B0BNF9 · HAOX1_RAT
- Protein2-Hydroxyacid oxidase 1
- GeneHao1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids370 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Broad substrate specificity (S)-2-hydroxy-acid oxidase that preferentially oxidizes glycolate. The glyoxylate produced by the oxidation of glycolate can then be utilized by alanine-glyoxylate aminotransferase for the peroxisomal synthesis of glycine; this pathway appears to be an important step for the detoxification of glyoxylate which, if allowed to accumulate, may be metabolized to oxalate with formation of kidney stones. Can also catalyze the oxidation of glyoxylate, and long chain hydroxyacids such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate. Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP), but O2 is believed to be the physiological electron acceptor, leading to the production of H2O2.
Catalytic activity
- a (2S)-2-hydroxycarboxylate + O2 = a 2-oxocarboxylate + H2O2This reaction proceeds in the forward direction.
- 2-hydroxyhexadecanoate + O2 = 2-oxohexadecanoate + H2O2This reaction proceeds in the forward direction.
- 2-hydroxyoctanoate + O2 = 2-oxooctanoate + H2O2This reaction proceeds in the forward direction.
Cofactor
Pathway
Amino-acid biosynthesis; glycine biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 79-81 | FMN (UniProtKB | ChEBI) | ||||
Sequence: ATA | ||||||
Binding site | 108 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 130 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 132 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 158 | FMN (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 167 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 236 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 258 | FMN (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 260 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 260 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 263 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 291-295 | FMN (UniProtKB | ChEBI) | ||||
Sequence: DGGVR | ||||||
Binding site | 314-315 | FMN (UniProtKB | ChEBI) | ||||
Sequence: GR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisomal matrix | |
Cellular Component | peroxisome | |
Molecular Function | (S)-2-hydroxy-acid oxidase activity | |
Molecular Function | FMN binding | |
Molecular Function | glyoxylate oxidase activity | |
Biological Process | fatty acid alpha-oxidation | |
Biological Process | glycine biosynthetic process | |
Biological Process | glycolate catabolic process | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name2-Hydroxyacid oxidase 1
- EC number
- Short namesHAOX1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionB0BNF9
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000453972 | 1-370 | 2-Hydroxyacid oxidase 1 | |||
Sequence: MLPRLVCISDYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPPQLRMKNFETNDLAFSPKGNFGDNSGLAEYVAQAIDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNPLAVSKI | ||||||
Modified residue | 184 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 194 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 230 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-365 | FMN hydroxy acid dehydrogenase | ||||
Sequence: MLPRLVCISDYEQHARTVLQKSVYDYYKSGANDQETLADNIRAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPPQLRMKNFETNDLAFSPKGNFGDNSGLAEYVAQAIDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNPL | ||||||
Motif | 368-370 | Microbody targeting signal | ||||
Sequence: SKI |
Sequence similarities
Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length370
- Mass (Da)40,968
- Last updated2008-02-26 v1
- Checksum2CFD33AFCF9021B0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AABR07053812 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH473949 EMBL· GenBank· DDBJ | EDL80285.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC158804 EMBL· GenBank· DDBJ | AAI58805.1 EMBL· GenBank· DDBJ | mRNA |