Protein profile

KP13_32231

Formate dehydrogenase-O major subunit

Genome: KpKP13

Gene: AHE47083.1 fdoG Structure source: ColabFold UniProt A0A4S6I5T3
Amino acids 1016
Annotations 13
Features 40
PDB binders 10
Druggability 0.932

Overview

Basic information about this protein and its source genome.

Accession
KP13_32231
Gene
AHE47083.1 fdoG
Status
annotated
Amino acids
1016
Structure source
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
Periplasmic
ColabFold pLDDT
95.11

Selected Druggability evidence

ColabFold / curated model

Selected 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.

FPocket 0.932
Structure CB_KP13_32231
Pocket Pocket 1
P2Rank 0.923
Structure CB_KP13_32231
Pocket Pocket 1
ColabFold model
FPocket 0.932 · Pocket 1
P2Rank 0.923 · Pocket 1
Core conservation Accessory gene
Roary accessory
CoreCruncher accessory
Gut microbiome 144 / 4744 genomes with a hit
Normalized 0.03

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

13 GO

Gene Ontology (GO)

13
  • GO:0047111 Catalysis of the reaction: ferricytochrome C-553 + formate = ferrocytochrome C-553 + CO2.
  • GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
  • GO:0008863 Catalysis of the reaction: formate + NAD+ = CO2 + NADH.
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
  • GO:0009055 A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways.
  • GO:0045333 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which either requires oxygen (aerobic respiration) or does not (anaerobic respiration).
  • GO:0043546 Binding to a molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
  • GO:0009326 An enzyme complex that catalyzes the dehydrogenation of formate to produce carbon dioxide (CO2).
  • GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
  • GO:0036397 Catalysis of the reaction: formate + a quinone = CO2 + a quinol.
  • GO:0030151 Binding to a molybdenum ion (Mo).
  • GO:0009061 The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.
  • GO:0015944 The chemical reactions and pathways by which formate is converted to CO2.

Sequence Features

Domain/signature hits from InterPro and related databases.

40 records
Show feature table
Start End DB Term Name
887 1015 CDD cd02792 MopB_CT_Formate-Dh-Na-like
1 1015 PANTHER PTHR43598 TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B
517 682 FunFam G3DSA:3.40.50.740:FF:000007 Formate dehydrogenase, alpha subunit, selenocysteine-containing
841 1016 FunFam G3DSA:2.40.40.20:FF:000017 Formate dehydrogenase, alpha subunit
35 159 FunFam G3DSA:3.30.200.210:FF:000003 Formate dehydrogenase-N subunit alpha
25 33 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
841 1016 Gene3D G3DSA:2.40.40.20 -
1 33 SignalP_GRAM_POSITIVE SignalP-TM SignalP-TM
48 66 ProSitePatterns PS00551 Prokaryotic molybdopterin oxidoreductases signature 1.
48 66 InterPro IPR027467 Molybdopterin oxidoreductase, molybdopterin cofactor binding site
44 103 Pfam PF04879 Molybdopterin oxidoreductase Fe4S4 domain
44 103 InterPro IPR006963 Molybdopterin oxidoreductase, 4Fe-4S domain
43 104 SMART SM00926 Molybdop_Fe4S4_2
43 104 InterPro IPR006963 Molybdopterin oxidoreductase, 4Fe-4S domain
192 485 Gene3D G3DSA:3.40.228.10 Dimethylsulfoxide Reductase, domain 2
34 158 Gene3D G3DSA:3.30.200.210 -
528 682 Gene3D G3DSA:3.40.50.740 -
192 485 FunFam G3DSA:3.40.228.10:FF:000006 Formate dehydrogenase, alpha subunit, selenocysteine-containing
47 874 CDD cd02752 MopB_Formate-Dh-Na-like
34 1016 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1 10 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
1 33 Phobius SIGNAL_PEPTIDE Signal peptide region
928 955 ProSitePatterns PS00932 Prokaryotic molybdopterin oxidoreductases signature 3.
928 955 InterPro IPR006655 Molybdopterin oxidoreductase, prokaryotic, conserved site
691 840 FunFam G3DSA:3.40.228.10:FF:000011 Formate dehydrogenase-N subunit alpha
894 1009 Pfam PF01568 Molydopterin dinucleotide binding domain
894 1009 InterPro IPR006657 Molybdopterin dinucleotide-binding domain
43 106 ProSiteProfiles PS51669 Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain profile.
43 106 InterPro IPR006963 Molybdopterin oxidoreductase, 4Fe-4S domain
11 24 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
2 1015 NCBIfam TIGR01553 formate dehydrogenase-N subunit alpha
2 1015 InterPro IPR006443 Formate dehydrogenase-N, alpha subunit
1 33 ProSiteProfiles PS51318 Twin arginine translocation (Tat) signal profile.
1 33 InterPro IPR006311 Twin-arginine translocation pathway, signal sequence
35 851 SUPERFAMILY SSF53706 Formate dehydrogenase/DMSO reductase, domains 1-3
107 589 Pfam PF00384 Molybdopterin oxidoreductase
107 589 InterPro IPR006656 Molybdopterin oxidoreductase
744 840 Gene3D G3DSA:3.40.228.10 Dimethylsulfoxide Reductase, domain 2
830 1016 SUPERFAMILY SSF50692 ADC-like
830 1016 InterPro IPR009010 Aspartate decarboxylase-like domain superfamily

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
ColabFold KP13_32231
ColabFold full sequence Viewing
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 0.932
31 0.825
4 0.306

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 12.27 0.645
2 9.18 0.492
3 8.94 0.479
4 8.22 0.438
5 7.69 0.406

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

60 records

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
2MD Q934F5 742.6 Da LogP -2.53 TPSA 346.6 3 viol. ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…
4MO P07658 95.9 Da LogP -0.00 TPSA 0.0 ✓ Ro5 ✓ Clean [Mo+4]
6MO D5AQH0 95.9 Da LogP -0.00 TPSA 0.0 ✓ Ro5 ✓ Clean [Mo+6]
CDL P24183 1464.1 Da LogP 23.31 TPSA 242.6 3 viol. ✓ Clean CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)([O-])OCC(…
FES D5AQH0 175.8 Da LogP 1.29 TPSA 0.0 ✓ Ro5 ✓ Clean S1[Fe]S[Fe]1
H2S Q72EJ1 34.1 Da LogP 0.11 TPSA 0.0 ✓ Ro5 ✓ Clean S
HQO P24183 259.3 Da LogP 3.69 TPSA 47.2 ✓ Ro5 Alert CCCCCCCc1cc(c2ccccc2[n+]1[O-])O
MGD Q72EJ1 740.6 Da LogP -2.06 TPSA 346.6 3 viol. ✓ Clean c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=…
NO2 P07658 46.0 Da LogP 0.25 TPSA 52.5 ✓ Ro5 ✓ Clean N(=O)[O-]
W Q72EJ1 183.8 Da LogP -0.00 TPSA 0.0 ✓ Ro5 ✓ Clean [W+6]

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.