Q86KR9 · P4HA_DICDI
- ProteinProlyl 4-hydroxylase subunit alpha
- GenephyA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids284 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the post-translational formation of 4-hydroxyproline. Probably hydroxylates skp1 on Pro-143.
Catalytic activity
- 2-oxoglutarate + L-prolyl-[Skp1 protein] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[Skp1 protein]
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Fe2+ ion per subunit.
Activity regulation
Inhibited by the prolyl-hydroxylase inhibitors alpha,alpha'-dipyridyl and ethyl 3,4-dihydroxybenzoate.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ferrous iron binding | |
Molecular Function | L-ascorbic acid binding | |
Molecular Function | peptidyl-proline 4-dioxygenase activity | |
Molecular Function | peptidyl-proline dioxygenase activity | |
Biological Process | cellular response to hypoxia | |
Biological Process | culmination involved in sorocarp development | |
Biological Process | oxygen metabolic process | |
Biological Process | SCF complex assembly |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProlyl 4-hydroxylase subunit alpha
- EC number
- Short namesProlyl 4-hydrolase
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Amoebozoa > Evosea > Eumycetozoa > Dictyostelia > Dictyosteliales > Dictyosteliaceae > Dictyostelium
Accessions
- Primary accessionQ86KR9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000327577 | 1-284 | Prolyl 4-hydroxylase subunit alpha | |||
Sequence: MDISNLPPHIRQQILGLISKPQQNNDESSSSNNKNNLINNEKVSNVLIDLTSNLKIENFKIFNKESLNQLEKKGYLIIDNFLNDLNKINLIYDESYNQFKENKLIEAGMNKGTDKWKDKSIRGDYIQWIHRDSNSRIQDKDLSSTIRNINYLLDKLDLIKNEFDNVIPNFNSIKTQTQLAVYLNGGRYIKHRDSFYSSESLTISRRITMIYYVNKDWKKGDGGELRLYTNNPNNTNQKELKQTEEFIDIEPIADRLLIFLSPFLEHEVLQCNFEPRIAITTWIY |
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 169-284 | Fe2OG dioxygenase | ||||
Sequence: NFNSIKTQTQLAVYLNGGRYIKHRDSFYSSESLTISRRITMIYYVNKDWKKGDGGELRLYTNNPNNTNQKELKQTEEFIDIEPIADRLLIFLSPFLEHEVLQCNFEPRIAITTWIY |
Sequence similarities
Belongs to the P4HA family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length284
- Mass (Da)33,348
- Last updated2003-06-01 v1
- Checksum19AE1D748793D0E3
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY768817 EMBL· GenBank· DDBJ | AAV37458.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAFI02000022 EMBL· GenBank· DDBJ | EAL68553.1 EMBL· GenBank· DDBJ | Genomic DNA |