Overview
| Uniprot ID | Q9BUT1 |
|---|
| Protein Name | Dehydrogenase/reductase SDR family member 6 |
|---|
| Gene Name | BDH2 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 63 |
VLDVTKKKQIDQFAN |
Function
NAD(H)-dependent dehydrogenase/reductase with a preference for cyclic substrates (By similarity) (PubMed:35150746). Catalyzes stereoselective conversion of 4-oxo-L-proline to cis-4-hydroxy-L-proline, likely a detoxification mechanism for ketoprolines (PubMed:35150746). Mediates the formation of 2,5-dihydroxybenzoate (2,5-DHBA), a siderophore that chelates free cytoplasmic iron and associates with LCN2, thereby regulating iron transport and homeostasis while protecting cells against free radical-induced oxidative stress. The iron-siderophore complex is imported into mitochondria, providing an iron source for mitochondrial metabolic processes in particular heme synthesis (By similarity). May act as a 3-hydroxybutyrate dehydrogenase (PubMed:16380372)
Protein Sequence
10
MGRLDGKVII
20
LTAAAQGIGQ
30
AAALAFAREG
40
AKVIATDINE
50
SKLQELEKYP
60
GIQTRVLDVT
70
KKKQIDQFAN
80
EVERLDVLFN
90
VAGFVHHGTV
100
LDCEEKDWDF
110
SMNLNVRSMY
120
LMIKAFLPKM
130
LAQKSGNIIN
140
MSSVASSVKG
150
VVNRCVYSTT
160
KAAVIGLTKS
170
VAADFIQQGI
180
RCNCVCPGTV
190
DTPSLQERIQ
200
ARGNPEEARN
210
DFLKRQKTGR
220
FATAEEIAML
230
CVYLASDESA
240
YVTGNPVIID
GGWSL
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0070062 |
extracellular exosome |
| Molecular Function |
GO:0003858 |
3-hydroxybutyrate dehydrogenase activity |
| Molecular Function |
GO:0016617 |
4-oxoproline reductase activity |
| Molecular Function |
GO:0051287 |
NAD binding |
| Molecular Function |
GO:0016628 |
oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| Biological Process |
GO:0030855 |
epithelial cell differentiation |
| Biological Process |
GO:0006635 |
fatty acid beta-oxidation |
| Biological Process |
GO:0042168 |
heme metabolic process |
| Biological Process |
GO:0019290 |
siderophore biosynthetic process |
| Cellular Component |
GO:0005829 |
cytosol |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.