6.2.1.13: acetate-CoA ligase (ADP-forming)
This is an abbreviated version!
For detailed information about acetate-CoA ligase (ADP-forming), go to the full flat file.
Word Map on EC 6.2.1.13
-
6.2.1.13
-
archaea
-
saethre-chotzen
-
amitochondriate
-
hyperthermophilic
-
cranial
-
protist
-
entamoeba
-
giardia
-
histolytica
-
acrocephalosyndactyly
-
amp-forming
-
pyrococcus
-
furiosus
-
succinyl-coa
-
skull
-
propionyl-coa
-
lamblia
-
pyruvate:ferredoxin
-
sutures
-
archaeoglobus
-
archaebacteria
-
phosphotransacetylase
-
acetate-forming
-
ppi-dependent
-
syndactyly
-
embden-meyerhof
- 6.2.1.13
- archaea
-
saethre-chotzen
-
amitochondriate
-
hyperthermophilic
-
cranial
-
protist
-
entamoeba
- giardia
- histolytica
-
acrocephalosyndactyly
-
amp-forming
- pyrococcus
- furiosus
- succinyl-coa
-
skull
- propionyl-coa
- lamblia
-
pyruvate:ferredoxin
-
sutures
- archaeoglobus
- archaebacteria
- phosphotransacetylase
-
acetate-forming
-
ppi-dependent
-
syndactyly
-
embden-meyerhof
Reaction
Synonyms
ACD, acetate:CoA ligase [ADP-forming], acetate:coenzyme A ligase (ADP-forming), Acetyl-CoA synthetase, Acetyl-CoA synthetase (ADP-forming), acetyl-coenzyme A synthetase, acetyl-coenzyme A synthetase (ADP-forming), ACS, ACS III, ACS1, ACS2, ADP acetyl-coenzyme A synthetase, ADP-ACS, ADP-forming acetyl-CoA synthetase, ADP-forming acetyl-CoA synthetase isoenzyme I, ADP-forming acetyl-coenzyme A synthetase, ADP-forming acyl coenzyme A synthetase, ADP-forming acyl-CoA synthetase, EhACD, PF1540, PF1787, Synthetase, acetyl coenzyme A (adenosine diphosphate-forming), TK0944/TK0943 protein
ECTree
Advanced search results
Subunits
Subunits on EC 6.2.1.13 - acetate-CoA ligase (ADP-forming)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
heterotetramer
homodimer
homotetramer
monomer
tetramer
additional information
Q9Y8L0, Q9Y8L1
alpha2,beta2, 2 * 47000 (alpha) + 2 * 25000 (beta), SDS-PAGE
heterotetramer
2 * 49965 (alpha) + 2 * 25878 (beta), calculated from sequence
tetramer
2 * 47000, alpha-subunit, + 2 * 27000, beta-subunit, SDS-PAGE
additional information
-
a heterotetrameric ACD with alpha2beta structure, structural model, ACD shows a spatial arrangement of the subunits different from Escherichia coli succinyl-CoA synthetase, SCS, but maintaining a similar catalytic site, structural consequences of the domain shuffling in ACD, overview
additional information
a heterotetrameric ACD with alpha2beta structure, structural model, ACD shows a spatial arrangement of the subunits different from Escherichia coli succinyl-CoA synthetase, SCS, but maintaining a similar catalytic site, structural consequences of the domain shuffling in ACD, overview