Record Information
Version2.0
Creation Date2012-05-31 10:21:46 -0600
Update Date2015-09-13 12:56:06 -0600
Secondary Accession Numbers
  • ECMDB00142
Identification
Name:Formic acid
Description:Formic acid is the simplest carboxylic acid. Formate is an intermediate in normal metabolism. It takes part in the metabolism of one-carbon compounds and its carbon may appear in methyl groups undergoing transmethylation. It is eventually oxidized to carbon dioxide. In nature, formic acid is found in the stings and bites of many insects of the order Hymenoptera, including bees and ants. The principal use of formic acid is as a preservative and antibacterial agent in livestock feed. When sprayed on fresh hay or other silage, it arrests certain decay processes and causes the feed to retain its nutritive value longer.
Structure
Thumb
Synonyms:
  • Add-F
  • Ameisensaure
  • Aminate
  • Aminic acid
  • Bilorin
  • Collo-Bueglatt
  • Collo-Didax
  • Formate
  • Formic acid
  • Formira
  • Formisoton
  • Formylate
  • Formylic acid
  • Hydrogen carboxylate
  • Hydrogen carboxylic acid
  • Methanoate
  • Methanoate monomer
  • Methanoic acid
  • Methanoic acid monomer
  • Myrmicyl
  • Sodium Formate
  • Sodium Formic acid
  • Sybest
  • Wonderbond Hardener M 600L
Chemical Formula:CH2O2
Weight:Average: 46.0254
Monoisotopic: 46.005479308
InChI Key:BDAGIHXWWSANSR-UHFFFAOYSA-N
InChI:InChI=1S/CH2O2/c2-1-3/h1H,(H,2,3)
CAS number:64-18-6
IUPAC Name:formic acid
Traditional IUPAC Name:formic acid
SMILES:OC=O
Chemical Taxonomy
DescriptionThis compound belongs to the class of organic compounds known as carboxylic acids. These are compounds containing a carboxylic acid group with the formula -C(=O)OH.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassCarboxylic acids
Direct ParentCarboxylic acids
Alternative Parents
Substituents
  • Monocarboxylic acid or derivatives
  • Carboxylic acid
  • Organic oxygen compound
  • Organic oxide
  • Hydrocarbon derivative
  • Organooxygen compound
  • Carbonyl group
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
State:Liquid
Charge:-1
Melting point:8.4 °C
Experimental Properties:
PropertyValueSource
Water Solubility:1000.0 mg/mL [RIDDICK,JA et al. (1986)]PhysProp
LogP:-0.54 [HANSCH,C ET AL. (1995)]PhysProp
Predicted Properties
PropertyValueSource
Water Solubility477.0 mg/mLALOGPS
logP-0.47ALOGPS
logP-0.27ChemAxon
logS1.02ALOGPS
pKa (Strongest Acidic)4.27ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count2ChemAxon
Hydrogen Donor Count1ChemAxon
Polar Surface Area37.3 Å2ChemAxon
Rotatable Bond Count0ChemAxon
Refractivity8.15 m3·mol-1ChemAxon
Polarizability3.37 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
2-Ketobutyric acid + Coenzyme A > Formic acid + Propionyl-CoA
Coenzyme A + Pyruvic acid <> Acetyl-CoA + Formic acid
2 Hydrogen ion + Menaquinone 8 + Formic acid > Menaquinol 8 + Carbon dioxide + Hydrogen ion
2 Hydrogen ion + Ubiquinone-8 + Formic acid > Ubiquinol-8 + Carbon dioxide + Hydrogen ion
Formic acid + Hydrogen ion > Carbon dioxide + Hydrogen (gas)
S-Formylglutathione + Water <> Formic acid + Glutathione + Hydrogen ion
N10-Formyl-THF + Water <> Formic acid + Hydrogen ion + Tetrahydrofolic acid
Guanosine triphosphate + 3 Water <> 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Formic acid +2 Hydrogen ion + Pyrophosphate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine
Adenosine triphosphate + Formic acid + Glycineamideribotide > ADP + 5'-Phosphoribosyl-N-formylglycineamide + Hydrogen ion + Phosphate
Guanosine triphosphate + Water > Dihydroneopterin triphosphate + Formic acid + Hydrogen ion
Water + Undecaprenyl phosphate-4-amino-4-formyl-L-arabinose > Formic acid + undecaprenyl phosphate-4-amino-4-deoxy-L-arabinose
Formyl-CoA + Oxalic acid <> Formic acid + Oxalyl-CoA
D-Ribulose 5-phosphate <> 3,4-Dihydroxy-2-butanone-4-P + Formic acid + Hydrogen ion
5-Aminoimidazole ribonucleotide + Water + NAD > 4-Amino-2-methyl-5-phosphomethylpyrimidine +2 Formic acid +3 Hydrogen ion + NADH
Acetyl-CoA + Formic acid <> Coenzyme A + Pyruvic acid
Guanosine triphosphate + 3 Water <> Formic acid + 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Pyrophosphate
Formic acid + NAD <> Hydrogen ion + Carbon dioxide + NADH
S-Formylglutathione + Water <> Formic acid + Glutathione
N10-Formyl-THF + Water <> Formic acid + Tetrahydrofolic acid
4-Amino-5-hydroxymethyl-2-methylpyrimidine + S-Adenosylmethionine <> 5-Aminoimidazole ribonucleotide + 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + CO
Formamidopyrimidine nucleoside triphosphate + Water <> 2,5-Diaminopyrimidine nucleoside triphosphate + Formic acid
2-Ketobutyric acid + Coenzyme A <> Propionyl-CoA + Formic acid
D-Ribulose 5-phosphate <> 3,4-Dihydroxy-2-butanone-4-P + Formic acid
Hydrogen ion + Formic acid > Carbon dioxide + Hydrogen (gas)
4-deoxy-4-formamido-&alpha;-L-arabinopyranosyl <i>ditrans,octacis</i>-undecaprenyl phosphate + Water > 4-amino-4-deoxy-&alpha;-L-arabinopyranosyl <i>ditrans,octacis</i>-undecaprenyl phosphate + Formic acid
Water + formyl-L-methionyl peptide > Hydrogen ion + methionyl peptide + Formic acid
D-Ribulose 5-phosphate > Hydrogen ion + 3,4-Dihydroxy-2-butanone-4-P + Formic acid
Formic acid + Hydrogen ion + a menaquinone > Hydrogen ion + Carbon dioxide + a menaquinol
Adenosine triphosphate + Formic acid + Tetrahydrofolic acid > ADP + Phosphate + N10-Formyl-THF
Water + N10-Formyl-THF > Hydrogen ion + Tetrahydrofolic acid + Formic acid
Glycineamideribotide + Formic acid + Adenosine triphosphate > Hydrogen ion + Phosphate + 5'-Phosphoribosyl-N-formylglycineamide + ADP
Guanosine triphosphate + Water > Hydrogen ion + Formic acid + Dihydroneopterin triphosphate
Water + Guanosine triphosphate > Hydrogen ion + Pyrophosphate + 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Formic acid
2-Ketobutyric acid + Coenzyme A > Propionyl-CoA + Formic acid
5-Aminoimidazole ribonucleotide + S-Adenosylmethionine 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + carbon monoxide + Hydrogen ion
Formic acid + Acetyl-CoA <> Pyruvic acid + Coenzyme A
Formyl-CoA + Oxalic acid Formic acid + Oxalyl-CoA
Formic acid + an oxidized electron acceptor + Hydrogen ion > Carbon dioxide + a reduced electron acceptor
S-Formylglutathione + Water > Hydrogen ion + Formic acid + Glutathione
4-deoxy-4-formamido-beta-L-arabinose di-trans,poly-cis-undecaprenyl phosphate + Water > 4-amino-4-deoxy-alpha-L-arabinose di-trans,poly-cis-undecaprenyl phosphate + Formic acid
Formyl-L-methionyl peptide + Water > Formic acid + methionyl peptide
Formyl-CoA + Oxalic acid > Formic acid + Oxalyl-CoA
Formic acid + NAD > Carbon dioxide + NADH
Formic acid + acceptor > Carbon dioxide + reduced acceptor
Formic acid + NAD > Carbon dioxide + NADH
Formic acid + NAD > Carbon dioxide + NADH
Guanosine triphosphate + Water > Formic acid + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Acetyl-CoA + Formic acid > CoA + Pyruvic acid
Acetyl-CoA + Formic acid > CoA + Pyruvic acid
Acetyl-CoA + Formic acid > CoA + Pyruvic acid
Formic acid + Adenosine triphosphate + 5'-Phospho-ribosylglycinamide > 5'-Phosphoribosyl-N-formylglycineamide + ADP + Pyrophosphate
N10-Formyl-THF + Water > Formic acid + Tetrahydrofolic acid
Guanosine triphosphate + 3 Water > Formic acid + 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Pyrophosphate
D-Ribulose 5-phosphate > Formic acid + 1-Deoxy-L-glycero-tetrulose 4-phosphate
S-Formylglutathione + Water > Glutathione + Formic acid
S-Formylglutathione + Water > Glutathione + Formic acid
Propionyl-CoA + Formic acid > CoA + 2-Ketobutyric acid
Acetyl-CoA + Formic acid > CoA + Pyruvic acid
5-Aminoimidazole ribonucleotide + S-adenosyl-L-methionine > 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + CO
Formic acid + Quinone <> Carbon dioxide + Hydroquinone
Formyl-L-methionyl peptide + Water <> Formic acid + Methionyl peptide
Guanosine triphosphate + Water <> Formic acid + Dihydroneopterin triphosphate
Formyl-CoA + Oxalic acid <> Formic acid + Oxalyl-CoA
N1-(5-phospho-β-D-ribosyl)glycinamide + Adenosine triphosphate + Formic acid > 5'-Phosphoribosyl-N-formylglycinamide + Adenosine diphosphate + Phosphate + Hydrogen ion + 5'-Phosphoribosyl-N-formylglycineamide + ADP
Formic acid + Tetrahydrofolic acid + Tetrahydrofolic acid > Water + 10-Formyltetrahydrofolate + N10-Formyl-THF
Guanosine triphosphate + Water > Formic acid + Hydrogen ion + 7,8-dihydroneopterin 3'-triphosphate
2-Ketobutyric acid + Coenzyme A > Formic acid + Propionyl-CoA + Propionyl-CoA
D-Ribulose 5-phosphate > 1-Deoxy-L-glycero-tetrulose 4-phosphate + Formic acid + Hydrogen ion
Formic acid + menaquinone-8 + Electron + Hydrogen ion > Carbon dioxide + Hydrogen ion + Menaquinol 8
Guanosine triphosphate + 3 Water > Formic acid + Pyrophosphate +2 Hydrogen ion + 2,5-Diamino-6-(5'-phosphoribosylamino)-4-pyrimidineone
Guanosine triphosphate + Water > 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Hydrogen ion + Formic acid + Pyrophosphate
D-Ribulose 5-phosphate > Formic acid + Hydrogen ion + 1-Deoxy-L-glycero-tetrulose 4-phosphate
5-Aminoimidazole ribonucleotide + S-adenosyl-L-methionine >3 Hydrogen ion + CO + Formic acid + L-Methionine + 5'-Deoxyadenosine + 4-amino-2-methyl-5-phosphomethylpyrimidine
More...

SMPDB Pathways:
Flavin biosynthesisPW001971 Pw001971Pw001971 greyscalePw001971 simple
Folate biosynthesisPW000908 Pw000908Pw000908 greyscalePw000908 simple
GTP degradationPW001888 Pw001888Pw001888 greyscalePw001888 simple
N-oxide electron transferPW001889 Pw001889Pw001889 greyscalePw001889 simple
Nitrogen metabolismPW000755 Pw000755Pw000755 greyscalePw000755 simple
One Carbon Pool by Folate IPW001735 Pw001735Pw001735 greyscalePw001735 simple
One carbon pool by folatePW000773 Pw000773Pw000773 greyscalePw000773 simple
Propanoate metabolismPW000940 Pw000940Pw000940 greyscalePw000940 simple
Tetrahydromonapterin BiosynthesisPW002043 Pw002043Pw002043 greyscalePw002043 simple
Thiamin diphosphate biosynthesisPW002028 Pw002028Pw002028 greyscalePw002028 simple
dimethyl sulfoxide electron transferPW001892 Pw001892Pw001892 greyscalePw001892 simple
polymyxin resistancePW002052 Pw002052Pw002052 greyscalePw002052 simple
preQ0 metabolismPW001893 Pw001893Pw001893 greyscalePw001893 simple
purine nucleotides de novo biosynthesisPW000910 Pw000910Pw000910 greyscalePw000910 simple
purine nucleotides de novo biosynthesis 1435709748PW000960 Pw000960Pw000960 greyscalePw000960 simple
purine nucleotides de novo biosynthesis 2PW002033 Pw002033Pw002033 greyscalePw002033 simple
KEGG Pathways:
EcoCyc Pathways:
Concentrations
ConcentrationStrainMediaGrowth StatusGrowth SystemTemperatureDetails
184± 25 uMBL21 DE3Luria-Bertani (LB) mediaStationary phase cultures (overnight culture)Shake flask37 oCExperimentally Determined
Download Details
Find out more about how we convert literature concentrations.
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
GC-MSGC-MS Spectrum - GC-MSsplash10-0002-9000000000-5d27bb312e37a2c8994fView in MoNA
GC-MSGC-MS Spectrum - GC-MS (1 TMS)splash10-0fmi-9200000000-2a89ba98485194acd75aView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0002-9000000000-092f816e62c8d2f5d56eView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0002-9000000000-092f816e62c8d2f5d56eView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0002-9000000000-092f816e62c8d2f5d56eView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0006-9000000000-eb2207f7400e9144fff7View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0006-9000000000-eb2207f7400e9144fff7View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0006-9000000000-eb2207f7400e9144fff7View in MoNA
MSMass Spectrum (Electron Ionization)splash10-004j-9000000000-2e63b0c1e2e417b0d747View in MoNA
1D NMR1H NMR SpectrumNot Available
1D NMR13C NMR SpectrumNot Available
1D NMR1H NMR SpectrumNot Available
1D NMR13C NMR SpectrumNot Available
1D NMR1H NMR SpectrumNot Available
1D NMR13C NMR SpectrumNot Available
2D NMR[1H,1H] 2D NMR SpectrumNot Available
2D NMR[1H,13C] 2D NMR SpectrumNot Available
References
References:
  • Bales JR, Higham DP, Howe I, Nicholson JK, Sadler PJ: Use of high-resolution proton nuclear magnetic resonance spectroscopy for rapid multi-component analysis of urine. Clin Chem. 1984 Mar;30(3):426-32. Pubmed: 6321058
  • Baumann K, Angerer J: Occupational chronic exposure to organic solvents. VI. Formic acid concentration in blood and urine as an indicator of methanol exposure. Int Arch Occup Environ Health. 1979 Jan 15;42(3-4):241-9. Pubmed: 422265
  • Berode M, Sethre T, Laubli T, Savolainen H: Urinary methanol and formic acid as indicators of occupational exposure to methyl formate. Int Arch Occup Environ Health. 2000 Aug;73(6):410-4. Pubmed: 11007345
  • Bloomer JC, Clarke SE, Chenery RJ: Determination of P4501A2 activity in human liver microsomes using [3-14C-methyl]caffeine. Xenobiotica. 1995 Sep;25(9):917-27. Pubmed: 8553685
  • D'Andrea MR, Reiser PA, Polkovitch DA, Gumula NA, Branchide B, Hertzog BM, Schmidheiser D, Belkowski S, Gastard MC, Andrade-Gordon P: The use of formic acid to embellish amyloid plaque detection in Alzheimer's disease tissues misguides key observations. Neurosci Lett. 2003 May 15;342(1-2):114-8. Pubmed: 12727331
  • Dal Pra I, Chiarini A, Boschi A, Freddi G, Armato U: Novel dermo-epidermal equivalents on silk fibroin-based formic acid-crosslinked three-dimensional nonwoven devices with prospective applications in human tissue engineering/regeneration/repair. Int J Mol Med. 2006 Aug;18(2):241-7. Pubmed: 16820930
  • Dunne VG, Bhattachayya S, Besser M, Rae C, Griffin JL: Metabolites from cerebrospinal fluid in aneurysmal subarachnoid haemorrhage correlate with vasospasm and clinical outcome: a pattern-recognition 1H NMR study. NMR Biomed. 2005 Feb;18(1):24-33. Pubmed: 15455468
  • Ferrari LA, Arado MG, Nardo CA, Giannuzzi L: Post-mortem analysis of formic acid disposition in acute methanol intoxication. Forensic Sci Int. 2003 Apr 23;133(1-2):152-8. Pubmed: 12742704
  • Ferry DG, Temple WA, McQueen EG: Methanol monitoring. Comparison of urinary methanol concentration with formic acid excretion rate as a measure of occupational exposure. Int Arch Occup Environ Health. 1980;47(2):155-63. Pubmed: 7440001
  • Foulon V, Sniekers M, Huysmans E, Asselberghs S, Mahieu V, Mannaerts GP, Van Veldhoven PP, Casteels M: Breakdown of 2-hydroxylated straight chain fatty acids via peroxisomal 2-hydroxyphytanoyl-CoA lyase: a revised pathway for the alpha-oxidation of straight chain fatty acids. J Biol Chem. 2005 Mar 18;280(11):9802-12. Epub 2005 Jan 11. Pubmed: 15644336
  • Grady S, Osterloh J: Improved enzymic assay for serum formate with colorimetric endpoint. J Anal Toxicol. 1986 Jan-Feb;10(1):1-5. Pubmed: 3754027
  • Igeta Y, Kawarabayashi T, Sato M, Yamada N, Matsubara E, Ishiguro K, Kanai M, Tomidokoro Y, Osuga J, Okamoto K, Hirai S, Shoji M: Apolipoprotein E accumulates with the progression of A beta deposition in transgenic mice. J Neuropathol Exp Neurol. 1997 Nov;56(11):1228-35. Pubmed: 9370233
  • Iwamoto N, Nishiyama E, Ohwada J, Arai H: Distribution of amyloid deposits in the cerebral white matter of the Alzheimer's disease brain: relationship to blood vessels. Acta Neuropathol (Berl). 1997 Apr;93(4):334-40. Pubmed: 9113198
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • Kerns W 2nd, Tomaszewski C, McMartin K, Ford M, Brent J: Formate kinetics in methanol poisoning. J Toxicol Clin Toxicol. 2002;40(2):137-43. Pubmed: 12126185
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • Lehmann P, Kligman AM: In vivo removal of the horny layer with formic acid. Br J Dermatol. 1983 Sep;109(3):313-20. Pubmed: 6615718
  • Nagasawa H, Wada M, Koyama S, Kawanami T, Kurita K, Kato T: [A case of methanol intoxication with optic neuropathy visualized on STIR sequence of MR images] Rinsho Shinkeigaku. 2005 Jul;45(7):527-30. Pubmed: 16119839
  • Nicholson JK, Foxall PJ, Spraul M, Farrant RD, Lindon JC: 750 MHz 1H and 1H-13C NMR spectroscopy of human blood plasma. Anal Chem. 1995 Mar 1;67(5):793-811. Pubmed: 7762816
  • Ohmori S, Sumii I, Toyonaga Y, Nakata K, Kawase M: High-performance liquid chromatographic determination of formate as benzimidazole in biological samples. J Chromatogr. 1988 Apr 8;426(1):15-24. Pubmed: 3384868
  • Tasaka Y, Nakaya F, Matsumoto H, Iwamoto Y, Omori Y: Pancreatic amylin content in human diabetic subjects and its relation to diabetes. Pancreas. 1995 Oct;11(3):303-8. Pubmed: 8577686
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
  • Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. Pubmed: 18331064
Synthesis Reference: Finholt, Albert E.; Jacobson, Eugene C. The reduction of carbon dioxide to formic acid with lithium aluminum hydride. Journal of the American Chemical Society (1952), 74 3943-4.
Material Safety Data Sheet (MSDS)Download (PDF)
External Links:
ResourceLink
CHEBI ID15740
HMDB IDHMDB00142
Pubchem Compound ID284
Kegg IDC00058
ChemSpider ID278
WikipediaFormic acid
BioCyc IDFORMATE
EcoCyc IDFORMATE
Ligand ExpoFMT

Enzymes

General function:
Involved in formate dehydrogenase (NAD+) activity
Specific function:
Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors
Gene Name:
fdhF
Uniprot ID:
P07658
Molecular weight:
79373
Reactions
Formate + NAD(+) = CO(2) + NADH.
General function:
Involved in formate C-acetyltransferase activity
Specific function:
Acetyl-CoA + formate = CoA + pyruvate
Gene Name:
pflB
Uniprot ID:
P09373
Molecular weight:
85357
Reactions
Acetyl-CoA + formate = CoA + pyruvate.
General function:
Involved in iron ion binding
Specific function:
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions
Gene Name:
def
Uniprot ID:
P0A6K3
Molecular weight:
19328
Reactions
Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide.
General function:
Involved in GTP cyclohydrolase I activity
Specific function:
GTP + H(2)O = formate + 2-amino-4-hydroxy-6- (erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Gene Name:
folE
Uniprot ID:
P0A6T5
Molecular weight:
24830
Reactions
GTP + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.
General function:
Involved in GTP cyclohydrolase II activity
Specific function:
Catalyzes the conversion of GTP to 2,5-diamino-6- ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate
Gene Name:
ribA
Uniprot ID:
P0A7I7
Molecular weight:
21836
Reactions
GTP + 3 H(2)O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.
General function:
Involved in 3,4-dihydroxy-2-butanone-4-phosphate synthase activity
Specific function:
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate
Gene Name:
ribB
Uniprot ID:
P0A7J0
Molecular weight:
23353
Reactions
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate.
General function:
Involved in catalytic activity
Specific function:
Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine
Gene Name:
pflA
Uniprot ID:
P0A9N4
Molecular weight:
28204
Reactions
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.
General function:
Involved in electron carrier activity
Specific function:
Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit
Gene Name:
fdnH
Uniprot ID:
P0AAJ3
Molecular weight:
32239
General function:
Involved in electron carrier activity
Specific function:
Allows to use formate as major electron donor during aerobic respiration. The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron- sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit
Gene Name:
fdoH
Uniprot ID:
P0AAJ5
Molecular weight:
33100
General function:
Involved in electron carrier activity
Specific function:
Probable electron transfer protein for hydrogenase 3
Gene Name:
hycB
Uniprot ID:
P0AAK1
Molecular weight:
21873
General function:
Involved in respiratory electron transport chain
Specific function:
Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. Subunit gamma is the cytochrome b556(FDN) component of the formate dehydrogenase
Gene Name:
fdnI
Uniprot ID:
P0AEK7
Molecular weight:
25368
General function:
Involved in respiratory electron transport chain
Specific function:
Allows to use formate as major electron donor during aerobic respiration. Subunit gamma is probably the cytochrome b556(FDO) component of the formate dehydrogenase
Gene Name:
fdoI
Uniprot ID:
P0AEL0
Molecular weight:
24606
General function:
Involved in oxidoreductase activity, acting on NADH or NADPH
Specific function:
Specific function unknown
Gene Name:
hycE
Uniprot ID:
P16431
Molecular weight:
64980
General function:
Involved in electron carrier activity
Specific function:
Probable electron transfer protein for hydrogenase 3
Gene Name:
hycF
Uniprot ID:
P16432
Molecular weight:
20309
General function:
Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:
Specific function unknown
Gene Name:
hycG
Uniprot ID:
P16433
Molecular weight:
27999
General function:
Involved in formate dehydrogenase (NAD+) activity
Specific function:
Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The alpha subunit forms the active site
Gene Name:
fdnG
Uniprot ID:
P24183
Molecular weight:
112963
Reactions
Formate + NAD(+) = CO(2) + NADH.
General function:
Involved in formate dehydrogenase (NAD+) activity
Specific function:
Allows to use formate as major electron donor during aerobic respiration. Subunit alpha possibly forms the active site
Gene Name:
fdoG
Uniprot ID:
P32176
Molecular weight:
112549
Reactions
Formate + NAD(+) = CO(2) + NADH.
General function:
Involved in catalytic activity
Specific function:
Acetyl-CoA + formate = CoA + pyruvate
Gene Name:
pflD
Uniprot ID:
P32674
Molecular weight:
85959
Reactions
Acetyl-CoA + formate = CoA + pyruvate.
General function:
Involved in iron-sulfur cluster binding
Specific function:
Activation of pyruvate formate-lyase 2 under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine
Gene Name:
pflC
Uniprot ID:
P32675
Molecular weight:
32429
Reactions
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.
General function:
Involved in carboxylesterase activity
Specific function:
Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against alpha-naphthyl acetate, lactoylglutathione, palmitoyl-CoA and several pNP-esters of short chain fatty acids
Gene Name:
yeiG
Uniprot ID:
P33018
Molecular weight:
31259
Reactions
S-formylglutathione + H(2)O = glutathione + formate.
General function:
Involved in ATP binding
Specific function:
Catalyzes two reactions:the first one is the production of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta GAR; the second, a side reaction, is the production of acetyl phosphate and ADP from acetate and ATP
Gene Name:
purT
Uniprot ID:
P33221
Molecular weight:
42433
Reactions
Formate + ATP + 5'-phospho-ribosylglycinamide = 5'-phosphoribosyl-N-formylglycinamide + ADP + diphosphate.
General function:
Involved in amino acid binding
Specific function:
Produces formate from formyl-tetrahydrofolate. Provides the major source of formate for the purT-dependent synthesis of 5'-phosphoribosyl-N-formylglycinamide (FGAR) during aerobic growth. Has a role in regulating the one-carbon pool
Gene Name:
purU
Uniprot ID:
P37051
Molecular weight:
31934
Reactions
10-formyltetrahydrofolate + H(2)O = formate + tetrahydrofolate.
General function:
Involved in formate C-acetyltransferase activity
Specific function:
Specific function unknown
Gene Name:
tdcE
Uniprot ID:
P42632
Molecular weight:
85935
Reactions
Propionyl-CoA + formate = CoA + 2-oxobutanoate.
Acetyl-CoA + formate = CoA + pyruvate.
General function:
Involved in carboxylesterase activity
Specific function:
Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against two pNP-esters (pNP- acetate and pNP-propionate), alpha-naphthyl acetate and lactoylglutathione
Gene Name:
frmB
Uniprot ID:
P51025
Molecular weight:
31424
Reactions
S-formylglutathione + H(2)O = glutathione + formate.
General function:
Involved in catalytic activity
Specific function:
Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate
Gene Name:
frc
Uniprot ID:
P69902
Molecular weight:
45828
Reactions
Formyl-CoA + oxalate = formate + oxalyl-CoA.
General function:
Involved in catalytic activity
Specific function:
Acetyl-CoA + formate = CoA + pyruvate
Gene Name:
ybiW
Uniprot ID:
P75793
Molecular weight:
90125
Reactions
Acetyl-CoA + formate = CoA + pyruvate.
General function:
Involved in catalytic activity
Specific function:
Catalyzes the formation of 4-diphosphocytidyl-2-C- methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4- phosphate (MEP)
Gene Name:
ispD
Uniprot ID:
Q46893
Molecular weight:
25737
Reactions
CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol.
General function:
Involved in oxidoreductase activity
Specific function:
Specific function unknown
Gene Name:
hyfJ
Uniprot ID:
P77453
Molecular weight:
15577
General function:
Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:
Specific function unknown
Gene Name:
hyfD
Uniprot ID:
P77416
Molecular weight:
51754
General function:
Involved in oxidoreductase activity, acting on NADH or NADPH
Specific function:
Specific function unknown
Gene Name:
hyfG
Uniprot ID:
P77329
Molecular weight:
63383
General function:
Involved in hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Specific function:
Catalyzes the deformylation of 4-deoxy-4-formamido-L- arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose- phosphoundecaprenol. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (Probable)
Gene Name:
arnD
Uniprot ID:
P76472
Molecular weight:
33112
Reactions
4-deoxy-4-formamido-beta-L-arabinose di-trans,poly-cis-undecaprenyl phosphate + H(2)O = 4-amino-4-deoxy-alpha-L-arabinose di-trans,poly-cis-undecaprenyl phosphate + formate.
General function:
Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:
Specific function unknown
Gene Name:
hyfF
Uniprot ID:
P77437
Molecular weight:
56766
General function:
Involved in oxidoreductase activity, acting on NADH or NADPH
Specific function:
Specific function unknown
Gene Name:
hyfE
Uniprot ID:
P0AEW1
Molecular weight:
23361
General function:
Involved in oxidation-reduction process
Specific function:
Specific function unknown
Gene Name:
hyfC
Uniprot ID:
P77858
Molecular weight:
34359
General function:
Involved in thiamine biosynthetic process
Specific function:
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction
Gene Name:
thiC
Uniprot ID:
P30136
Molecular weight:
70850
Reactions
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-phosphomethylpyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO.
General function:
Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:
Specific function unknown
Gene Name:
hyfI
Uniprot ID:
P77668
Molecular weight:
28101
General function:
Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:
Specific function unknown
Gene Name:
hyfB
Uniprot ID:
P23482
Molecular weight:
72582
General function:
Involved in catalytic activity
Specific function:
Acts as a radical domain for damaged PFL and possibly other radical proteins
Gene Name:
grcA
Uniprot ID:
P68066
Molecular weight:
14284
General function:
Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:
Specific function unknown
Gene Name:
hycC
Uniprot ID:
P16429
Molecular weight:
64076
General function:
Involved in electron carrier activity
Specific function:
Probable electron transfer protein for hydrogenase 4
Gene Name:
hyfH
Uniprot ID:
P77423
Molecular weight:
20159
General function:
Involved in electron carrier activity
Specific function:
Probable electron transfer protein for hydrogenase 4
Gene Name:
hyfA
Uniprot ID:
P23481
Molecular weight:
22154
General function:
Involved in oxidation-reduction process
Specific function:
Specific function unknown
Gene Name:
hycD
Uniprot ID:
P16430
Molecular weight:
33029

Transporters

General function:
Lipid transport and metabolism
Specific function:
Responsible for the intake of short-chain fatty acids
Gene Name:
atoE
Uniprot ID:
P76460
Molecular weight:
47527
General function:
Involved in transporter activity
Specific function:
Involved in the bidirectional transport of formate
Gene Name:
focB
Uniprot ID:
P77733
Molecular weight:
30564
General function:
Involved in transporter activity
Specific function:
Involved in the bidirectional transport of formate
Gene Name:
focA
Uniprot ID:
P0AC23
Molecular weight:
30991
General function:
Involved in transporter activity
Specific function:
Non-specific porin
Gene Name:
ompN
Uniprot ID:
P77747
Molecular weight:
41220
General function:
Involved in transporter activity
Specific function:
Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes
Gene Name:
phoE
Uniprot ID:
P02932
Molecular weight:
38922
General function:
Involved in transporter activity
Specific function:
OmpF is a porin that forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane. It is also a receptor for the bacteriophage T2
Gene Name:
ompF
Uniprot ID:
P02931
Molecular weight:
39333
General function:
Involved in transporter activity
Specific function:
Forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane
Gene Name:
ompC
Uniprot ID:
P06996
Molecular weight:
40368