the apo structure / absent conserved Cys). Supporting Evidence: file:SACEN/eryCII/eryCII-uniprot.txt Although related to the cytochrome P450 family, lacks the heme-binding sites. PMID:22056329 the conserved cysteine is absent (Supplementary Fig. S5); thus, they are not active P450 enzymes
GO:0020037 heme binding	IEA GO_REF:0000002	REMOVE	Summary: IEA heme binding from the P450 signature. EryCII explicitly lacks the heme-binding sites, so it does not bind heme. Reason: Both the UniProt CAUTION ("lacks the heme-binding sites") and primary structural data agree: the conserved heme-ligating cysteine is absent and EryCII has "lost the heme group in the central core" (PMID:22056329); the 2YJN structure contains no heme ligand. The most clearly incorrect of the inherited P450 terms. Supporting Evidence: file:SACEN/eryCII/eryCII-uniprot.txt Although related to the cytochrome P450 family, lacks the heme-binding sites. PMID:22056329 Having lost the heme group in the central core, the protein may be more conformationally dynamic
GO:0008047 enzyme activator activity	IDA PMID:22056329 Structure of the glycosyltransferase EryCIII in complex with...	NEW	Summary: Proposed NEW annotation capturing EryCII's actual molecular function: it allosterically activates the glycosyltransferase EryCIII (EryCIII is inactive on its own; activity is restored by EryCII). Not present in GOA, which carries only the inherited (incorrect) P450 catalytic terms. Reason: Replaces the removed P450 catalytic terms with EryCII's true, experimentally supported activator role. Supporting Evidence: PMID:22056329 EryCII stabilizes EryCIII and also functions as an allosteric activator of the GT

Core Functions

EryCII is required to activate the desosaminyl transferase EryCIII: EryCIII is inactive on its own, and EryCII allosterically activates and stabilizes it within the alpha2-beta2 EryCII-EryCIII heterotetramer (via its N-terminal A'' helix contacting EryCIII's acceptor domain), enabling glycosyl transfer to the macrolide and hence the desosaminylation step of erythromycin biosynthesis (PMID:22056329, PMID:15303858; PDB 2YJN). This activator/stabilizer role is the accurate molecular function in place of the inherited (incorrect) P450 catalytic terms. The fold stabilization is conformational-chaperone-like, but EryCII is a stably bound stoichiometric subunit, not a transient folding chaperone.

Molecular Function:

enzyme activator activity

Directly Involved In:

protein stabilization erythromycin biosynthetic process

In Complex:

protein-containing complex

Supporting Evidence:

PMID:22056329
EryCII stabilizes EryCIII and also functions as an allosteric activator of the GT
PMID:22056329
one function of the auxiliary proteins is to stabilize the fold and quaternary structure of its partner GT

References

PMID:22056329

Structure of the glycosyltransferase EryCIII in complex with its activating P450 homologue EryCII.

EryCII forms a heterotetramer with EryCIII, stabilizes it, and acts as an allosteric activator of the glycosyltransferase.

"Our biophysical and enzymatic data support a model in which EryCII stabilizes EryCIII and also functions as an allosteric activator of the GT."
The EryCIII-EryCII complex is a heterotetramer.

"The structure reveals a heterotetramer with a distinctive, elongated quaternary organization."
EryCII lacks the conserved heme-ligating cysteine of P450s and has no heme; it is not an active P450 enzyme (structure-based alignment, apo structure).

"As expected for EryCII—and indeed the macrolide auxiliary proteins generally—the conserved cysteine is absent (Supplementary Fig. S5); thus, they are not active P450 enzymes."
EryCII has lost the heme group from the central core of the P450-like fold.

"Having lost the heme group in the central core, the protein may be more conformationally dynamic"
EryCIII is inactive on its own; EryCII is required to restore its glycosyltransferase activity.

"When separate EryCIII- and EryCII-containing extracts were combined, the GT activity of EryCIII was restored, confirming as expected that EryCII is required by EryCIII."
The complex is an alpha2-beta2 heterotetramer (dimer of EryCIII-EryCII heterodimers); EryCII activates allosterically via its N-terminal A'' helix, which contacts EryCIII's acceptor domain without touching the active site directly.

"Binding of EryCII to the N-terminal acceptor domain of EryCIII (Fig. 6) may likewise trigger a closer association with the C-terminal sugar-nucleotide binding domain and the correct juxtaposition of the acceptor and donor sites of EryCIII."

PMID:15303858

Reconstitution and characterization of a new desosaminyl transferase, EryCIII, from the erythromycin biosynthetic pathway.

EryCIII transfers TDP-D-desosamine to alpha-mycarosyl erythronolide B to form erythromycin D; EryCII is its biosynthetic partner.

"EryCIII converts alpha-mycarosyl erythronolide B into erythromycin D using TDP-d-desosamine as the glycosyl donor."

file:SACEN/eryCII/eryCII-notes.md

eryCII review notes (BGC project); pseudoenzyme over-annotation analysis

file:SACEN/eryCII/eryCII-uniprot.txt

UniProtKB A4F7P2 (ERYC2_SACEN) record

UniProt flags that EryCII, though related to the cytochrome P450 family, lacks the heme-binding sites.

"Although related to the cytochrome P450 family, lacks the heme-binding sites."

GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

Suggested Experiments

Experiment: Confirm absence of heme binding and monooxygenase activity for purified EryCII, and quantify EryCIII GT stimulation as a function of EryCII, to formally retire the P450 catalytic annotations.

📚 Additional Documentation

Notes

(eryCII-notes.md)

eryCII (A4F7P2, SACE_0725) — review notes

Part of the BGC exemplar curation project (projects/BGC.md). MIBiG BGC0000055
(Saccharopolyspora erythraea, erythromycin PKS). GenBank CAM00066.1 → UniProt
A4F7P2 (ERYC2_SACEN), gene eryCII / SACE_0725. Also relevant to
projects/PSEUDOENZYMES.md.

Function — a P450 PSEUDOENZYME that activates a glycosyltransferase

EryCII is a cytochrome-P450-family homologue that has lost catalytic competence
and instead serves as the activating partner of the desosaminyl transferase
EryCIII in erythromycin biosynthesis.

UniProt A4F7P2 CAUTION: "Although related to the cytochrome P450 family, lacks the
heme-binding sites." (ECO:0000305) — note this is a curator inference, so it needs
corroboration (below).
Beyond the assertion — primary structural evidence (PMID:22056329 full text):
"...lacks the essential cysteine residue that coordinates the heme iron."
"the conserved cysteine is absent (Supplementary Fig. S5); thus, they are not
active P450 enzymes." (structure-based alignment vs P450 Cyp125)
"Having lost the heme group in the central core, the protein may be more
conformationally dynamic..."
PDB 2YJN is apo: the RCSB entry has zero non-polymer entities (no heme ligand).
Activation mechanism: EryCIII activity "is almost completely rescued by the
addition of soluble EryCII... able to induce a catalytically active structure in
EryCIII."

So the no-heme / no-catalysis conclusion rests on (1) the absent conserved Cys in a
structure-based alignment, and (2) an apo crystal structure — not merely UniProt.
- UniProt FUNCTION: "Involved in the erythromycin biosynthesis pathway. Acts by
forming a complex and stabilizing the desosaminyl transferase EryCIII."
(ECO:0000269|PubMed:22056329); SUBUNIT: "Heterotetramer composed of EryCII and EryCIII."
- Structure (PDB 2YJN): "EryCIII, in concert with its partner EryCII, attaches a
nucleotide-activated sugar to the macrolide scaffold... a heterotetramer...
EryCII stabilizes EryCIII and also functions as an allosteric activator of the GT."
PMID:22056329
- EryCII is required for EryCIII catalysis (not merely an enhancer): purified
EryCIII "was inactive under all conditions tried"; combining EryCIII + EryCII
extracts "restored" GT activity [PMID:22056329 full text]. Stoichiometry is
α2β2 (dimer of heterodimers, ~188 kDa); activation is allosteric via EryCII's
N-terminal A″ helix, which contacts EryCIII's acceptor domain.

Annotation issues — domain-based over-annotation of a pseudoenzyme

All four GOA molecular-function terms are IEA from the P450 sequence signature and are
incorrect for this catalytically dead homologue:

GO:0004497 monooxygenase activity → REMOVE
GO:0005506 iron ion binding → REMOVE
GO:0016705 oxidoreductase activity (paired donors, O2) → REMOVE
GO:0020037 heme binding → REMOVE (UniProt: "lacks the heme-binding sites")

Accurate roles to assert instead: GO:0008047 enzyme activator activity (allosteric
activator of EryCIII; added as a NEW annotation), GO:0050821 protein stabilization
(stabilizes EryCIII's fold/quaternary structure), GO:1901115 erythromycin
biosynthetic process (BP), GO:0032991 protein-containing complex (EryCII-EryCIII
heterotetramer).

"Conformational chaperone"?

Mechanistically EryCII templates/stabilizes the catalytically competent conformation of
EryCIII, which is chaperone-like. But it is not annotated as a protein folding chaperone (GO:0044183): a chaperone acts transiently and is released, and its client
stays active afterwards; EryCII is a stably bound stoichiometric subunit and EryCIII
is inactive without it (PMID:22056329). So the stabilizing aspect is captured by
protein stabilization (GO:0050821) and the activating aspect by enzyme activator activity (GO:0008047) - not a chaperone MF. (The older fold-and-release / "does not
bind tightly" model, ref 13, was superseded by the stable-complex structure.)

Capturing absence of function (NOT annotations)

A "NEW NOT" (negated: true + action: NEW) can only be used for a term NOT already in
GOA. Here the erroneous P450 functions (monooxygenase, heme binding, iron binding,
oxidoreductase) are already present in GOA, so they are handled by REMOVE; there is no
review action to convert an existing positive annotation into a NOT.

Predicted-complex evidence (BGC project)

Moriwaki et al. (bioRxiv 2025.10.26.684697) predict the EryCII-EryCIII interaction
(BGC0000055; CAM00066.1/CAM00067.1) at ipTM 0.92, matching PDB 2YJN (hetero 4-mer).

References

PMID:22056329 — Moncrieffe et al. 2012, J Mol Biol (EryCIII·EryCII structure, PDB
2YJN; EryCII stabilizes and allosterically activates EryCIII). VERIFIED.
UniProt A4F7P2 (CAUTION: lacks heme-binding sites).

📄 View Raw YAML

id: A4F7P2
gene_symbol: eryCII
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:405948
  label: Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC
    13426 / NCIMB 8594 / NRRL 2338)
description: >-
  EryCII (SACE_0725) is a cytochrome-P450-family homologue that has lost catalytic
  competence and instead acts as the activating partner of the desosaminyl
  transferase EryCIII in erythromycin biosynthesis in Saccharopolyspora erythraea.
  Although related to cytochrome P450s by sequence, EryCII lacks the heme-binding
  sites and therefore cannot perform P450 monooxygenase chemistry; it is a
  pseudoenzyme. Functionally, EryCII forms an elongated EryCII-EryCIII heterotetramer
  in which it stabilizes EryCIII and acts as an allosteric activator of the
  glycosyltransferase, enabling efficient transfer of TDP-D-desosamine to the
  macrolide scaffold (PMID:22056329, PMID:15303858). Mechanistically EryCII behaves
  like a conformational chaperone that templates the catalytically competent state of
  EryCIII, but - unlike a classical chaperone - it remains stably bound as a
  stoichiometric subunit and EryCIII is inactive without it, so it is best described as
  an activator/stabilizer subunit rather than a transient folding chaperone. EryCII is
  thus a clear example of domain-based over-annotation: its sequence-derived
  P450/heme/monooxygenase annotations do not reflect its true non-catalytic,
  GT-activating role.
references:
- id: PMID:22056329
  title: Structure of the glycosyltransferase EryCIII in complex with its activating
    P450 homologue EryCII.
  findings:
  - statement: >-
      EryCII forms a heterotetramer with EryCIII, stabilizes it, and acts as an
      allosteric activator of the glycosyltransferase.
    supporting_text: >-
      Our biophysical and enzymatic data support a model in which EryCII stabilizes
      EryCIII and also functions as an allosteric activator of the GT.
  - statement: >-
      The EryCIII-EryCII complex is a heterotetramer.
    supporting_text: >-
      The structure reveals a heterotetramer with a distinctive, elongated quaternary
      organization.
  - statement: >-
      EryCII lacks the conserved heme-ligating cysteine of P450s and has no heme; it is
      not an active P450 enzyme (structure-based alignment, apo structure).
    supporting_text: >-
      As expected for EryCII—and indeed the macrolide auxiliary proteins generally—the
      conserved cysteine is absent (Supplementary Fig. S5); thus, they are not active
      P450 enzymes.
  - statement: >-
      EryCII has lost the heme group from the central core of the P450-like fold.
    supporting_text: >-
      Having lost the heme group in the central core, the protein may be more
      conformationally dynamic
  - statement: >-
      EryCIII is inactive on its own; EryCII is required to restore its
      glycosyltransferase activity.
    supporting_text: >-
      When separate EryCIII- and EryCII-containing extracts were combined, the GT
      activity of EryCIII was restored, confirming as expected that EryCII is required
      by EryCIII.
  - statement: >-
      The complex is an alpha2-beta2 heterotetramer (dimer of EryCIII-EryCII
      heterodimers); EryCII activates allosterically via its N-terminal A'' helix, which
      contacts EryCIII's acceptor domain without touching the active site directly.
    supporting_text: >-
      Binding of EryCII to the N-terminal acceptor domain of EryCIII (Fig. 6) may
      likewise trigger a closer association with the C-terminal sugar-nucleotide binding
      domain and the correct juxtaposition of the acceptor and donor sites of EryCIII.
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      PubMed-verified; PDB 2YJN. Beyond the UniProt CAUTION (ECO:0000305), the full text
      provides primary evidence that EryCII lacks the conserved heme-ligating cysteine
      and the heme group ("not active P450 enzymes"); the 2YJN coordinates contain no
      heme ligand (apo structure).
- id: PMID:15303858
  title: 'Reconstitution and characterization of a new desosaminyl transferase, EryCIII,
    from the erythromycin biosynthetic pathway.'
  findings:
  - statement: >-
      EryCIII transfers TDP-D-desosamine to alpha-mycarosyl erythronolide B to form
      erythromycin D; EryCII is its biosynthetic partner.
    supporting_text: >-
      EryCIII converts alpha-mycarosyl erythronolide B into erythromycin D using
      TDP-d-desosamine as the glycosyl donor.
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: >-
      Characterizes the partner GT EryCIII; supports the erythromycin-biosynthesis role
      of the EryCII/EryCIII system.
- id: file:SACEN/eryCII/eryCII-notes.md
  title: eryCII review notes (BGC project); pseudoenzyme over-annotation analysis
- id: file:SACEN/eryCII/eryCII-uniprot.txt
  title: UniProtKB A4F7P2 (ERYC2_SACEN) record
  findings:
  - statement: >-
      UniProt flags that EryCII, though related to the cytochrome P450 family, lacks
      the heme-binding sites.
    supporting_text: >-
      Although related to the cytochrome P450 family, lacks the heme-binding sites.
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      The CAUTION is an ECO:0000305 curator inference; it carries real weight as an
      expert assessment and is independently corroborated by the structure (absent
      conserved Cys; apo 2YJN). Both lines of evidence are cited together.
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO terms
existing_annotations:
- term:
    id: GO:0004497
    label: monooxygenase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: >-
      InterPro-based (IEA) monooxygenase activity from the cytochrome P450 signature.
      EryCII is a P450 homologue that lacks the heme-binding sites and is catalytically
      dead; it has no monooxygenase activity. Its real role is as an allosteric
      activator of the EryCIII glycosyltransferase.
    action: REMOVE
    reason: >-
      Demonstrably incorrect. Beyond the UniProt CAUTION ("lacks the heme-binding
      sites"), the structure paper shows by structure-based alignment that EryCII lacks
      the conserved heme-ligating cysteine and is "not an active P450 enzyme", and the
      2YJN structure is apo (no heme). EryCII functions as a GT activator, not a
      monooxygenase. Classic domain-propagation over-annotation of a pseudoenzyme.
    supported_by:
    - reference_id: file:SACEN/eryCII/eryCII-uniprot.txt
      supporting_text: >-
        Although related to the cytochrome P450 family, lacks the heme-binding sites.
    - reference_id: PMID:22056329
      supporting_text: >-
        the conserved cysteine is absent (Supplementary Fig. S5); thus, they are not
        active P450 enzymes
- term:
    id: GO:0005506
    label: iron ion binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: >-
      IEA iron ion binding inherited from the P450 signature (P450s bind a heme iron).
      EryCII lacks the heme-binding sites and does not bind a catalytic iron.
    action: REMOVE
    reason: >-
      Incorrect; depends on heme/iron cofactor binding that EryCII has lost. The UniProt
      CAUTION (lacks the heme-binding sites) and the structure (no heme; absent conserved
      Cys) agree.
    supported_by:
    - reference_id: file:SACEN/eryCII/eryCII-uniprot.txt
      supporting_text: >-
        Although related to the cytochrome P450 family, lacks the heme-binding sites.
    - reference_id: PMID:22056329
      supporting_text: >-
        Having lost the heme group in the central core, the protein may be more
        conformationally dynamic
- term:
    id: GO:0016705
    label: oxidoreductase activity, acting on paired donors, with incorporation or reduction
      of molecular oxygen
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: >-
      IEA oxidoreductase activity from the P450 signature. EryCII performs no
      oxygen-dependent oxidoreductase chemistry; it is a non-catalytic P450 homologue.
    action: REMOVE
    reason: >-
      Incorrect catalytic MF for a heme-less, non-catalytic P450 homologue (UniProt
      CAUTION plus the apo structure / absent conserved Cys).
    supported_by:
    - reference_id: file:SACEN/eryCII/eryCII-uniprot.txt
      supporting_text: >-
        Although related to the cytochrome P450 family, lacks the heme-binding sites.
    - reference_id: PMID:22056329
      supporting_text: >-
        the conserved cysteine is absent (Supplementary Fig. S5); thus, they are not
        active P450 enzymes
- term:
    id: GO:0020037
    label: heme binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: >-
      IEA heme binding from the P450 signature. EryCII explicitly lacks the
      heme-binding sites, so it does not bind heme.
    action: REMOVE
    reason: >-
      Both the UniProt CAUTION ("lacks the heme-binding sites") and primary structural
      data agree: the conserved heme-ligating cysteine is absent and EryCII has "lost
      the heme group in the central core" (PMID:22056329); the 2YJN structure contains
      no heme ligand. The most clearly incorrect of the inherited P450 terms.
    supported_by:
    - reference_id: file:SACEN/eryCII/eryCII-uniprot.txt
      supporting_text: >-
        Although related to the cytochrome P450 family, lacks the heme-binding sites.
    - reference_id: PMID:22056329
      supporting_text: >-
        Having lost the heme group in the central core, the protein may be more
        conformationally dynamic
- term:
    id: GO:0008047
    label: enzyme activator activity
  evidence_type: IDA
  original_reference_id: PMID:22056329
  qualifier: enables
  review:
    summary: >-
      Proposed NEW annotation capturing EryCII's actual molecular function: it
      allosterically activates the glycosyltransferase EryCIII (EryCIII is inactive on
      its own; activity is restored by EryCII). Not present in GOA, which carries only
      the inherited (incorrect) P450 catalytic terms.
    action: NEW
    reason: >-
      Replaces the removed P450 catalytic terms with EryCII's true, experimentally
      supported activator role.
    supported_by:
    - reference_id: PMID:22056329
      supporting_text: >-
        EryCII stabilizes EryCIII and also functions as an allosteric activator of the GT
core_functions:
- description: >-
    EryCII is required to activate the desosaminyl transferase EryCIII: EryCIII is
    inactive on its own, and EryCII allosterically activates and stabilizes it within
    the alpha2-beta2 EryCII-EryCIII heterotetramer (via its N-terminal A'' helix
    contacting EryCIII's acceptor domain), enabling glycosyl transfer to the macrolide
    and hence the desosaminylation step of erythromycin biosynthesis (PMID:22056329,
    PMID:15303858; PDB 2YJN). This activator/stabilizer role is the accurate molecular
    function in place of the inherited (incorrect) P450 catalytic terms. The fold
    stabilization is conformational-chaperone-like, but EryCII is a stably bound
    stoichiometric subunit, not a transient folding chaperone.
  molecular_function:
    id: GO:0008047
    label: enzyme activator activity
  directly_involved_in:
    - id: GO:0050821
      label: protein stabilization
    - id: GO:1901115
      label: erythromycin biosynthetic process
  in_complex:
    id: GO:0032991
    label: protein-containing complex
  supported_by:
  - reference_id: PMID:22056329
    supporting_text: >-
      EryCII stabilizes EryCIII and also functions as an allosteric activator of the GT
  - reference_id: PMID:22056329
    supporting_text: >-
      one function of the auxiliary proteins is to stabilize the fold and quaternary
      structure of its partner GT
suggested_questions:
- question: >-
    Would a dedicated "glycosyltransferase activator activity" term (child of
    GO:0008047) better capture the role of EryCII and analogous P450-homologue GT
    activators (e.g. in other deoxysugar pathways)?
suggested_experiments:
- description: >-
    Confirm absence of heme binding and monooxygenase activity for purified EryCII, and
    quantify EryCIII GT stimulation as a function of EryCII, to formally retire the P450
    catalytic annotations.

eryCII

Gene Description

Existing Annotations Review

Core Functions

References

Suggested Questions for Experts

Suggested Experiments

📚 Additional Documentation

Notes

eryCII (A4F7P2, SACE_0725) — review notes

Function — a P450 PSEUDOENZYME that activates a glycosyltransferase

Annotation issues — domain-based over-annotation of a pseudoenzyme

"Conformational chaperone"?

Capturing absence of function (NOT annotations)

Predicted-complex evidence (BGC project)

References

📄 View Raw YAML