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MetaCyc Reaction: 3.6.1.3/3.6.1.15/3.6.3.50/3.6.3.51/3.6.3.52/3.6.4.1/3.6.4.2/3.6.4.3/3.6.4.4/3.6.4.5/3.6.4.6/3.6.4.7/3.6.4.8/3.6.4.9/3.6.4.10/3.6.4.11/3.6.4.12/3.6.4.13

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.6.1.3 , 3.6.1.15 , 3.6.3.50 , 3.6.3.51 , 3.6.3.52 , 3.6.4.1 , 3.6.4.2 , 3.6.4.3 , 3.6.4.4 , 3.6.4.5 , 3.6.4.6 , 3.6.4.7 , 3.6.4.8 , 3.6.4.9 , 3.6.4.10 , 3.6.4.11 , 3.6.4.12 , 3.6.4.13

Enzymes and Genes:

Aquifex aeolicus VF5 : nucleoside-triphosphatase Inferred from experiment : THEP1
Arabidopsis thaliana col : purple acid phosphatase [multifunctional] Inferred from experiment : PAP12
Bacillus subtilis subtilis 168 : nucleoside triphosphate phosphohydrolase : ytkD
Escherichia coli K-12 substr. MG1655 :
Glycine soja :
Homo sapiens :
Pisum sativum : nucleoside-triphosphatase : NTP1
Saccharomyces cerevisiae : apyrase : YND1
Solanum tuberosum : nucleoside triphosphate phosphohydrolase / ATP phosphohydrolase : RROP1

Sub-reaction of:
3.6.1.5: ATP + 2 H2O → AMP + 2 phosphate + 2 H+

Supersedes EC numbers: 3.6.1.32, 3.6.1.33

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name for 3.6.1.3: adenosinetriphosphatase

Enzyme Commission Synonyms for 3.6.1.3: adenylpyrophosphatase, ATP monophosphatase, triphosphatase, ATPase (ambiguous), SV40 T-antigen, adenosine 5'-triphosphatase, ATP hydrolase, complex V (mitochondrial electron transport), (Ca2+ + Mg2+)-ATPase, HCO3--ATPase, adenosine triphosphatase

Enzyme Commission Primary Name for 3.6.1.15: nucleoside-triphosphate phosphatase

Enzyme Commission Synonyms for 3.6.1.15: nucleoside-triphosphatase, nucleoside triphosphate phosphohydrolase, nucleoside-5-triphosphate phosphohydrolase, nucleoside 5-triphosphatase, unspecific diphosphate phosphohydrolase

Enzyme Commission Primary Name for 3.6.3.50: protein-secreting ATPase

Enzyme Commission Primary Name for 3.6.3.51: mitochondrial protein-transporting ATPase

Enzyme Commission Primary Name for 3.6.3.52: chloroplast protein-transporting ATPase

Enzyme Commission Primary Name for 3.6.4.1: myosin ATPase

Enzyme Commission Synonyms for 3.6.4.1: Actomyosin

Enzyme Commission Primary Name for 3.6.4.2: dynein ATPase

Enzyme Commission Synonyms for 3.6.4.2: dynein adenosine 5'-triphosphatase

Enzyme Commission Primary Name for 3.6.4.3: microtubule-severing ATPase

Enzyme Commission Synonyms for 3.6.4.3: Katanin

Enzyme Commission Primary Name for 3.6.4.4: plus-end-directed kinesin ATPase

Enzyme Commission Synonyms for 3.6.4.4: kinesin

Enzyme Commission Primary Name for 3.6.4.5: minus-end-directed kinesin ATPase

Enzyme Commission Primary Name for 3.6.4.6: vesicle-fusing ATPase

Enzyme Commission Primary Name for 3.6.4.7: peroxisome-assembly ATPase

Enzyme Commission Synonyms for 3.6.4.7: peroxisome assembly factor-2

Enzyme Commission Primary Name for 3.6.4.8: proteasome ATPase

Enzyme Commission Synonyms for 3.6.4.8: RP triple-A protein, RP triphosphatase

Enzyme Commission Primary Name for 3.6.4.9: chaperonin ATPase

Enzyme Commission Synonyms for 3.6.4.9: chaperonin

Enzyme Commission Primary Name for 3.6.4.10: non-chaperonin molecular chaperone ATPase

Enzyme Commission Synonyms for 3.6.4.10: molecular chaperone Hsc70 ATPase

Enzyme Commission Primary Name for 3.6.4.11: nucleoplasmin ATPase

Enzyme Commission Primary Name for 3.6.4.12: DNA helicase

Enzyme Commission Synonyms for 3.6.4.12: 3' to 5' DNA helicase, 3'-5' DNA helicase, 3'-5' PfDH, 5' to 3' DNA helicase, AvDH1, BACH1 helicase, BcMCM, BLM protein, BRCA1-associated C-terminal helicase, CeWRN-1, Dbp9p, DmRECQ5, DNA helicase 120, DNA helicase A, DNA helicase E, DNA helicase II, DNA helicase III, DNA helicase RECQL5β, DNA helicase VI, dnaB, DnaB helicase E1, helicase HDH IV, Hel E, helicase DnaB, helicase domain of bacteriophage T7 gene 4 protein helicase, UvrD, hHcsA, Hmi1p, hPif1, MCM helicase, MCM protein, MER3 helicase, MER3 protein, MPH1, PcrA, PcrA helicase, PDH120, PfDH A, Pfh1p, PIF1

Enzyme Commission Primary Name for 3.6.4.13: RNA helicase

Enzyme Commission Synonyms for 3.6.4.13: CSFV NS3 helicase, DBP2, DbpA, DDX17, DDX25, DDX3, DDX3X, DDX3Y, DDX4, DDX5, DEAD-box protein DED1, DEAD-box RNA helicase, DEAH-box protein 2, DEAH-box RNA helicase, DED1, Dex(H/D) RNA helicase, EhDEAD1, EhDEAD1 RNA helicase, eIF4A helicase, KOKV helicase, Mtr4p, nonstructural protein 3 helicase, NPH-II, RHA, RNA helicase A, RNA helicase DDX3, RNA helicase Hera, RNA-dependent ATPase, TGBp1 NTPase/helicase domain, VRH1, GRTH/DDX25

Taxonomic Range: Archaea , Viridiplantae , Bacteria , Fungi , Metazoa

Standard Gibbs Free Energy (ΔrG in kcal/mol): -7.598877 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary for 3.6.1.3:
Many enzymes previously listed under this number are now listed separately under EC 3.6.3 and EC 3.6.4.

Enzyme Commission Summary for 3.6.1.15:
Also hydrolyses other nucleoside triphosphates, diphosphates, thiamine diphosphate and FAD.

Enzyme Commission Summary for 3.6.3.50:
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport.

There are several families of enzymes included here, e.g. ATP-hydrolyzing enzymes of the general secretory pathway (Sec or Type II), of the virulence-related secretory pathway (Type III) and of the conjugal DNA-protein transfer pathway (Type IV).

Type II enzymes occur in bacteria, archaea and eucarya, whereas type III and type IV enzymes occur in bacteria where they form components of a multi-subunit complex.

Enzyme Commission Summary for 3.6.3.51:
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase involved in the transport of proteins or preproteins into mitochondria using the TIM protein complex.

TIM is the protein transport machinery of the inner mitochondrial membrane that contains three essential Tim proteins: Tim17 and Tim23 are thought to build a preprotein translocation channel while Tim44 interacts transiently with the matrix heat- shock protein Hsp70 to form an ATP-driven import motor.

Enzyme Commission Summary for 3.6.3.52:
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport.

Involved in the transport of proteins or preproteins into chloroplast stroma (several ATPases may participate in this process).

Enzyme Commission Summary for 3.6.4.1:
Proteins of the contractile apparatus of muscle and nonmuscle cells; myosin molecule consists of two heavy chains (about 200 kDa) and two pairs of light chains (15-27 kDa). The head region of the heavy chain contains actin- and ATP-binding sites. ATP hydrolysis provides energy for actomyosin contraction.

Enzyme Commission Summary for 3.6.4.2:
A multisubunit protein complex associated with microtubules. Hydrolysis of ATP provides energy for the movement of organelles (endosomes, lysosomes, mitochondria) along microtubules to the centrosome towards the microtubule's minus end. It also functions in the movement of eukaryotic flagella and cilia. It consists of two heavy chains (about 500 kDa), three-four intermediate chains (about 70 kDa) and four light chains (about 50 kDa).

Enzyme Commission Summary for 3.6.4.3:
Another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.

Enzyme Commission Summary for 3.6.4.4:
Microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (α) chains (110 kDa) and two or more light (β) chains (65-75 kDa). Also hydrolyses GTP.

Enzyme Commission Summary for 3.6.4.5:
Structurally almost identical to EC 3.6.4.4, plus-end-directed kinesin ATPase, but the movement it catalyzes is towards the minus end of microtubules.

Enzyme Commission Summary for 3.6.4.6:
A large family of ATP-hydrolyzing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments.

They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily.

They include peroxin, which apparently is involved in Zellweger's syndrome.

Enzyme Commission Summary for 3.6.4.7:
An extremely diversified group of enzymes that use the energy of ATP hydrolysis to import and assemble peroxisome components into the organelle.

Their molecular masses range from 25 to 600 kDa.

Enzyme Commission Summary for 3.6.4.8:
Belongs to the AAA-type superfamily and, like EC 3.6.4.5, minus-end-directed kinesin ATPase, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome.

Enzyme Commission Summary for 3.6.4.9:
Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or to entry into mitochondria and chloroplasts. Molecular masses of subunits ranges from 10-90 kDa.

Enzyme Commission Summary for 3.6.4.10:
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins.

They comprise a number of heat-shock-cognate proteins.

They are also active in clathrin uncoating and in the oligomerization of actin.

Enzyme Commission Summary for 3.6.4.11:
An acidic nuclear protein that is active in the ATP-dependent assembly of nucleosome cores, in decondensation of sperm chromatin and in other histone-involving processes.

Enzyme Commission Summary for 3.6.4.12:
DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. Some of them unwind duplex DNA with a 3 to 5 polarity [Ozsoy01, Nakagawa01, Phan03, Curti07], others show 5 to 3 polarity [Ivanov04, Ivessa02, Zhou02, George09] or unwind DNA in both directions [Naqvi03, RuizMaso06]. Some helicases unwind DNA as well as RNA [Frick07, Ivanov04]. May be identical with EC 3.6.4.13, RNA helicase.

Enzyme Commission Summary for 3.6.4.13:
RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. Some of them unwind RNA with a 3 to 5 polarity [Lee92a], other show 5 to 3 polarity. Some helicases unwind DNA as well as RNA [Frick07]. May be identical with EC 3.6.4.12, DNA helicase.

Citations: [Martin80, Geider81, Riley81, Tjian81, Matsushita68, Lewis65, Brightwell68, Tong93, Hsieh96, Klinger03, Placzek07, Saier94, Mecsas, Thomas97, Baker97, Martinez98, Schuch99, Bomer97, Berthold95, Voos99, Cline92, Nakai94, Scott96, Rayment96, Hasson96, Murphy99a, Gibbons88, Summers71, Gee98, McNally93, Hartman98, Vale85, Howard97, Nakagawa97, Henningsen97, Sharp97, Sablin98, Babst98, Imamura98, Confalonieri95, Lee92b, Tsukamoto95, Yahraus96, Rivett97, Mason98, Lubben89, Hemmingsen88, Ranson98, Sadis92, BlondElguindi93, Wawrzynow95, Sriram97, Li98, Laskey93, Cote94, Ito96, Pike09, Bernstein03, Lee98, Tanner03, Cordin04, Rodamilans07, Li01, Wu05a, Gross98]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reaction of [a nucleoside triphosphate + H2O → a nucleoside diphosphate + phosphate + H+] (3.6.1.15):
i1: ATP + H2O → ADP + phosphate + H+ (3.6.1.3/3.6.1.15/3.6.3.50/3.6.3.51/3.6.3.52/3.6.4.1/3.6.4.2/3.6.4.3/3.6.4.4/3.6.4.5/3.6.4.6/3.6.4.7/3.6.4.8/3.6.4.9/3.6.4.10/3.6.4.11/3.6.4.12/3.6.4.13)

Unification Links: KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , KEGG:R00086 , Rhea:13065 , Rhea:13065

Relationship Links: BRENDA:EC:3.6.1.3 , BRENDA:EC:3.6.1.15 , BRENDA:EC:3.6.3.50 , BRENDA:EC:3.6.3.51 , BRENDA:EC:3.6.3.52 , BRENDA:EC:3.6.4.1 , BRENDA:EC:3.6.4.2 , BRENDA:EC:3.6.4.3 , BRENDA:EC:3.6.4.4 , BRENDA:EC:3.6.4.5 , BRENDA:EC:3.6.4.6 , BRENDA:EC:3.6.4.7 , BRENDA:EC:3.6.4.8 , BRENDA:EC:3.6.4.9 , BRENDA:EC:3.6.4.10 , BRENDA:EC:3.6.4.11 , BRENDA:EC:3.6.4.12 , BRENDA:EC:3.6.4.13 , ENZYME:EC:3.6.1.3 , ENZYME:EC:3.6.1.15 , ENZYME:EC:3.6.3.50 , ENZYME:EC:3.6.3.51 , ENZYME:EC:3.6.3.52 , ENZYME:EC:3.6.4.1 , ENZYME:EC:3.6.4.2 , ENZYME:EC:3.6.4.3 , ENZYME:EC:3.6.4.4 , ENZYME:EC:3.6.4.5 , ENZYME:EC:3.6.4.6 , ENZYME:EC:3.6.4.7 , ENZYME:EC:3.6.4.8 , ENZYME:EC:3.6.4.9 , ENZYME:EC:3.6.4.10 , ENZYME:EC:3.6.4.11 , ENZYME:EC:3.6.4.12 , ENZYME:EC:3.6.4.13 , IUBMB-ExplorEnz:EC:3.6.1.3 , IUBMB-ExplorEnz:EC:3.6.1.15 , IUBMB-ExplorEnz:EC:3.6.3.50 , IUBMB-ExplorEnz:EC:3.6.3.51 , IUBMB-ExplorEnz:EC:3.6.3.52 , IUBMB-ExplorEnz:EC:3.6.4.1 , IUBMB-ExplorEnz:EC:3.6.4.2 , IUBMB-ExplorEnz:EC:3.6.4.3 , IUBMB-ExplorEnz:EC:3.6.4.4 , IUBMB-ExplorEnz:EC:3.6.4.5 , IUBMB-ExplorEnz:EC:3.6.4.6 , IUBMB-ExplorEnz:EC:3.6.4.7 , IUBMB-ExplorEnz:EC:3.6.4.8 , IUBMB-ExplorEnz:EC:3.6.4.9 , IUBMB-ExplorEnz:EC:3.6.4.10 , IUBMB-ExplorEnz:EC:3.6.4.11 , IUBMB-ExplorEnz:EC:3.6.4.12 , IUBMB-ExplorEnz:EC:3.6.4.13 , UniProt:RELATED-TO:O24875 , UniProt:RELATED-TO:O27798 , UniProt:RELATED-TO:O51558 , UniProt:RELATED-TO:O51774 , UniProt:RELATED-TO:O66605 , UniProt:RELATED-TO:O67325 , UniProt:RELATED-TO:O83110 , UniProt:RELATED-TO:O83536 , UniProt:RELATED-TO:O84115 , UniProt:RELATED-TO:O84288 , UniProt:RELATED-TO:O84348 , UniProt:RELATED-TO:P02563 , UniProt:RELATED-TO:P02564 , UniProt:RELATED-TO:P02566 , UniProt:RELATED-TO:P02567 , UniProt:RELATED-TO:P03018 , UniProt:RELATED-TO:P05444 , UniProt:RELATED-TO:P05659 , UniProt:RELATED-TO:P08716 , UniProt:RELATED-TO:P08799 , UniProt:RELATED-TO:P0A9M0 , UniProt:RELATED-TO:P0A522 , UniProt:RELATED-TO:P0ABH9 , UniProt:RELATED-TO:P10568 , UniProt:RELATED-TO:P10569 , UniProt:RELATED-TO:P10587 , UniProt:RELATED-TO:P11055 , UniProt:RELATED-TO:P12844 , UniProt:RELATED-TO:P12845 , UniProt:RELATED-TO:P12847 , UniProt:RELATED-TO:P12883 , UniProt:RELATED-TO:P13533 , UniProt:RELATED-TO:P13535 , UniProt:RELATED-TO:P14105 , UniProt:RELATED-TO:P17422 , UniProt:RELATED-TO:P19524 , UniProt:RELATED-TO:P19706 , UniProt:RELATED-TO:P23098 , UniProt:RELATED-TO:P23596 , UniProt:RELATED-TO:P23787 , UniProt:RELATED-TO:P24428 , UniProt:RELATED-TO:P24733 , UniProt:RELATED-TO:P31539 , UniProt:RELATED-TO:P31540 , UniProt:RELATED-TO:P31541 , UniProt:RELATED-TO:P31542 , UniProt:RELATED-TO:P32492 , UniProt:RELATED-TO:P34036 , UniProt:RELATED-TO:P34092 , UniProt:RELATED-TO:P34109 , UniProt:RELATED-TO:P35100 , UniProt:RELATED-TO:P35579 , UniProt:RELATED-TO:P35580 , UniProt:RELATED-TO:P36022 , UniProt:RELATED-TO:P36773 , UniProt:RELATED-TO:P36774 , UniProt:RELATED-TO:P36775 , UniProt:RELATED-TO:P36776 , UniProt:RELATED-TO:P37276 , UniProt:RELATED-TO:P37571 , UniProt:RELATED-TO:P37945 , UniProt:RELATED-TO:P38650 , UniProt:RELATED-TO:P39057 , UniProt:RELATED-TO:P42762 , UniProt:RELATED-TO:P43864 , UniProt:RELATED-TO:P44403 , UniProt:RELATED-TO:P45443 , UniProt:RELATED-TO:P45444 , UniProt:RELATED-TO:P46067 , UniProt:RELATED-TO:P46523 , UniProt:RELATED-TO:P47481 , UniProt:RELATED-TO:P47807 , UniProt:RELATED-TO:P49574 , UniProt:RELATED-TO:P51332 , UniProt:RELATED-TO:P55995 , UniProt:RELATED-TO:P63284 , UniProt:RELATED-TO:P63288 , UniProt:RELATED-TO:P70704 , UniProt:RELATED-TO:P71404 , UniProt:RELATED-TO:P74361 , UniProt:RELATED-TO:P74459 , UniProt:RELATED-TO:P77810 , UniProt:RELATED-TO:P78025 , UniProt:RELATED-TO:P93647 , UniProt:RELATED-TO:Q7M4G4 , UniProt:RELATED-TO:Q9I8A2 , UniProt:RELATED-TO:Q9WY41 , UniProt:RELATED-TO:Q9X1B1 , UniProt:RELATED-TO:Q9X1W8 , UniProt:RELATED-TO:Q9Z8A6 , UniProt:RELATED-TO:Q9Z9F4 , UniProt:RELATED-TO:Q9ZD92 , UniProt:RELATED-TO:Q9ZEA9 , UniProt:RELATED-TO:Q9ZJL3 , UniProt:RELATED-TO:Q9ZMH1 , UniProt:RELATED-TO:Q9ZN31 ... [28 more not displayed]

Credits:
Created 22-Dec-2009 by Kothari A , SRI International


References

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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