List of EC numbers (EC 7)

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This list contains a list of sub-classes for the seventh group of Enzyme Commission numbers, EC 7, translocases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. [1] The database is developed and maintained by Andrew McDonald. [2]


EC 7.1: Catalysing the translocation of hydrons [3]

EC 7.1.1: Linked to oxidoreductase reactions

* No Wikipedia article

EC 7.1.2: Linked to the hydrolysis of a nucleoside triphosphate

* No Wikipedia article

EC 7.1.3: Linked to the hydrolysis of diphosphate

* No Wikipedia article

EC 7.2: catalysing the translocation of inorganic cations and their chelates

EC 7.2.1: Linked to oxidoreductase reactions

* No Wikipedia article

EC 7.2.2: Linked to the hydrolysis of a nucleoside triphosphate

* No Wikipedia article

EC 7.2.4: Linked to decarboxylation

* No Wikipedia article

EC 7.3: Catalysing the translocation of inorganic anions

EC 7.3.2: Linked to the hydrolysis of a nucleoside triphosphate

* No Wikipedia article

EC 7.4: Catalysing the translocation of amino acids and peptides

EC 7.4.2: Linked to the hydrolysis of a nucleoside triphosphate

* No Wikipedia article

EC 7.5: Catalysing the translocation of carbohydrates and their derivatives

EC 7.5.2: Linked to the hydrolysis of a nucleoside triphosphate

* No Wikipedia article

EC 7.6: Catalysing the translocation of other compounds

EC 7.6.2: Linked to the hydrolysis of a nucleoside triphosphate

* No Wikipedia article

Related Research Articles

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In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP+ or NAD+ as cofactors. Transmembrane oxidoreductases create electron transport chains in bacteria, chloroplasts and mitochondria, including respiratory complexes I, II and III. Some others can associate with biological membranes as peripheral membrane proteins or be anchored to the membranes through a single transmembrane helix.

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Aromatic-ring-hydroxylating dioxygenases (ARHD) incorporate two atoms of dioxygen (O2) into their substrates in the dihydroxylation reaction. The product is (substituted) cis-1,2-dihydroxycyclohexadiene, which is subsequently converted to (substituted) benzene glycol by a cis-diol dehydrogenase.

The Transporter Classification Database is an International Union of Biochemistry and Molecular Biology (IUBMB)-approved classification system for membrane transport proteins, including ion channels.

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Translocase is a general term for a protein that assists in moving another molecule, usually across a cell membrane. These enzymes catalyze the movement of ions or molecules across membranes or their separation within membranes. The reaction is designated as a transfer from “side 1” to “side 2” because the designations “in” and “out”, which had previously been used, can be ambiguous. Translocases are the most common secretion system in Gram positive bacteria.

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<span class="mw-page-title-main">Protochlorophyllide reductase</span>

In enzymology, protochlorophyllide reductases (POR) are enzymes that catalyze the conversion from protochlorophyllide to chlorophyllide a. They are oxidoreductases participating in the biosynthetic pathway to chlorophylls.

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In enzymology, a ferredoxin–NAD+ reductase (EC is an enzyme that catalyzes the chemical reaction:

<span class="mw-page-title-main">Pyrroline-5-carboxylate reductase</span>

In enzymology, a pyrroline-5-carboxylate reductase (EC is an enzyme that catalyzes the chemical reaction

Oxidoreductase NAD-binding domain is an evolutionary conserved protein domain present in a variety of proteins that include, bacterial flavohemoprotein, mammalian NADH-cytochrome b5 reductase, eukaryotic NADPH-cytochrome P450 reductase, nitrate reductase from plants, nitric-oxide synthase, bacterial vanillate demethylase and others.

NADH:ubiquinone reductase (Na+-transporting) (EC is an enzyme with systematic name NADH:ubiquinone oxidoreductase (Na+-translocating). In bacteria, three different types of respiratory NADH:quinone oxidoreductases (NQr) have been described: the electrogenic complex I, also called NDH I in bacteria, the non-electrogenic NADH:quinone oxidoreductases (NDH II), and the Na+-translocating NADH:quinone oxidoreductases Na+-NQr. The common function of these transmembrane enzymes in respiration is to oxidize NADH using ubiquinone (Q) as electron acceptor. The net reaction thus yields ubiquinol (QH2), the reducing substrate of enzyme complexes further along the respiratory chain, and NAD+, which is used as oxidizing agent in numerous cellular processes.

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The H+-translocating F420H2 Dehydrogenase (F420H2DH) Family(TC# 3.D.9) is a member of the Na+ transporting Mrp superfamily. A single F420H2 dehydrogenase (also referred to as F420H2:quinol oxidoreductase) from the methanogenic archaeon, Methanosarcina mazei Gö1, has been shown to be a redox driven proton pump. The F420H2DH of M. mazei has a molecular size of about 120 kDa and contains Fe-S clusters and FAD. A similar five-subunit enzyme has been isolated from Methanolobus tindarius. The sulfate-reducing Archaeoglobus fulgidus (and several other archaea) also have this enzyme.


  1. "ExplorEnz – The Enzyme Database".
  2. McDonald, A.G.; Boyce, S.; K.F., Tipton (2009). "ExplorEnz: the primary source of the IUBMB enzyme list". Nucleic Acids Res. 37: D593–D597. doi: 10.1093/nar/gkn582 . PMC   2686581 .
  3. Hydron is a generic term that includes all isotopes of H+, i.e. not only 1H+ but also 2H+ (D+) and 3H+ (T+).