C3NHU6 · HOSA_SULIN
- ProteinHomocitrate synthase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids461 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Catalyzes the aldol-type condensation of 2-oxoglutarate with acetyl-CoA to yield homocitrate. Carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway.
Catalytic activity
- 2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA + H+This reaction proceeds in the forward direction.
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Pathway
Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 1/5.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 12 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 13 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 76 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 136 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 170 | 2-oxoglutarate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 198 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 200 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 292 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | homocitrate synthase activity | |
Molecular Function | metal ion binding | |
Biological Process | lysine biosynthetic process via aminoadipic acid |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHomocitrate synthase
- EC number
- Short namesHCS
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Sulfolobus
Accessions
- Primary accessionC3NHU6
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000213321 | 1-461 | Homocitrate synthase | |||
Sequence: MIKVGILDSTLREGEQTPGVIFTVDQRVEIAKALSDLGVSMIEAGHPAVSPDIYEGIKRIVKLKKEGIITSEIVGHSRAVKRDIEIAAELEVDRIAIFYGVSDLHLKAKHKATREEALRTIAETISYAKNHGVKVRFTAEDGSRTDFDFLVTVSKTARDAGADRVSIADTVGILYPSKTKELFSALTREVPNLEFDIHAHNDLGLAVANALAAIEGGATIIHATVNGLGERVGIVPLQQIAAAIKYHFGIEVVKLDKLQYVSSLVEKYSGIPMPPNYPITGDYAFLHKAGVHVAGVLNDPRTYEFMPPETFGRTRDYTIDKYTGKHALRDKYEKLGVKISDAEMDQILAKIKSNTTIRFYRDVDLLELAEEVTGRVLKPRPPEQIEALISVKCDSNVYTTSVTRRLSVINGVKEVMEISGDYDILVKVQAKDSNELNQIIESIRATKGVRSTLTSLVLKKM |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-259 | Pyruvate carboxyltransferase | ||||
Sequence: VGILDSTLREGEQTPGVIFTVDQRVEIAKALSDLGVSMIEAGHPAVSPDIYEGIKRIVKLKKEGIITSEIVGHSRAVKRDIEIAAELEVDRIAIFYGVSDLHLKAKHKATREEALRTIAETISYAKNHGVKVRFTAEDGSRTDFDFLVTVSKTARDAGADRVSIADTVGILYPSKTKELFSALTREVPNLEFDIHAHNDLGLAVANALAAIEGGATIIHATVNGLGERVGIVPLQQIAAAIKYHFGIEVVKLDKLQ |
Sequence similarities
Belongs to the alpha-IPM synthase/homocitrate synthase family. Homocitrate synthase LYS20/LYS21 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length461
- Mass (Da)50,825
- Last updated2009-06-16 v1
- Checksum1067BD15BAEF4646
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001404 EMBL· GenBank· DDBJ | ACP48706.1 EMBL· GenBank· DDBJ | Genomic DNA |