Q0P5I5 (HOGA1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 50.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable 4-hydroxy-2-oxoglutarate aldolase, mitochondrial EC=4.1.3.16 Alternative name(s): Dihydrodipicolinate synthase-like Short name=DHDPS-like protein Probable 2-keto-4-hydroxyglutarate aldolase Short name=Probable KHG-aldolase | ||||
| Gene names |
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| Organism | Bos taurus (Bovine) [Reference proteome] | ||||
| Taxonomic identifier | 9913 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 327 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the final step in the metabolic pathway of hydroxyproline By similarity. |
| Catalytic activity | 4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate. |
| Enzyme regulation | Inhibited by divalent cations. |
| Subunit structure | Homotetramer. Ref.3 |
| Subcellular location | Mitochondrion By similarity. |
| Sequence similarities | Belongs to the DapA family. |
| Biophysicochemical properties | Kinetic parameters: KM=26 µM for DL-4-hydroxy-2-oxoglutarate Ref.3 Vmax=10.7 µmol/min/mg enzyme pH dependence: Optimum pH is 8.8. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Schiff base |
| Molecular function | Lyase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | 4-hydroxyproline catabolic process Inferred from electronic annotation. Source: Compara glyoxylate catabolic processInferred from direct assay Ref.3. Source: UniProtKB oxalate metabolic processInferred from electronic annotation. Source: Compara pyruvate biosynthetic processInferred from electronic annotation. Source: Compara |
| Cellular_component | mitochondrion Inferred from direct assay PubMed 21998747. Source: BHF-UCL |
| Molecular_function | 4-hydroxy-2-oxoglutarate aldolase activity Inferred from direct assay Ref.3. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 25 | 25 | Mitochondrion Potential | ||||||
| Chain | 26 – 327 | 302 | Probable 4-hydroxy-2-oxoglutarate aldolase, mitochondrial | PRO_0000273345 | |||||
Regions | |||||||||
| Region | 77 – 78 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 196 | 1 | Schiff-base intermediate with substrate By similarity | ||||||
| Site | 168 | 1 | Involved in proton transfer during cleavage By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 327 | 1 | L → F in ABH06334. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal liver. |
| [3] | "2-Keto-4-hydroxyglutarate aldolase: purification and characterization of the homogeneous enzyme from bovine kidney." Dekker E.E., Kitson R.P. J. Biol. Chem. 267:10507-10514(1992) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES. |
| [4] | "Mutations in DHDPSL are responsible for primary hyperoxaluria type III." Belostotsky R., Seboun E., Idelson G.H., Milliner D.S., Becker-Cohen R., Rinat C., Monico C.G., Feinstein S., Ben-Shalom E., Magen D., Weissman I., Charon C., Frishberg Y. Am. J. Hum. Genet. 87:392-399(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BT026547 mRNA. Translation: ABH06334.1. BC119998 mRNA. Translation: AAI19999.1. |
| IPI | IPI00788592. |
| RefSeq | NP_001068705.1. NM_001075237.1. |
| UniGene | Bt.54337. |
3D structure databases | |
| ProteinModelPortal | Q0P5I5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9913.ENSBTAP00000016909. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000016909; ENSBTAP00000016909; ENSBTAG00000012721. |
| GeneID | 506001. |
| KEGG | bta:506001. |
Organism-specific databases | |
| CTD | 112817. |
Phylogenomic databases | |
| eggNOG | COG0329. |
| GeneTree | ENSGT00530000063604. |
| HOVERGEN | HBG081405. |
| InParanoid | Q0P5I5. |
| OMA | GCESTRA. |
| OrthoDB | EOG4NGGNF. |
Enzyme and pathway databases | |
| BioCyc | CATTLE:506001-MONOMER. |
Family and domain databases | |
| Gene3D | 3.20.20.70. 1 hit. |
| InterPro | IPR013785. Aldolase_TIM. IPR002220. Dihydrodipicolinate_synth-like. IPR020625. Dihydrodipicolinate_synth_AS. [Graphical view] |
| PANTHER | PTHR12128. PTHR12128. 1 hit. |
| Pfam | PF00701. DHDPS. 1 hit. [Graphical view] |
| PIRSF | PIRSF001365. DHDPS. 1 hit. |
| PRINTS | PR00146. DHPICSNTHASE. |
| PROSITE | PS00665. DHDPS_1. False negative. PS00666. DHDPS_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20867406. |
Entry information
| Entry name | HOGA1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q0P5I5 Secondary accession number(s): Q0V7M3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
