sulfur globule

traitmech:000069 · CLASS · REVIEWED

An intracellular (or periplasmic) inclusion of elemental sulfur formed as an intermediate during the oxidation of reduced sulfur compounds, characteristic of many sulfur-oxidizing and phototrophic sulfur bacteria.

Sulfur globules store elemental sulfur during oxidative sulfur metabolism

Evidence-backed causal sketch linking oxidative sulfur metabolism to deposition of elemental sulfur as intracellular/periplasmic globules.

Sulfur globules store elemental sulfur during oxidative sulfur metabolism Interactive directed graph showing evidence-backed causal relationships for sulfur globule.

Edge evidence

  • oxidative sulfur metabolism has output elemental sulfur RO:0002234

    Oxidation of reduced sulfur compounds generates elemental sulfur as an intermediate.

    • DOI:10.1016/S0065-2911(08)00002-7 Frigaard & Dahl describe sulfur globules as sulfur-storage intermediates formed during oxidative sulfur metabolism.
  • elemental sulfur located in sulfur globule biolink:located_in

    The deposited elemental sulfur forms a globule inclusion.

    • DOI:10.1038/s41579-020-0413-0 Greening & Lithgow include sulfur globules among bacterial intracellular storage inclusions.
  • sulfide:quinone oxidoreductase (SQR) produces sulfane sulfur METPO:2007800

    SQR-catalyzed oxidation of sulfide generates sulfane sulfur intermediates.

    • DOI:10.3390/ijms252010962 Initial oxidation of sulfide occurs under the action of SQR, producing sulfane sulfur; generalizes broadly to intracellular sulfur oxidizers.
  • sulfide:quinone oxidoreductase (SQR) produces polysulfide (H2Sn) METPO:2007800

    SQR oxidizes sulfide to short-chain inorganic polysulfide (H2Sn, n>=2).

    • DOI:10.1128/aem.01941-21 SQR oxidized H2S into short-chain inorganic polysulfide (H2Sn, n >= 2); broad sulfur-chemistry mechanism.
  • polysulfide (H2Sn) precursor of sulfur globule

    Polysulfide/sulfane sulfur spontaneously generates S8 that aggregates into sulfur globules.

    • DOI:10.1128/aem.01941-21 SQR oxidized H2S to H2Sn, which spontaneously generated S8; S8 aggregated into sulfur globules.
  • persulfide dioxygenase (PDO) oxidizes sulfite METPO:2007803

    PDO oxidizes glutathione persulfide (GSSH) to sulfite (GSSH + O2 + H2O -> GSH + SO3^2- + 2H+).

    • DOI:10.3390/ijms252010962 PDO acts on GSSH: GSSH + O2 + H2O -> GSH + SO3^2- + 2H+; well-defined enzymatic edge.
  • persulfide dioxygenase (PDO) participates in oxidative sulfur metabolism biolink:participates_in

    PDO acts downstream of SQR in the same sulfide-oxidation pathway that deposits elemental sulfur as globules.

    • PMID:35653932 Heterotrophic bacteria and human mitochondria often use sulfide: quinone oxidoreductase (SQR) and persulfide dioxygenase (PDO) to oxidize sulfide to sulfite and thiosulfate. Places PDO in the same SQR-initiated sulfide-oxidation pathway the rest of this graph models, which is what attaches the PDO/sulfite branch to the globule mechanism rather than leaving it a free-standing enzymatic fact. Scope caveat (issue 297) - the quote covers heterotrophic bacteria and human mitochondria, not the Thiomargarita/Beggiatoa exemplars of this trait, so it supports the generic pathway claim the object node makes and no more.

Provenance

Source
METPO (2025-11-25)
Definition source
DOI:10.1016/S0065-2911(08)00002-7

Synonyms (1)

  • sulfur inclusion RELATED_SYNONYM · DOI:10.1016/S0065-2911(08)00002-7

kg-microbe context

Matched 1 kg-microbe node via parent_proxy.

  • METPO:1000059 [-2.682, -2.070, -3.656, -0.652, …]

512-dim DeepWalkSkipGramEnsmallen embedding from kg-microbe (2026-04-25).

Nearest neighbors in embedding space

Top-8 cosine-similar METPO traits from the 2026-04-25 deepwalk (512-D).

Deep research

Generated by just research-trait; source: research/traits/morphology/sulfur_globule-deep-research-falcon.md

Unreviewed literature output — not curated TraitMech content Ontology identifiers suggested below have not been resolved against their ontologies, and some are known to be wrong. Check any CURIE against the source before using it.
# Curation-focused research report: sulfur globule

**Trait:** `traitmech:000069`  
**Category:** MORPHOLOGY | **Term kind:** CLASS | **Mapping:** REVIEWED  
**Parent:** `traitmech:000066`  
**Synonym:** sulfur inclusion

## 1. Scope and current interpretation

For TraitMech, a **sulfur globule** should denote a cell-associated, microscopically discernible inclusion enriched in zero-valent/elemental sulfur, formed during oxidation of reduced sulfur compounds. It may be **cytoplasmic** or **periplasmic (intracellular but extracytoplasmic)** and ordinarily represents a transient metabolic intermediate or reserve that can subsequently be oxidized. In *Allochromatium vinosum*, globules are obligatory periplasmic intermediates of oxidative sulfur metabolism; in SQR-containing aerobic bacteria, S8 can instead aggregate in the cytoplasm. These are mechanistically distinct realizations of the same high-level morphology (wang2022thepathwayof pages 3-4, wang2022thepathwayof pages 1-3, kumpel2023cellbiologyof pages 1-3).

The graph should not imply that all sulfur globules share one coat, localization, chemical allotrope, or downstream oxidation pathway. Classical Sgp-coated globules are best established in *A. vinosum*, whereas *Beggiatoa leptomitoformis* D-402 uses a distinct PDO/Sox-associated route and lacks several canonical sulfur-oxidation systems (rudenko2024mechanismofintracellular pages 10-12, kumpel2023cellbiologyof pages 1-3).

### Boundary cases

1. **Extracellular biogenic S(0): exclude from this trait.** *Chlorobaculum tepidum* uses extracellular biogenic sulfur particles requiring direct cell contact and oxidizes them to sulfate. These are substrates outside the cell, not intracellular/periplasmic inclusions (hanson2016chlorobaculumtepidumgrowth pages 5-6).
2. **Desulfurase encapsulins: exclude or model as a sibling trait.** The 2024 system is a 24-nm, T=1 icosahedral protein nanocompartment containing cysteine desulfurase and crystalline S0. Its cysteine-derived sulfur, ordered shell, nanoscale architecture, and proposed assimilatory/detoxification role distinguish it from lithotrophic sulfur globules (benisch2024awidespreadbacterial pages 9-10, benisch2024awidespreadbacterial pages 1-2, benisch2024awidespreadbacterial pages 3-4).
3. **Visible extracellular sulfur deposits adjacent to cells:** do not infer `traitmech:000069` without localization evidence.
4. **Generic “sulfur granule” annotations:** insufficient unless microscopy, fractionation, or localization establishes a cell-associated inclusion.

| candidate mechanism/edge | exemplar taxon | evidence strength | curate now? | key caveat |
|---|---|---|---|---|
| Sulfur globule envelope proteins SgpA/SgpB/SgpC support classical periplasmic sulfur globule formation/expansion; rDsr supports downstream oxidation of stored sulfur | *Allochromatium vinosum* | Strong for this taxon; direct microscopy/genetic evidence (kumpel2023cellbiologyof pages 1-3, kumpel2023cellbiologyof pages 7-10) | Yes, as taxon-scoped edges | 2023 source is a preprint; avoid overgeneralizing to all sulfur bacteria without broader evidence (kumpel2023cellbiologyof pages 1-3, kumpel2023cellbiologyof pages 7-10) |
| SQR-catalyzed sulfide oxidation produces polysulfides that spontaneously yield S8, which aggregates into cytoplasmic sulfur globules | *Corynebacterium vitaeruminis* DSM 20294; recombinant *Escherichia coli* | Strong for SQR-to-S8 cytoplasmic route in tested systems (wang2022thepathwayof pages 3-4, wang2022thepathwayof pages 1-3) | Yes, but mark as non-classical/taxon-contextual | Represents a cytoplasmic aerobic route distinct from classical periplasmic Sgp-coated globules; engineered *E. coli* evidence should not be treated as native species-wide trait evidence (wang2022thepathwayof pages 3-4, wang2022thepathwayof pages 1-3) |
| Intracellular sulfur oxidation uses PDO to oxidize stored sulfur to sulfite, with thiosulfate then oxidized by periplasmic Sox system | *Beggiatoa leptomitoformis* D-402 | Moderate to strong; multi-omic and biochemical support in one species (rudenko2024mechanismofintracellular pages 10-12) | Yes, as uncertain/taxon-specific consumption pathway edges | Mechanism is unusual because this strain lacks canonical Dsr/SOR routes; formation steps are less directly established than oxidation steps (rudenko2024mechanismofintracellular pages 10-12) |
| Direct utilization of extracellular biogenic S(0) globules as electron donor | *Chlorobaculum tepidum* | Strong for extracellular sulfur use, not for sulfur globule trait itself (hanson2016chlorobaculumtepidumgrowth pages 5-6) | No | Boundary case: evidence concerns extracellular biogenic sulfur particles requiring cell contact, not intracellular/periplasmic sulfur globules matching traitmech:000069 (hanson2016chlorobaculumtepidumgrowth pages 5-6) |
| Cysteine-desulfurase encapsulin stores elemental sulfur inside a 24-nm protein nanocompartment | desulfurase-encapsulin bacteria (broad distribution) | Strong for encapsulin sulfur storage as a distinct compartment (benisch2024awidespreadbacterial pages 9-10, benisch2024awidespreadbacterial pages 8-9, benisch2024awidespreadbacterial pages 6-7, benisch2024awidespreadbacterial pages 4-6, benisch2024awidespreadbacterial pages 1-2, benisch2024awidespreadbacterial pages 3-4) | No | Distinct boundary case: ordered protein nanocompartment, cysteine-derived sulfur donor, likely detoxification/assimilatory role, and nanometer-scale shell differ from classical sulfur globules used in sulfur oxidation metabolism (benisch2024awidespreadbacterial pages 9-10, benisch2024awidespreadbacterial pages 1-2) |


*Table: This table summarizes which sulfur-storage mechanisms are strong candidates for TraitMech curation of traitmech:000069 and which are better treated as boundary cases. It helps separate classical sulfur globules from related but mechanistically distinct sulfur inclusions or extracellular sulfur particles.*

## 2. Candidate nodes grouped by type

### Focal morphology and localization

| Node | Type | Suggested grounding |
|---|---|---|
| sulfur globule | morphology | `traitmech:000069` |
| sulfur-globule envelope | cellular structure | Label only |
| cytoplasm | localization | `GO:0005737` |
| periplasmic space | localization | `GO:0042597` |
| extracellular biogenic sulfur particle | boundary morphology | Label only; exclude from focal trait |
| desulfurase encapsulin | protein nanocompartment/boundary case | Label only pending system-specific grounding |

### Chemicals and metabolites

Use label-only nodes until the exact ChEBI record and protonation state have been curator-verified:

- hydrogen sulfide/sulfide;
- thiosulfate;
- elemental sulfur, S0;
- octasulfur, S8;
- short- and long-chain inorganic polysulfides;
- organic polysulfides;
- sulfane sulfur;
- glutathione and glutathione persulfide;
- sulfite;
- sulfate;
- L-cysteine, relevant to the excluded encapsulin system.

Showing the first 60 of 202 lines of findings; the linked file also carries the run's front matter and the prompt it was given — read the full report.

Curation history

  1. · PROPOSED_FROM_RESEARCH · claude

    Proposed candidate MORPHOLOGY trait (sulfur globule); storage sub-variant of intracellular inclusion.

  2. · CURATED_CAUSAL_GRAPH · claude

    Added evidence-backed causal graph (oxidative sulfur metabolism → elemental sulfur globule) with METPO/biolink predicate groundings; promoted PROPOSED to REVIEWED.

  3. · GROUND_CAUSAL_NODES · claude

    Grounded 1 causal-node grounding field(s) via mappings/node_grounding.tsv (CHEBI:26833×1).

  4. · ENRICH_CAUSAL_GRAPH · claude

    Added 4 evidence-backed generic edges (5 new nodes) from the deep-research report.

  5. · GROUND_CAUSAL_PREDICATES · claude

    Grounded 3 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (METPO:2000202×2, METPO:2000016×1).

  6. · GROUND_CAUSAL_NODES · claude

    Grounded 1 causal-node grounding field(s) via mappings/node_grounding.tsv (GO:0070224×1).

  7. · ENRICH_CAUSAL_GRAPH · claude

    Added 1 evidence-backed edge attaching the stranded PDO/sulfite branch to the pathway the rest of the graph models (issue 183): persulfide_dioxygenase participates in oxidative_sulfur_metabolism, grounded biolink:participates_in. The snippet is verbatim from PMID:35653932, checked against the PubMed abstract. Resolves this graph's FRAGMENTED_GRAPH and its 2 UNREACHABLE_FROM_TRAIT findings.

  8. · MIGRATE_MICROBE_DOMAIN_EDGES · claude

    Re-grounded 1 causal edge(s) off microbe-domain METPO predicates (1 to has output), issue 301. The previous predicates are transitively rdfs:subPropertyOf METPO:2000001, whose rdfs:domain is METPO:1000525 (microbe), so a causal-graph subject entailed that the subject IS a microbe; CausalNodeTypeEnum has no organism member, so no such edge could ever satisfy the domain. Edge directions are unchanged - this pass only relabels and re-grounds. RO:0002234 (has output) is used where the subject is an activity, since biolink gives it the domain 'biological process or activity'; the METPO replacements are proposed in proposals/metpo_traitmech_v8 and v9 and are placeholder ids until METPO mints them.

  9. · MIGRATE_MICROBE_DOMAIN_EDGES_PART2 · claude

    Re-grounded 3 causal edge(s) off microbe-domain METPO predicates onto their causal-graph counterparts (1 to oxidizes, 2 to produces), issue 301 part 2. The previous predicates are transitively rdfs:subPropertyOf METPO:2000001, whose rdfs:domain is METPO:1000525 (microbe), so a causal-graph subject entailed that the subject IS a microbe; CausalNodeTypeEnum has no organism member, so no such edge could ever satisfy the domain. Each replacement is a 1:1 mirror of its source predicate that changes only the domain, so the claim each edge makes is unchanged and directions are unchanged. The replacements are proposed in proposals/metpo_traitmech_v9 and are placeholder ids until METPO mints them.