| Accession | TIGR02717 |
| Name | AcCoA-syn-alpha |
| Function | acetyl coenzyme A synthetase (ADP forming), alpha domain |
| Gene Symbol | acs |
| Trusted Cutoff | 567.15 |
| Domain Trusted Cutoff | 567.15 |
| Noise Cutoff | 463.00 |
| Domain Noise Cutoff | 463.00 |
| Isology Type | equivalog_domain |
| EC Number | 6.2.1.13 |
| HMM Length | 447 |
| Gene Ontology Term | GO:0003985: acetyl-CoA C-acetyltransferase activity molecular_function |
| | GO:0046356: acetyl-CoA catabolic process biological_process |
| Author | Selengut J |
| Entry Date | Dec 2 2005 3:03PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Although technically reversible, it is believed that this group of ADP-dependent acetyl-CoA synthetases (ACS) act in the direction of acetate and ATP production in the organisms in which it has been characterized [1,2,3]. In most species this protein exists as a fused alpha-beta domain polypeptide. In Pyrococcus and related species, however the domains exist as separate polypeptides. This model represents the alpha (N-terminal) domain. In Pyrococcus and related species there appears to have been the development of a paralogous family such that four other proteins are close relatives. In reference [1], one of these (along with its beta-domain partner) was characterized as ACS-II showing specificity for phenylacetyl-CoA. This model has been constructed to exclude these non-ACS-I paralogs. This may result in new, authentic ACS-I sequences falling below the trusted cutoff. |
| References | RN [1]
RM 8830684
RT Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus.
RA Mai X, Adams MW
RL J Bacteriol. 1996 Oct;178(20):5897-903
RN [2]
RM 10375639
RT Cloning and sequencing of an acetyl-CoA synthetase (ADP-forming) gene from the amitochondriate protist, Giardia lamblia.
RA Sanchez LB, Morrison HG, Sogin ML, Muller M
RL Gene. 1999 Jun 11;233(1-2):225-31
RN [3]
RM 11069669
RT Early lateral transfer of genes encoding malic enzyme, acetyl-CoA synthetase and alcohol dehydrogenases from anaerobic prokaryotes to Entamoeba histolytica.
RA Field J, Rosenthal B, Samuelson J
RL Mol Microbiol. 2000 Nov;38(3):446-55 |
