Overview
Basic information about this protein and its source genome.
- Accession
- VK055_4953
- Gene
- AIK83479.1
- Status
- annotated
- Amino acids
- 581
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- DEG identity (%)
- 0.0
- Localization
- CytoplasmicMembrane
- ColabFold pLDDT
- 92.95
Selected Druggability evidence
AlphaFold / UniProt modelSelected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
13- GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
- GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
- GO:0016901 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces a quinone or a similar acceptor molecule.
- GO:0019516 OBSOLETE. The chemical reactions and pathways resulting in the conversion of lactate to other compounds, such as pyruvate, with concomitant loss of electrons.
- GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
- GO:0022904 A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
- GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
- GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
- GO:0006089 The chemical reactions and pathways involving lactate, the anion of lactic acid.
- GO:0031234 The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region.
- GO:0004458 Catalysis of the reaction: (R)-lactate + 2 [Fe(III)cytochrome c] = 2 [Fe(II)cytochrome c] + 2 H+ + pyruvate.
- GO:0102029 Catalysis of the reaction: (R)-lactate + an ubiquinone = pyruvate + an ubiquinol.
- GO:0048038 Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 269 | 353 | FunFam | G3DSA:3.30.70.610:FF:000001 | Quinone-dependent D-lactate dehydrogenase |
| 276 | 567 | SUPERFAMILY | SSF55103 | FAD-linked oxidases, C-terminal domain |
| 276 | 567 | InterPro | IPR016164 | FAD-linked oxidase-like, C-terminal |
| 106 | 268 | FunFam | G3DSA:3.30.465.10:FF:000015 | Quinone-dependent D-lactate dehydrogenase |
| 435 | 519 | Gene3D | G3DSA:3.30.1370.20 | - |
| 435 | 519 | InterPro | IPR016173 | D-lactate dehydrogenase, cap domain, subdomain 2 |
| 435 | 519 | FunFam | G3DSA:3.30.1370.20:FF:000001 | Quinone-dependent D-lactate dehydrogenase |
| 547 | 581 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 278 | 567 | Pfam | PF09330 | D-lactate dehydrogenase, membrane binding |
| 278 | 567 | InterPro | IPR015409 | D-lactate dehydrogenase, membrane binding, C-terminal |
| 10 | 271 | SUPERFAMILY | SSF56176 | FAD-binding/transporter-associated domain-like |
| 10 | 271 | InterPro | IPR036318 | FAD-binding, type PCMH-like superfamily |
| 1 | 103 | Gene3D | G3DSA:3.30.43.10 | - |
| 1 | 103 | InterPro | IPR016167 | FAD-binding, type PCMH, subdomain 1 |
| 355 | 434 | FunFam | G3DSA:3.30.70.610:FF:000002 | Quinone-dependent D-lactate dehydrogenase |
| 47 | 168 | Pfam | PF01565 | FAD binding domain |
| 47 | 168 | InterPro | IPR006094 | FAD linked oxidase, N-terminal |
| 4 | 569 | PIRSF | PIRSF000101 | D-lactate_dh |
| 4 | 569 | InterPro | IPR012256 | D-lactate dehydrogenase |
| 106 | 268 | Gene3D | G3DSA:3.30.465.10 | - |
| 106 | 268 | InterPro | IPR016169 | FAD-binding, type PCMH, subdomain 2 |
| 269 | 352 | Gene3D | G3DSA:3.30.70.610 | - |
| 269 | 352 | InterPro | IPR016172 | D-lactate dehydrogenase, cap domain, subdomain 1 |
| 353 | 434 | Gene3D | G3DSA:3.30.70.610 | - |
| 353 | 434 | InterPro | IPR016172 | D-lactate dehydrogenase, cap domain, subdomain 1 |
| 42 | 272 | ProSiteProfiles | PS51387 | PCMH-type FAD-binding domain profile. |
| 42 | 272 | InterPro | IPR016166 | FAD-binding domain, PCMH-type |
| 2 | 103 | FunFam | G3DSA:3.30.43.10:FF:000005 | Quinone-dependent D-lactate dehydrogenase |
| 9 | 557 | PANTHER | PTHR43716 | D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL |
| 10 | 568 | Hamap | MF_02092 | Quinone-dependent D-lactate dehydrogenase [dld]. |
| 10 | 568 | InterPro | IPR012256 | D-lactate dehydrogenase |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GW01
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
VK055_4953
|
ColabFold | — | — | full sequence | — | Loaded |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 1 | 0.995 | ||||||
| 13 | 0.655 | ||||||
| 16 | 0.233 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 70.68 | 0.991 | ||||||
| 2 | 1.17 | 0.009 |
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 6 | 0.937 | ||||||
| 38 | 0.59 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 60.95 | 0.988 | ||||||
| 2 | 10.35 | 0.556 | ||||||
| 3 | 0.82 | 0.003 |