B0TKZ7
Gene name |
pdxB |
Protein name |
Erythronate-4-phosphate dehydrogenase |
Names |
|
Species |
Shewanella halifaxensis (strain HAW-EB4) |
KEGG Pathway |
shl:Shal_2644 |
EC number |
1.1.1.290: With NAD(+) or NADP(+) as acceptor |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for B0TKZ7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B0TKZ7-F1 | Predicted | AlphaFoldDB |
No variants for B0TKZ7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B0TKZ7 | |||||
No associated diseases with B0TKZ7
4 regional properties for B0TKZ7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain | 9 - 277 | IPR006139 |
| domain | D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain | 113 - 257 | IPR006140 |
| domain | Erythronate-4-phosphate dehydrogenase, dimerisation domain | 290 - 370 | IPR024531 |
| conserved_site | D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain conserved site | 198 - 214 | IPR029753 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.1.1.290 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4-phosphoerythronate dehydrogenase activity | Catalysis of the reaction: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + H(+) + NADH. |
| NAD binding | Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. |
| protein dimerization activity | The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| pyridoxine biosynthetic process | The chemical reactions and pathways resulting in the formation of pyridoxine, 2-methyl-3-hydroxy-4,5-bis(hydroxymethyl)pyridine, one of the vitamin B6 compounds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKILADENMP | YVQQLFGDLG | TIETVNGREL | TPEQVKDADV | LLVRSVTKVD | QALLAENNRL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KFVGSATIGT | DHIDLDYLAS | HNIPFSNAPG | CNATAVGEFA | FIAMLELAQR | FNSPLKGKVV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GIVGAGNTGT | AVVKCLEAYG | IEVLLNDPLL | EQSGDPRDFV | SLDTLIEKCD | VISLHVPITK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TGEHKTWYLF | DEQRLNSLAE | NTWLVNCCRG | EVIDNRALIK | FKQQRDDVKV | VLDVWEGEPN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PMPELVPYVE | FCTPHIAGYS | LEGKARGTYI | LYQKLAEVLQ | ISADKQMESL | LPALWSERVL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VQEISDERAL | LQLARFVYDL | RDDDELFRKQ | FLNNQGFDHM | RKNHTHRREF | SALKVGNTGQ |
| 370 | |||||
| TNVNWLSNLG | FSGVEL |