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
Edge evidence
-
oxidative sulfur metabolism
has output
elemental sulfur
RO:0002234Oxidation of reduced sulfur compounds generates elemental sulfur as an intermediate.
-
DOI:10.1016/S0065-2911(08)00002-7
-
-
elemental sulfur
located in
sulfur globule
biolink:located_inThe deposited elemental sulfur forms a globule inclusion.
-
DOI:10.1038/s41579-020-0413-0
-
-
sulfide:quinone oxidoreductase (SQR)
produces
sulfane sulfur
METPO:2007800SQR-catalyzed oxidation of sulfide generates sulfane sulfur intermediates.
-
DOI:10.3390/ijms252010962
-
-
sulfide:quinone oxidoreductase (SQR)
produces
polysulfide (H2Sn)
METPO:2007800SQR oxidizes sulfide to short-chain inorganic polysulfide (H2Sn, n>=2).
-
DOI:10.1128/aem.01941-21
-
-
polysulfide (H2Sn)
precursor of
sulfur globule
Polysulfide/sulfane sulfur spontaneously generates S8 that aggregates into sulfur globules.
-
DOI:10.1128/aem.01941-21
-
-
persulfide dioxygenase (PDO)
oxidizes
sulfite
METPO:2007803PDO oxidizes glutathione persulfide (GSSH) to sulfite (GSSH + O2 + H2O -> GSH + SO3^2- + 2H+).
-
DOI:10.3390/ijms252010962
-
-
persulfide dioxygenase (PDO)
participates in
oxidative sulfur metabolism
biolink:participates_inPDO acts downstream of SQR in the same sulfide-oxidation pathway that deposits elemental sulfur as globules.
-
PMID:35653932Heterotrophic bacteria and human mitochondria often use sulfide: quinone oxidoreductase (SQR) and persulfide dioxygenase (PDO) to oxidize sulfide to sulfite and thiosulfate.
-
Provenance
- Source
- METPO (2025-11-25)
- Definition source
- DOI:10.1016/S0065-2911(08)00002-7
Parent traits (1)
Synonyms (1)
- sulfur inclusion
kg-microbe context
Matched 1 kg-microbe node via parent_proxy.
METPO:1000059[-2.682, -2.070, -3.656, -0.652, …]
Nearest neighbors in embedding space
- environment cadmium tolerant 1.000
- physiology bioluminescence 1.000
- environment cobalt tolerant 1.000
- environment copper tolerant 1.000
- environment desiccation tolerant 1.000
- environment piezotolerant 1.000
- environment obligately piezophilic 1.000
- morphology gas vesicle 1.000
Deep research
# 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.
Curation history
-
·
PROPOSED_FROM_RESEARCH · claude
Proposed candidate MORPHOLOGY trait (sulfur globule); storage sub-variant of intracellular inclusion.
-
·
CURATED_CAUSAL_GRAPH · claude
Added evidence-backed causal graph (oxidative sulfur metabolism → elemental sulfur globule) with METPO/biolink predicate groundings; promoted PROPOSED to REVIEWED.
-
·
GROUND_CAUSAL_NODES · claude
Grounded 1 causal-node grounding field(s) via mappings/node_grounding.tsv (CHEBI:26833×1).
-
·
ENRICH_CAUSAL_GRAPH · claude
Added 4 evidence-backed generic edges (5 new nodes) from the deep-research report.
-
·
GROUND_CAUSAL_PREDICATES · claude
Grounded 3 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (METPO:2000202×2, METPO:2000016×1).
-
·
GROUND_CAUSAL_NODES · claude
Grounded 1 causal-node grounding field(s) via mappings/node_grounding.tsv (GO:0070224×1).
-
·
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.
-
·
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.
-
·
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.