A4YDR9 · HBCL2_METS5
- Protein4-hydroxybutyrate--CoA ligase 2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids549 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the ligation of coenzyme A (CoA) to 4-hydroxybutyrate (4HB). It can also use butyrate, valerate, propionate, acetate and 3-hydroxybutyrate (3HB) as substrates.
Catalytic activity
- 4-hydroxybutanoate + ATP + CoA = 4-hydroxybutanoyl-CoA + AMP + diphosphate
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
60 μM | butyrate | |||||
120 μM | valerate | |||||
540 μM | propionate | |||||
680 μM | acetate | |||||
1540 μM | 4HB | |||||
1880 μM | 3HB |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.22 μmol/min/mg | with 4HB as substrate | ||||
0.21 μmol/min/mg | with butyrate as substrate | ||||
0.2 μmol/min/mg | with valerate as substrate | ||||
0.2 μmol/min/mg | with propionate as substrate | ||||
0.13 μmol/min/mg | with acetate as substrate | ||||
0.07 μmol/min/mg | with 3HB as substrate |
kcat is 0.24 sec-1 for ligase activity with 4HB as substrate. kcat is 0.23 sec-1 for ligase activity with butyrate as substrate. kcat is 0.22 sec-1 for ligase activity with valerate as substrate. kcat is 0.21 sec-1 for ligase activity with propionate as substrate. kcat is 0.14 sec-1 for ligase activity with acetate as substrate. kcat is 0.08 sec-1 for ligase activity with 3HB as substrate.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 195-203 | ATP (UniProtKB | ChEBI) | ||||
Sequence: TSGTTGLPK | ||||||
Binding site | 336-341 | ATP (UniProtKB | ChEBI) | ||||
Sequence: ETYGPH | ||||||
Binding site | 425 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 440 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 448-450 | CoA (UniProtKB | ChEBI) | ||||
Sequence: GGE | ||||||
Binding site | 506 | CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 514-516 | CoA (UniProtKB | ChEBI) | ||||
Sequence: CPK | ||||||
Binding site | 530 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | acetate-CoA ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | medium-chain fatty acid-CoA ligase activity | |
Molecular Function | propionate-CoA ligase activity | |
Biological Process | fatty acid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4-hydroxybutyrate--CoA ligase 2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Metallosphaera
Accessions
- Primary accessionA4YDR9
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000435709 | 1-549 | 4-hydroxybutyrate--CoA ligase 2 | |||
Sequence: MGGFKIPNYEGVDPTGSWYSVLTPLLFLERAGKYFKDKTAVVYRDSRYTYSTFYDNVMVQASALMRRGFSREDKLSFISRNRPEFLESFFGVPYAGGVLVPINFRLSPKEMAYIINHSDSKFVVVDEPYLNSLLEVKDQIKAEIILLEDPDNPSASETARKEVRMTYRELVKGGSRDPLPIPAKEEYSMITLYYTSGTTGLPKGVMHHHRGAFLNAMAEVLEHQMDLNSVYLWTLPMFHAASWGFSWATVAVGATNVCLDKVDYPLIYRLVEKERVTHMCAAPTVYVNLADYMKRNNLKFSNRVHMLVAGAAPAPATLKAMQEIGGYMCHVYGLTETYGPHSICEWRREWDSLPLEEQAKLKARQGIPYVSFEMDVFDANGKPVPWDGKTIGEVVMRGHNVALGYYKNPEKTAESFRDGWFHSGDAAVVHPDGYIEIVDRFKDLINTGGEKVSSILVEKTLMEIPGVKAVAVYGTPDEKWGEVVTARIELQEGVKLTEEEVIKFCKERLAHFECPKIVEFGPIPMTATGKMQKYVLRNEAKAKANKEKS |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length549
- Mass (Da)62,011
- Last updated2007-05-29 v1
- Checksum31D61ED874513B53
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000682 EMBL· GenBank· DDBJ | ABP94571.1 EMBL· GenBank· DDBJ | Genomic DNA |