EC Numbers

Enzyme Commission numbers represent classes of Functional Roles assigned by the International Union of Biochemistry and Molecular Biology. In particular, they represent functional roles performed by specific, known enzymes.

EC Number example for ribose-phosphate diphosphokinase
The EC numbers are organized in a four-level hierarchy, and each EC number consists of four numbers separated by dots. A hyphen (-) is used as a wild card, and numbers in the 90s are used to represent miscellaneous categories. A full, four-part EC number without any wild cards represents a specific enzyme. The example on the right shows the EC number for an enzyme that catalyzes reactions which transfer a specific type of phosphorous-containing sub-molecular group.

In the Sprout Database, EC numbers are stored as part of a gene's functional assignment, as shown below.

CampySearchResult.GIF

Note that because EC numbers are associated with enzymes, only a Protein Encoding Gene can have an EC number in its assignment.

A complete outline of the EC numbers is given below. Click on a number to search for matching genes in the Sprout Database.

1 Oxidoreductases.
  1.1 Acting on the CH-OH group of donors.
    1.1.1 With NAD(+) or NADP(+) as acceptor.
    1.1.2 With a cytochrome as acceptor.
    1.1.3 With oxygen as acceptor.
    1.1.4 With a disulfide as acceptor.
    1.1.5 With a quinone or similar compound as acceptor.
    1.1.99 With other acceptors.
  1.2 Acting on the aldehyde or oxo group of donors.
    1.2.1 With NAD(+) or NADP(+) as acceptor.
    1.2.2 With a cytochrome as acceptor.
    1.2.3 With oxygen as acceptor.
    1.2.4 With a disulfide as acceptor.
    1.2.7 With an iron-sulfur protein as acceptor.
    1.2.99 With other acceptors.
  1.3 Acting on the CH-CH group of donors.
    1.3.1 With NAD(+) or NADP(+) as acceptor.
    1.3.2 With a cytochrome as acceptor.
    1.3.3 With oxygen as acceptor.
    1.3.5 With a quinone or related compound as acceptor.
    1.3.7 With an iron-sulfur protein as acceptor.
    1.3.99 With other acceptors.
  1.4 Acting on the CH-NH(2) group of donors.
    1.4.1 With NAD(+) or NADP(+) as acceptor.
    1.4.2 With a cytochrome as acceptor.
    1.4.3 With oxygen as acceptor.
    1.4.4 With a disulfide as acceptor.
    1.4.7 With an iron-sulfur protein as acceptor.
    1.4.99 With other acceptors.
  1.5 Acting on the CH-NH group of donors.
    1.5.1 With NAD(+) or NADP(+) as acceptor.
    1.5.3 With oxygen as acceptor.
    1.5.4 With a disulfide as acceptor.
    1.5.5 With a quinone or similar compound as acceptor.
    1.5.7 With an iron-sulfur protein as acceptor.
    1.5.8 With a flavin as acceptor.
    1.5.99 With other acceptors.
  1.6 Acting on NADH or NADPH.
    1.6.1 With NAD(+) or NADP(+) as acceptor.
    1.6.2 With a heme protein as acceptor.
    1.6.3 With a oxygen as acceptor.
    1.6.5 With a quinone or similar compound as acceptor.
    1.6.6 With a nitrogenous group as acceptor.
    1.6.99 With other acceptors.
  1.7 Acting on other nitrogenous compounds as donors.
    1.7.1 With NAD(+) or NADP(+) as acceptor.
    1.7.2 With a cytochrome as acceptor.
    1.7.3 With oxygen as acceptor.
    1.7.7 With an iron-sulfur protein as acceptor.
    1.7.99 With other acceptors.
  1.8 Acting on a sulfur group of donors.
    1.8.1 With NAD(+) or NADP(+) as acceptor.
    1.8.2 With a cytochrome as acceptor.
    1.8.3 With oxygen as acceptor.
    1.8.4 With a disulfide as acceptor.
    1.8.5 With a quinone or similar compound as acceptor.
    1.8.7 With an iron-sulfur protein as acceptor.
    1.8.98 With other, known, acceptors.
    1.8.99 With other acceptors.
  1.9 Acting on a heme group of donors.
    1.9.3 With oxygen as acceptor.
    1.9.6 With a nitrogenous group as acceptor.
    1.9.99 With other acceptors.
  1.10 Acting on diphenols and related substances as donors.
    1.10.1 With NAD(+) or NADP(+) as acceptor.
    1.10.2 With a cytochrome as acceptor.
    1.10.3 With oxygen as acceptor.
    1.10.99 With other acceptors.
  1.11 Acting on a peroxide as acceptor.
    1.11.1 Peroxidases.
  1.12 Acting on hydrogen as donor.
    1.12.1 With NAD(+) or NADP(+) as acceptor.
    1.12.2 With a cytochrome as acceptor.
    1.12.5 With a quinone or similar compound as acceptor.
    1.12.7 With an iron-sulfur protein as acceptor.
    1.12.98 With other known acceptors.
    1.12.99 With other acceptors.
  1.13 Acting on single donors with incorporation of molecular oxygen.
    1.13.11 With incorporation of two atoms of oxygen.
    1.13.12 With incorporation of one atom of oxygen.
    1.13.99 Miscellaneous (requires further characterization).
  1.14 Acting on paired donors, with incorporation or reduction of
    1.14.11 With 2-oxoglutarate as one donor, and incorporation of one
    1.14.12 With NADH or NADPH as one donor, and incorporation of two
    1.14.13 With NADH or NADPH as one donor, and incorporation of one atom
    1.14.14 With reduced flavin or flavoprotein as one donor, and
    1.14.15 With a reduced iron-sulfur protein as one donor, and
    1.14.16 With reduced pteridine as one donor, and incorporation of one
    1.14.17 With reduced ascorbate as one donor, and incorporation of one
    1.14.18 With another compound as one donor, and incorporation of one
    1.14.19 With oxidation of a pair of donors resulting in the reduction
    1.14.20 With 2-oxoglutarate as one donor, and the other dehydrogenated.
    1.14.21 With NADH or NADPH as one donor, and the other dehydrogenated.
    1.14.99 Miscellaneous (requires further characterization).
  1.15 Acting on superoxide as acceptor.
    1.15.1 Acting on superoxide as acceptor.
  1.16 Oxidizing metal ions.
    1.16.1 With NAD(+) or NADP(+) as acceptor.
    1.16.3 With oxygen as acceptor.
    1.16.8 With flavin as acceptor.
  1.17 Acting on CH or CH(2) groups.
    1.17.1 With NAD(+) or NADP(+) as acceptor.
    1.17.3 With oxygen as acceptor.
    1.17.4 With a disulfide as acceptor.
    1.17.5 With a quinone or similar compound as acceptor.
    1.17.99 With other acceptors.
  1.18 Acting on iron-sulfur proteins as donors.
    1.18.1 With NAD(+) or NADP(+) as acceptor.
    1.18.6 With dinitrogen as acceptor.
  1.19 Acting on reduced flavodoxin as donor.
    1.19.6 With dinitrogen as acceptor.
  1.20 Acting on phosphorus or arsenic in donors.
    1.20.1 Acting on phosphorus or arsenic in donors, with NAD(P)(+) as
    1.20.4 Acting on phosphorus or arsenic in donors, with disulfide as
    1.20.98 Acting on phosphorus or arsenic in donors, with other, known
    1.20.99 Acting on phosphorus or arsenic in donors, with other
  1.21 Acting on x-H and y-H to form an x-y bond.
    1.21.3 With oxygen as acceptor.
    1.21.4 With a disulfide as acceptor.
    1.21.99 With other acceptors.
  1.97 Other oxidoreductases.
    1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the
2 Transferases.
  2.1 Transferring one-carbon groups.
    2.1.1 Methyltransferases.
    2.1.2 Hydroxymethyl-, formyl- and related transferases.
    2.1.3 Carboxyl- and carbamoyltransferases.
    2.1.4 Amidinotransferases.
  2.2 Transferring aldehyde or ketone residues.
    2.2.1 Transketolases and transaldolases.
  2.3 Acyltransferases.
    2.3.1 Transferring groups other than amino-acyl groups.
    2.3.2 Aminoacyltransferases.
    2.3.3 Acyl groups converted into alkyl on transfer.
  2.4 Glycosyltransferases.
    2.4.1 Hexosyltransferases.
    2.4.2 Pentosyltransferases.
    2.4.99 Transferring other glycosyl groups.
  2.5 Transferring alkyl or aryl groups, other than methyl groups.
    2.5.1 Transferring alkyl or aryl groups, other than methyl groups.
  2.6 Transferring nitrogenous groups.
    2.6.1 Transaminases (aminotransferases).
    2.6.3 Oximinotransferases.
    2.6.99 Transferring other nitrogenous groups.
  2.7 Transferring phosphorous-containing groups.
    2.7.1 Phosphotransferases with an alcohol group as acceptor.
    2.7.2 Phosphotransferases with a carboxyl group as acceptor.
    2.7.3 Phosphotransferases with a nitrogenous group as acceptor.
    2.7.4 Phosphotransferases with a phosphate group as acceptor.
    2.7.6 Diphosphotransferases.
    2.7.7 Nucleotidyltransferases.
    2.7.8 Transferases for other substituted phosphate groups.
    2.7.9 Phosphotransferases with paired acceptors.
    2.7.10 Protein-tyrosine kinases.
    2.7.11 Protein-serine/threonine kinases.
    2.7.12 Dual-specificity kinases (those acting on Ser/Thr and Tyr
    2.7.13 Protein-histidine kinases.
    2.7.99 Other protein kinases.
  2.8 Transferring sulfur-containing groups.
    2.8.1 Sulfurtransferases.
    2.8.2 Sulfotransferases.
    2.8.3 Co a? -transferases.
    2.8.4 Transferring alkylthio groups.
  2.9 Transferring selenium-containing groups.
    2.9.1 Selenotransferases.
3 Hydrolases.
  3.1 Acting on ester bonds.
    3.1.1 Carboxylic ester hydrolases.
    3.1.2 Thiolester hydrolases.
    3.1.3 Phosphoric monoester hydrolases.
    3.1.4 Phosphoric diester hydrolases.
    3.1.5 Triphosphoric monoester hydrolases.
    3.1.6 Sulfuric ester hydrolases.
    3.1.7 Diphosphoric monoester hydrolases.
    3.1.8 Phosphoric triester hydrolases.
    3.1.11 Exodeoxyribonucleases producing 5'-phosphomonoesters.
    3.1.13 Exoribonucleases producing 5'-phosphomonoesters.
    3.1.14 Exoribonucleases producing 3'-phosphomonoesters.
    3.1.15 Exonucleases active with either ribo- or deoxyribonucleic acid
    3.1.16 Exonucleases active with either ribo- or deoxyribonucleic acid
    3.1.21 Endodeoxyribonucleases producing 5'-phosphomonoesters.
    3.1.22 Endodeoxyribonucleases producing other than 5'-phosphomonoesters.
    3.1.25 Site-specific endodeoxyribonucleases specific for altered bases.
    3.1.26 Endoribonucleases producing 5'-phosphomonoesters.
    3.1.27 Endoribonucleases producing other than 5'-phosphomonoesters.
    3.1.30 Endoribonucleases active with either ribo- or deoxyribonucleic
    3.1.31 Endoribonucleases active with either ribo- or deoxyribonucleic
  3.2 Glycosylases.
    3.2.1 Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl
    3.2.2 Hydrolyzing N-glycosyl compounds.
  3.3 Acting on ether bonds.
    3.3.1 Thioether and trialkylsulfonium hydrolases.
    3.3.2 Ether hydrolases.
  3.4 Acting on peptide bonds (peptide hydrolases).
    3.4.11 Aminopeptidases.
    3.4.13 Dipeptidases.
    3.4.14 Dipeptidyl-peptidases and tripeptidyl-peptidases.
    3.4.15 Peptidyl-dipeptidases.
    3.4.16 Serine-type carboxypeptidases.
    3.4.17 Metallocarboxypeptidases.
    3.4.18 Cysteine-type carboxypeptidases.
    3.4.19 Omega peptidases.
    3.4.21 Serine endopeptidases.
    3.4.22 Cysteine endopeptidases.
    3.4.23 Aspartic endopeptidases.
    3.4.24 Metalloendopeptidases.
    3.4.25 Threonine endopeptidases.
    3.4.99 Endopeptidases of unknown catalytic mechanism.
  3.5 Acting on carbon-nitrogen bonds, other than peptide bonds.
    3.5.1 In linear amides.
    3.5.2 In cyclic amides.
    3.5.3 In linear amidines.
    3.5.4 In cyclic amidines.
    3.5.5 In nitriles.
    3.5.99 In other compounds.
  3.6 Acting on acid anhydrides.
    3.6.1 In phosphorous-containing anhydrides.
    3.6.2 In sulfonyl-containing anhydrides.
    3.6.3 Acting on acid anhydrides; catalyzing transmembrane movement
    3.6.4 Acting on acid anhydrides; involved in cellular and
    3.6.5 Acting on GTP; involved in cellular and subcellular movement.
  3.7 Acting on carbon-carbon bonds.
    3.7.1 In ketonic substances.
  3.8 Acting on halide bonds.
    3.8.1 In C-halide compounds.
  3.9 Acting on phosphorus-nitrogen bonds.
    3.9.1 Acting on phosphorus-nitrogen bonds.
  3.10 Acting on sulfur-nitrogen bonds.
    3.10.1 Acting on sulfur-nitrogen bonds.
  3.11 Acting on carbon-phosphorus bonds.
    3.11.1 Acting on carbon-phosphorus bonds.
  3.12 Acting on sulfur-sulfur bonds.
    3.12.1 Acting on sulfur-sulfur bonds.
  3.13 Acting on carbon-sulfur bonds.
    3.13.1 Acting on carbon-sulfur bonds.
4 Lyases.
  4.1 Carbon-carbon lyases.
    4.1.1 Carboxy-lyases.
    4.1.2 Aldehyde-lyases.
    4.1.3 Oxo-acid-lyases.
    4.1.99 Other carbon-carbon lyases.
  4.2 Carbon-oxygen lyases.
    4.2.1 Hydro-lyases.
    4.2.2 Acting on polysaccharides.
    4.2.3 Acting on phosphates.
    4.2.99 Other carbon-oxygen lyases.
  4.3 Carbon-nitrogen lyases.
    4.3.1 Ammonia-lyases.
    4.3.2 Lyases acting on amides, amidines, etc.
    4.3.3 Amine-lyases.
  4.4 Carbon-sulfur lyases.
    4.4.1 Carbon-sulfur lyases.
  4.5 Carbon-halide lyases.
    4.5.1 Carbon-halide lyases.
  4.6 Phosphorus-oxygen lyases.
    4.6.1 Phosphorus-oxygen lyases.
  4.99 Other lyases.
    4.99.1 Sole sub-subclass for lyases that do not belong in the other
5 Isomerases.
  5.1 Racemases and epimerases.
    5.1.1 Acting on amino acids and derivatives.
    5.1.2 Acting on hydroxy acids and derivatives.
    5.1.3 Acting on carbohydrates and derivatives.
    5.1.99 Acting on other compounds.
  5.2 Cis-trans-isomerases.
    5.2.1 Cis-trans Isomerases.
  5.3 Intramolecular oxidoreductases.
    5.3.1 Interconverting aldoses and ketoses.
    5.3.2 Interconverting keto- and enol- groups.
    5.3.3 Transposing C==C bonds.
    5.3.4 Transposing S-S bonds.
    5.3.99 Other intramolecular oxidoreductases.
  5.4 Intramolecular transferases (mutases).
    5.4.1 Transferring acyl groups.
    5.4.2 Phosphotransferases (phosphomutases).
    5.4.3 Transferring amino groups.
    5.4.4 Transferring hydroxy groups.
    5.4.99 Transferring other groups.
  5.5 Intramolecular lyases.
    5.5.1 Intramolecular lyases.
  5.99 Other isomerases.
    5.99.1 Sole sub-subclass for isomerases that do not belong in the other
6 Ligases.
  6.1 Forming carbon-oxygen bonds.
    6.1.1 Ligases forming aminoacyl-tRNA and related compounds.
  6.2 Forming carbon-sulfur bonds.
    6.2.1 Acid--thiol ligases.
  6.3 Forming carbon-nitrogen bonds.
    6.3.1 Acid--ammonia (or amide) ligases (amide synthases).
    6.3.2 Acid--D-amino-acid ligases (peptide synthases).
    6.3.3 Cyclo-ligases.
    6.3.4 Other carbon--nitrogen ligases.
    6.3.5 Carbon--nitrogen ligases with glutamine as amido-N-donor.
  6.4 Forming carbon-carbon bonds.
    6.4.1 Ligases that form carbon-carbon bonds.
  6.5 Forming phosphoric ester bonds.
    6.5.1 Ligases that form phosphoric-ester bonds.
  6.6 Forming nitrogen-metal bonds.
    6.6.1 Forming coordination complexes.
Topic revision: r6 - 16 Jan 2009 - 15:05:02 - Bruce Parrello
FIG.EcNumber moved from FIG.ECNumber on 24 Dec 2008 - 04:38 by Bruce Parrello - put it back
 
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