ectoine biosynthesis
MetaCyc:P101-PWY
Ectoine biosynthesis converts L-aspartate to L-ectoine through 4-phospho-L-aspartate, L-aspartate 4-semialdehyde, L-2,4-diaminobutanoate, and (2S)-4-acetamido-2-aminobutanoate.
- Pathway type
- compatible solute biosynthesis
- Organism scope
Pathway network
33 nodes · 38 asserted directed edges
Arrows show recorded subject → object relationships, not necessarily metabolic flow. Select a node for details or an arrow for evidence. Scroll, zoom or find a node to explore.
- Reaction / activity
- Chemical / cofactor
- Protein / complex
- Other participant
- Cell / process context
- Solid arrow: mechanistic relation
- Dashed arrow: membership, location or cofactor relation
Components and activities
| Node | Kind or role | Source direction |
|---|---|---|
Halomonas elongataNCBITaxon:2746 | taxon | |
aspartate kinaseEC:2.7.2.4 | molecular activity | |
aspartate-semialdehyde dehydrogenaseEC:1.2.1.11 | molecular activity | |
diaminobutyrate-2-oxoglutarate transaminaseEC:2.6.1.76 | molecular activity | |
diaminobutyrate acetyltransferaseEC:2.3.1.178 | molecular activity | |
ectoine synthaseEC:4.2.1.108 | molecular activity | |
L-aspartateCHEBI:29991 | small molecule | |
ATPCHEBI:30616 | small molecule | |
4-phospho-L-aspartateCHEBI:57535 | small molecule | |
ADPCHEBI:456216 | small molecule | |
NADPHCHEBI:57783 | small molecule | |
H+CHEBI:15378 | small molecule | |
L-aspartate 4-semialdehydeCHEBI:537519 | small molecule | |
phosphateCHEBI:43474 | small molecule | |
NADP(+)CHEBI:58349 | small molecule | |
L-glutamateCHEBI:29985 | small molecule | |
L-2,4-diaminobutanoateCHEBI:58761 | small molecule | |
2-oxoglutarateCHEBI:16810 | small molecule | |
acetyl-CoACHEBI:57288 | small molecule | |
(2S)-4-acetamido-2-aminobutanoateCHEBI:58929 | small molecule | |
CoACHEBI:57287 | small molecule | |
L-ectoineCHEBI:58515 | small molecule | |
H2OCHEBI:15377 | small molecule | |
Diaminobutyrate--2-oxoglutarate transaminaseUniProtKB:E1V7V7 | protein | |
cytoplasmGO:0005737 | cellular component | |
pyridoxal 5'-phosphate(2-)CHEBI:597326 | cofactor | |
L-2,4-diaminobutyric acid acetyltransferaseUniProtKB:O52249 | protein | |
Diaminobutyrate--2-oxoglutarate transaminaseUniProtKB:O52250 | protein | |
L-ectoine synthaseUniProtKB:O52251 | protein | |
ATP-dependent aspartate kinase reactionRHEA:23777 | reaction | left to right |
NADPH-dependent aspartate-semialdehyde dehydrogenase reactionRHEA:24286 | reaction | right to left |
biosynthetic diaminobutyrate transaminase reactionRHEA:11162 | reaction | right to left |
diaminobutanoate acetyltransferase reactionRHEA:16902 | reaction | left to right |
L-ectoine synthase reactionRHEA:17282 | reaction | left to right |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
L-aspartateCHEBI:29991 | consumes | ATP-dependent aspartate kinase reactionRHEA:23777 |
|
ATPCHEBI:30616 | consumes | ATP-dependent aspartate kinase reactionRHEA:23777 |
|
ATP-dependent aspartate kinase reactionRHEA:23777 | produces | ADPCHEBI:456216 |
|
ATP-dependent aspartate kinase reactionRHEA:23777 | produces | 4-phospho-L-aspartateCHEBI:57535 |
|
H+CHEBI:15378 | consumes | NADPH-dependent aspartate-semialdehyde dehydrogenase reactionRHEA:24286 |
|
4-phospho-L-aspartateCHEBI:57535 | consumes | NADPH-dependent aspartate-semialdehyde dehydrogenase reactionRHEA:24286 |
|
NADPHCHEBI:57783 | consumes | NADPH-dependent aspartate-semialdehyde dehydrogenase reactionRHEA:24286 |
|
NADPH-dependent aspartate-semialdehyde dehydrogenase reactionRHEA:24286 | produces | phosphateCHEBI:43474 |
|
NADPH-dependent aspartate-semialdehyde dehydrogenase reactionRHEA:24286 | produces | L-aspartate 4-semialdehydeCHEBI:537519 |
|
NADPH-dependent aspartate-semialdehyde dehydrogenase reactionRHEA:24286 | produces | NADP(+)CHEBI:58349 |
|
L-glutamateCHEBI:29985 | consumes | biosynthetic diaminobutyrate transaminase reactionRHEA:11162 |
|
L-aspartate 4-semialdehydeCHEBI:537519 | consumes | biosynthetic diaminobutyrate transaminase reactionRHEA:11162 |
|
biosynthetic diaminobutyrate transaminase reactionRHEA:11162 | produces | 2-oxoglutarateCHEBI:16810 |
|
biosynthetic diaminobutyrate transaminase reactionRHEA:11162 | produces | L-2,4-diaminobutanoateCHEBI:58761 |
|
acetyl-CoACHEBI:57288 | consumes | diaminobutanoate acetyltransferase reactionRHEA:16902 |
|
L-2,4-diaminobutanoateCHEBI:58761 | consumes | diaminobutanoate acetyltransferase reactionRHEA:16902 |
|
diaminobutanoate acetyltransferase reactionRHEA:16902 | produces | H+CHEBI:15378 |
|
diaminobutanoate acetyltransferase reactionRHEA:16902 | produces | CoACHEBI:57287 |
|
diaminobutanoate acetyltransferase reactionRHEA:16902 | produces | (2S)-4-acetamido-2-aminobutanoateCHEBI:58929 |
|
(2S)-4-acetamido-2-aminobutanoateCHEBI:58929 | consumes | L-ectoine synthase reactionRHEA:17282 |
|
L-ectoine synthase reactionRHEA:17282 | produces | H2OCHEBI:15377 |
|
L-ectoine synthase reactionRHEA:17282 | produces | L-ectoineCHEBI:58515 |
|
aspartate kinaseEC:2.7.2.4 | catalyzes | ATP-dependent aspartate kinase reactionRHEA:23777 |
|
aspartate-semialdehyde dehydrogenaseEC:1.2.1.11 | catalyzes | NADPH-dependent aspartate-semialdehyde dehydrogenase reactionRHEA:24286 |
|
diaminobutyrate-2-oxoglutarate transaminaseEC:2.6.1.76 | catalyzes | biosynthetic diaminobutyrate transaminase reactionRHEA:11162 |
|
diaminobutyrate acetyltransferaseEC:2.3.1.178 | catalyzes | diaminobutanoate acetyltransferase reactionRHEA:16902 |
|
ectoine synthaseEC:4.2.1.108 | catalyzes | L-ectoine synthase reactionRHEA:17282 |
|
biosynthetic diaminobutyrate transaminase reactionRHEA:11162 | precedes | diaminobutanoate acetyltransferase reactionRHEA:16902 |
|
diaminobutanoate acetyltransferase reactionRHEA:16902 | precedes | L-ectoine synthase reactionRHEA:17282 |
|
ATP-dependent aspartate kinase reactionRHEA:23777 | precedes | NADPH-dependent aspartate-semialdehyde dehydrogenase reactionRHEA:24286 |
|
NADPH-dependent aspartate-semialdehyde dehydrogenase reactionRHEA:24286 | precedes | biosynthetic diaminobutyrate transaminase reactionRHEA:11162 |
|
Diaminobutyrate--2-oxoglutarate transaminaseUniProtKB:E1V7V7 | enables | biosynthetic diaminobutyrate transaminase reactionRHEA:11162 |
|
Diaminobutyrate--2-oxoglutarate transaminaseUniProtKB:E1V7V7 | located_in | cytoplasmGO:0005737 |
|
Diaminobutyrate--2-oxoglutarate transaminaseUniProtKB:E1V7V7 | has_cofactor | pyridoxal 5'-phosphate(2-)CHEBI:597326 |
|
L-2,4-diaminobutyric acid acetyltransferaseUniProtKB:O52249 | enables | diaminobutanoate acetyltransferase reactionRHEA:16902 |
|
Diaminobutyrate--2-oxoglutarate transaminaseUniProtKB:O52250 | enables | biosynthetic diaminobutyrate transaminase reactionRHEA:11162 |
|
Diaminobutyrate--2-oxoglutarate transaminaseUniProtKB:O52250 | has_cofactor | pyridoxal 5'-phosphate(2-)CHEBI:597326 |
|
L-ectoine synthaseUniProtKB:O52251 | enables | L-ectoine synthase reactionRHEA:17282 |
|
References
MetaCyc:P101-PWYMetaCyc ectoine biosynthesis pathway (source version: 22.5)RHEA:23777Rhea L-aspartate kinase direction (source version: 139)RHEA:24286Rhea biosynthetic aspartate-semialdehyde dehydrogenase direction (source version: 139)RHEA:11162Rhea biosynthetic diaminobutyrate transaminase direction (source version: 139)RHEA:16902Rhea diaminobutanoate acetyltransferase direction (source version: 139)RHEA:17282Rhea L-ectoine synthase direction (source version: 139)PMID:9864317Ono et al., Journal of Bacteriology, 1999RHEA:23776RHEA:23776 authority record (source version: 139)RHEA:24284RHEA:24284 authority record (source version: 139)RHEA:11160RHEA:11160 authority record (source version: 139)RHEA:16901RHEA:16901 authority record (source version: 139)RHEA:17281RHEA:17281 authority record (source version: 139)UniProtKB:E1V7V7UniProtKB:E1V7V7 authority record (source version: 2026_03)UniProtKB:O52249UniProtKB:O52249 authority record (source version: 2026_03)UniProtKB:O52250UniProtKB:O52250 authority record (source version: 2026_03)UniProtKB:O52251UniProtKB:O52251 authority record (source version: 2026_03)
Curation history
- codex
- EDIT — Review causal chemistry and add sourced molecular context
Reviewed the entire record against MetaCyc 22.5 native pathway XML (including nested pathways), Rhea 139 explicit sides and directions, ENZYME 02-Sep-2026, PubMed records, and reviewed UniProt 2026_03 annotations within the record's taxon scope. Replaced generated structured-source quotations with source_assertion and source_locator. Typed molecular activities and participants. Reaction count 5 to 5; 0 directed-ID corrections; 4 protein annotations, 2 cofactor annotations and 1 sourced locations. All Rhea reaction substrate/product sets checked against independent Rhea authority; native pathway leaf coverage and source exceptions recorded in reports/causal_graph_review/metacyc-review.json. Full source URLs, versions and byte hashes are in metacyc-sources.json. All 50 MetaCyc records passed native schema validation; six targeted chemistry/evidence regression tests passed. Missing protein or cofactor annotations are not treated as biological absence; qualifications and exclusions are preserved in the ledger.
- EDIT — Review causal chemistry and add sourced molecular context